V6 Symposium: The 6th International Vanadium Symposium" July 17 To 19th, 2008 Lisbon, Portugal

6 th
International
Vanadium Symposium
Book of Abstracts
Book of Abstracts
The Chemistry and Biological

Chemistry of Vanadium Lisbon2008
17-19 July Portugal
Coordination by: João da Costa Pessoa
Cover designed by: Isabel Correia and Hugo Tomás
Organized and compiled by: Isabel Tomaz, Gisela Gonçalves and Sofia Gama
The assistance of Pedro Adão and Amit Tyagi is acknowledged.
This book was prepared from text supplied by the authors. No additional English
corrections of the included articles were made.
General Information G1
Organizing Committee
João Costa Pessoa (Chair), IST-TU Lisbon, Portugal

Hitoshi Michibata (Co-chair), Hiroshima University, Japan
Kan Kanamori (Co-chair), Toyama University, Japan
Isabel Correia (secretariat), CQE/IST-TU Lisbon, Portugal
Ana Isabel Tomaz (secretariat), CCMM/FC-UL, Portugal
Gisela Gonçalves (secretariat), IST-TU Lisbon, Portugal
Pedro Adão (secretariat), IST-TU Lisbon, Portugal
Sofia Gama (secretariat), ITN, Sacavém, Portugal
Amit Tyagi (secretariat), CQE/IST-TU Lisbon, Portugal
National Organizing Committee
João Costa Pessoa, IST-TU Lisbon, Portugal

Armando Pombeiro, IST-TU Lisbon, Portugal
J.J.R. Fraústo da Silva, IST-TU Lisbon, Portugal
Carlos C. F. Geraldes, CNC, Coimbra University, Portugal
M. Margarida C. A. Castro, CNC, Coimbra University, Portugal
Manuel Aureliano Alves, FCT - Algarve University, Portugal
Isabel Cavaco, FCT - Algarve University, Portugal
Isabel Correia, CQE/IST-TU Lisbon, Portugal
Ana Isabel Tomaz, CCMM/FC-UL, Portugal
Gisela Gonçalves (secretariat), IST-TU Lisbon, Portugal
Pedro Adão, IST-TU Lisbon, Portugal
Sofia Gama, ITN, Sacavém, Portugal
Amit Tyagi, CQE/IST-TU Lisbon, Portugal
International Advisory Board
Valeria Conte, Rome, Italy

João Costa Pessoa, Lisbon, Portugal
Debbie C. Crans, Forth Collins, USA
Toshikazu Hirao, Osaka, Japan
Kan Kanamori, Toyama, Japan
Tamas Kiss, Szeged, Hungary
Kenneth Kustin, San Diego, USA
Hitoshi Michibata, Higashi-Hiroshima, Japan
Lage Pettersson, Umeå, Sweden
Dieter Rehder, Hamburg, Germany
Alan S. Tracey, British Columbia, Canada
V6 Symposium ∷ Lisbon 2008

G2 General information
Acknowledgements
We would like to thank the following organizations for making this event possible.

The Calouste Gulbenkian Foundation gardens
Entrance
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The V6 Symposium Venue at Calouste Gulbenkian Foundation

V6 Symposium Program

Scientific Program – Oral Sessions

Thursday, 17th July
9:10 - Introductory Remarks

9 :30 - O1 - Conte, V. (Italy) – “V-catalysed, MW assisted, oxidations with H2O2”
9.50 - O2 - Chen, C.T. (Taiwan) – ”Directed Evolution of C4-Symmetric Metal Vanadate-centered
Quadruplexes: Synergistic Metal-specific Ion Transport and Asymmetric Catalysis”
10:10 - O3 - Correia, I. (Portugal) – “Vanadium-salen and salan complexes as catalysts for
oxidation reactions”
10:30 - O4 - Rosenthal, E. (Germany) – “From Vanadium(V) to Vanadium(IV) – and backwards?”
10:50 - O5 - Sasai, H. (Japan) – “Chiral dinuclear vanadium(V) catalyst for dual activation of
2-naphthols in oxidative couplings”
11:10 Coffee Break
11:40 - O6 - Lorber, C. France) – “[ONNO]-type Amine Bis(phenolate)-Based Vanadium Catalysts

for Ethylene Homo- and Co-polymerization”
12:00 - O7 - Hartung, J. (Germany) – “On the Reactivity of Bromoperoxidase I (Ascophyllum
nodosum) in Buffered Organic Media – Formation of Carbon Bromine Bonds”
12:20 - O8 - Maurya, M. (India) – “ Synthesis, characterisation, reactivity and catalytic potential of
oxovanadium(IV), oxovanadium(V) and dioxovandium(V) complexes of monobasic
tridentate ligand derived from pyridoxal and 2 aminoethylbenzimidazole”
12:40 - O9 – Rangel, M. C. (Portugal) – “Insulin enhancing complexes derived from 3-hydroxy-
4-pyridinones”
13:00 Lunch
14.30 - O10 -Pecoraro, V. (USA) – “Computationally Assisted Design of Asymmetric Sulfoxidation

Catalysts based on Functional Models for Vanadium Dependent Haloperoxidases”
14:50 - O11 - Pettersson, L. (Sweden) – “Aqueous Vanadium(V) Speciation - The Umeå
Perspective”
15:10 - O12 - Hashimoto, M. (Japan) – “Simple peroxovanadate-amino acid complexes”
15:30 - O13 - Tomaz, I. (Portugal) – “The Vanadium-MHCPE system: an evaluation towards
bioavailability”
15:50 - O14 - Kiss, T. (Hungary) & IUPAC Presentation – “Comparative studies on the
biospeciation of antidiabetic vanadium and zinc compounds”
16:20 Poster Session
16:50 Poster Session / Coffee Break
17:50 - O15 - Gambino, D. (Uruguay) – “Vanadium complexes with polipyridyl ligands as

potential antiprotozoa agents”
18:10 - O16 - Kanamori, K. (Japan) – “Oscillating reaction of a vanadium compound. II
What triggers the chaotic reaction?”
18:30 - O17 - Salifoglou, A. (Greece) – “New ternary and binary species in the structural
speciation of insulin mimetic vanadium(V) in the presence of the physiological citrate and
hydrogen peroxide”
18:50 - O18 – Schwendt, P. (Slovak Republic) – “Stereospecific formation of dinuclear vanadium(V)
19:10 tartrato complexes”

Friday, 18th July
9:10 - O19 - Castro, M. (Portugal) – “Chemical and Biochemical Studies of a 5-hydroxy-

4-pyrimidinone V(V) Complex”
9:30 - O20 - Crans, D. C. (USA) – “How Lipids Interfaces Affect the Coordination Chemistry of
Vanadium Compounds”
9 :50 - O21 - Sakurai, H. (Japan) – “Development of Anti-diabetic Vanadium Complexes and
Analysis of their Molecular Mechanism”
10:10 - O22 - Willsky, G. (USA) – “Chemical and Biological Variability in Anti-diabetic and
Anti-apoptotic Effects of Vanadium Complexes”
10:30 - O23 - Orvig, C. (Canada) – “Coordination of oxovanadium(IV) to human serum apo-
transferrin: a calorimetric comparison study”
10:50 - O24 - Thompson, K. (Canada) – “VO(IV) complexes of maltol and ethylmaltol for oral
treatment of type 2 diabetes mellitus: lessons from speciation studies and phase I and II
clinical trials”
11:10 Coffee Break
11:40 - O25 - Katoh, A. (Japan) – ”Evaluation of Insulin-Mimetic Activities of Vanadyl Complexes

from the Viewpoint of Heterocyclic Bidentate Ligands”
12:00 - O26 - Ding, W. (China) – “The insulin-mimetic properties of vanadium with its effects on
the gene expression profiling of the insulin signaling pathway in diabetic mellitus”
12:20 - O27 - Zorzano, A. (Spain) – “Arylalkylamine vanadium salts as a new generation of
antidiabetic compounds.”
12:40 - O28 - Makinen, M.W. (USA) – “Can Vanadyl Chelates Help To Detect Cancer?”
13:00 Lunch
14.30 - O29 - Zonta, C. (Italy) – “Lewis Bases in Vanadium(V) Catalyzed Oxygen Transfer
Catalysis”
14:50 - O30 - Garriba, E. (Italy) – “Octahedral-square pyramidal equilibrium in bis-chelated VIVO
species: spectroscopic and DFT characterization”
15:10 - O31 - Rehder, D. (Germany) – “Vanadium in Life”
15:30 - O32 - Etcheverry, S. (Argentina) – “Biological Effects and Cytotoxicity of a complex of
Vanadium(V) with salicylaldehyde semicarbazone in osteoblasts in cult”
15:50 - O33A – Majlesi, K. (Iran) – “Interaction of Dioxovanadium(V) with Iminodiacetic Acid and
Phenylalanine Using SIT”
O33B – Rezaienejad, S. (Iran) – “Complexation of Dioxovanadium(V) with Nitrilotriacetic
Acid in Different Sodium Perchlorate Aqueous Solutions Using SIT”
16:50 Poster Session / Coffee Break
17:50 - O34 - Aureliano, M. (Portugal) – “Recent advances in decameric vanadate biochemistry”

18:10 - O35 - Michibata, H. (Japan) – “A novel function of Vanabin2 and the relationship among
proteins involved in the accumulation and reduction of vanadium by ascidians”
18:30 - O36 - Cohen, M. (USA) – “Vanadium Induces AIH: Implications for the Pulmonary Immune
System”
18:50 - O37 - Cavaco, I. (Portugal) – “DNA cleavage activity of VO(acac)2 and derivatives”
19:10
20.30 Symposium dinner

Saturday, 19th July
9:10 - O38 - Plass, W. (Germany) – “Vanadium haloperoxidases as versatile biological matrix:

Mechanistic aspects towards cofactor and substrate specificity”
9 :30 - O39 - Almeida, M. (Portugal) – “Vanadium haloperoxidases – a biocatalyst for iodination
reactions”
9.50 - O40 - Wever, R. (Netherlands) – “Directed evolution of vanadium chloroperoxidase: a
mutant with high bactericidal activity at alkaline pH”
10:10 - O41 - Littlechild, J. (UK) – “Vanadium containing Bromoperoxidase – Insights into the
enzymatic mechanism using X-ray crystallography”
10:30 - O42 -Butler, A. (USA) – No title available
10:50 - O46 - Ghermani, N. E. (France) – “Structural and Electrostatic properties of a
decavanadate-cytosine co-crystallized complex”
11:10 Coffee Break
11:40 - O44 - Avecilla, F. (Spain) – “Influence of polydentate ligands in the structure of dinuclear
V(V) compounds”
12:00 - O45 - Hayashi, Y. (Japan) – “Hexavanadate core and discovery of double stranded
octadecavanadate”
12:20 - O43 - Spasojevic, A. (France) – “Crystallographic statistical studies of the decavanadate
anion: toward a prediction of the non-covalent interactions”
12:40 - O47 - Antunes, O. (Brasil) – “A New Oxo-Vanadium complex employing an imidazole rich
tripodal ligand”
13:00 Lunch
14.30 - O48 - Kabanos, T. (Greece) – “Oxovanadium(V) compounds with bis(hydroxyamino)-

triazines: Synthesis, structural, and physical studies ”
14:50 - O49 - Honzicek, J. (Czech Republic) – ”Ring-substituted vanadocene(IV) and
molybdenocene(IV) complexes”
15:10 - O50 - Pombeiro, A. (Portugal) – “Vanadium Catalysts for the Functionalization of Alkanes
under Mild Conditions”
15:30 - O51 - Baran, E. (Argentina) – “Oxovanadium (IV) complexes of carbohydrates. Some
recent advances”
15:50 - Vanadium Award combined Lecture
O52 – Hirao, T. – “Vanadium-Catalyzed Oxidative Bromination Reaction under Molecular
Oxygen”
16:40 Coffee break
17:10 - O53 - Krzystek, J. (USA) –” Electron Paramagnetic Resonance of Vanadium(III)

Coordination Complexes”
17:30 - O54 - Keramidas, A. (Greece) – “Structure and spectroscopic properties of new VIV/V
semiquinone and hydroquinone complexes”
17:50 - O55 - McLauchlan, C.C. (USA) – “ Vanadium Coordination Complexes with the
[CpP(OEt,OEt)Co]- ligand : Towards Catalysis “
18:10 - O56 - Carn, F. (France) – “Bio-inspired Synthesis of Bionanocomposites Elastomers via a
Complex Coacervation Process Between Gelatin and Decavanadates”
18:30 - 18.45: Closing Remarks

Scientific Program – Poster Titles
P1 - Daniel Geibig DFT Model Studies of Vanadium Chloroperoxidase: Dissociative or Associative

Enzymatic Mechanism and its Dependency on the Degree of Protonation.
P2 - Tamás Jakusch – “Anion “complexes” of diperoxo-vanadate Model compounds for

haloperoxidase enzyme?”
P3 - Manuel Aureliano – “Decameric vanadate reduction by physiological concentrations of

glutathione in mitochondrial assay conditions”
P4 - Shogo Kamiya – “Template synthesis of a spherical polyoxovanadate(V) by oxidative coupling

reaction”
P5 - Pedro Adão – “Asymmetric oxidation of thioanisole catalysed by reduced Schiff base

oxovanadium(IV) complexes”
P6 - Amit Kumar – “Oxidation of p-chlorotoluene and cyclohexene catalysed by polymer-

anchored oxovanadium(IV) and copper(II) complexes of amino acid derived tridentate
ligands”
P7 - Christian Lorber – “Organometallic chemistry of vanadium with B(C6F5)3”
P8 - Silvia Lovat – “Vanadium(V) complexes as oxidation catalysts”
P9 - Ana M. Martins – “Vanadium diamine bisphenolate complexes: Synthesis, structures and

catalytic activity in sulfoxidations”
P10 - Mannar R. Maurya – “Polystyrene bound dioxovanadium(V) complex of histamine derived

ligand for the oxidation of methyl phenyl sulfide, diphenyl sulfide and benzoin”
P11 - Grzegorz Romanowski – “Dioxovanadium(V) Schiff base complexes of R(-)-1,2-

diaminopropane and o-hydroxycarbonyl compounds. Synthesis, characterization, catalytic
properties and structure”
P12 - Grzegorz Romanowski – “Chiral dioxovanadium(V) complexes of Schiff bases derived from
1,2-diphenyl-1,2-diaminoethane and aromatic o-hydroxyaldehydes. Synthesis,
characterization, catalytic properties and structure”
P13 - Valeria Conte – “V-catalysed oxidations with H2O2”
P14 - Valeria Conte – “On the nature of V(V) species in hydrophilic ionic liquids: a spectroscopic
approach”
P15 - Fernando Avecilla – “Characterization in the solid state of chiral salen and salan ligands and
their vanadium(V) compounds”
P16 - Pabitra Baran Chatterjee – “Intramolecular electron transfer in the solid phase: presenting a
unique example of single-crystal-to-single-crystal transformation from a binuclear
vanadium(V)-alcoholate to an oligomeric vanadium(IV)-aldehydic compound”
P17 - Debbie C. Crans – “Electron transfer reactions of an amavadin-like complex”
P18 - Chryssoula Drouza – “Interaction of Hydroquinonate ligands with VV and MoVI”
P19 - Éva Anna Enyedy –“New insight into the lipo-hydrophilic characterisation of a series of
antidiabetic VO(IV) and Zn(II) complexes and their carrier ligands”
P20 - Takeshi Higuchi –“ Syntheses and characterisation of novel [VO(O2)2L](L=ligand) type

complexes”

P21 - Licínia L.G. Justino – “Density functional theory study of structure and NMR chemical shifts of
oxoperoxo vanadium(V) complexes of L-lactic acid”
P22 - Licínia L.G. Justino – “Density functional theory study of the oxoperoxo vanadium(V)
complexes of glycolic acid. structural correlations with NMR chemical shifts”
P23 - Tatsuya Ueki – “Protein-protein interactions among vanadium-binding proteins and related
proteins in a vanadium-rich ascidian”
P24 - Jessica Nilsson – “Synthesis of new oxo-vanadium(IV) coordination compounds and

evaluation of their insulin mimetic activity”
P25 - Gloria Omoruyi –“ The analysis and determination of vanadium IV in wastes collected from
mining ores in Nigeria”
P26 - Mirta Rubčić – “Vanadium induced cyclization of thiosemicarbazone: formation of

heptanuclear mixed valence V(IV)/V(V) complex”
P27 - Athanasios Salifoglou – “A new vanadium(V)-peroxo species in the presence of physiological

citrate. The missing link in the structural speciation of the V(V)-peroxo-citrate system”
P28 - Telma F.S. Silva – “New C-functionalized tris(pyrazolyl)methanes and their vanadium
complexes”
P29 - Michal Sivák – “Synthesis, molecular and supramolecular structures of oxo compounds
formed by biologically active central atom, heteroligand/s and counterions: vanadium(V),
pyridine or pyrazine carboxylates and amides”
P30 - Marios Stylianou – “Bi- and Hexanuclear Vanadium (IV) complexes of a p-hydroquinone-
based ligand: synthesis and structural characterization”
P31 - Karim Zare – “The effect of ionic strength on the stability constant of vanadium(IV) complex
with methionine”
P32 - Gisela Gonçalves – “Interaction of a pyrimidinone-V(IV) complex with human serum

transferrin”
P33 - Daniele Sanna – “VIVO complexes with bis(pyridyl) derivatives”
P34 - Daniele Sanna – “Interaction of insulin-enhancing vanadium compounds with transferrin and
low molecular mass bioligands”
P35 - Eugenio Garribba – “The effects of the trigonal bipyramidal distortion on the spectroscopic
and electrochemical properties of VIVO bis-chelated species”
P36 - Susana B. Etcheverry – “VO(oda): a vanadyl(IV) complex with an OOO-donor group. Bioactivity
on human colon adenocarcinoma Caco-2 cell line”
P37 - Dinorah Gambino – “Modifying antiprotozoa activity of organic compounds through

complexation with vanadium”
P38 - Maria João Pereira – “Diabetes and vanadium: levels of vanadium in blood samples”
P39 - Allison Ross – “Oxovanadium(IV) macrocycles: potential antivirals against HIV”
P40 - Jaromír Vinklárek – “Vanadocene complexes of a-amino acids: synthesis, structure and
cytostatic activity”
P41 - Gail R. Willsky – “Biological variability in the anti-apoptotic effects of vanadium”
P42 - Sarah Angus-Dunne – “Fenton chemistry revisited: vanadate’s role in the study of
antioxidants”

P43 - Sarah Angus-Dunne – “Hydroxylamino-vanadate derivatives as protein tyrosine phosphatase

inhibitors”
P44 - Rosa F. Brissos – “Vanadium interactions with the calcium pump ATPase: an overview”
P45 - Mirjana Colovic – “Decavanadate effect on rat synaptic plasma membrane Na+/K+-ATPase
activity”
P46 - Gil Fraqueza – “Differential interaction of Sarcoplasmic Reticulum Calcium ATPase with Mo, V
and W Oxometalates”
P47 - Norifumi Kawakami. – “Vanabin2 extracted from ascidian vanadocyte is a novel vanadium
reductase”
P48 - Danijela Krstica – “Inhibition of rat synaptic plasma membrane Ca2+-ATPase activity by
decavanadate”
P49 - Ines Lippold – “Modeling supramolecular interactions of vanadium species”
P50 - Craig C. McLauchlan – “Vanadium imidazolylcarboxylate complexes: synthesis,

characterization, and phosphatase inhibition”
P51 - Ana M. Pereira - “Functional and structural interactions of three vanadium coordination
complexes with the Sarcoplasmic Reticulum Calcium Pump”
P52 - Susana Ramos – “Binding of vanadium (IV) and (V) to actin: effects on function and structure”

Congratulations
Toshikazu Hirao
on receiving
the
3rd Vanadis Award!

Oral
Lectures

Oral lectures

Oral lectures O1
V-catalysed, MW assisted, oxidations with H2O2
V. Contea, F. Fabbianesia, B. Florisa , P. Gallonia, D. Sordia, I. Arendsb,

M. Bonchioc, S. Berardic, D. Rehderd
a
Dip. Scienze e Tecnologie Chim., Univ. Roma Tor Vergata, via Ricerca Scientifica, 00133, Roma IT
b
Lab. of Biocatalysis and Organic Chemistry, Delft University of Technology, Delft, NL.
c
ITM-CNR & Università di Padova, Dip. Scienze Chimiche, via Marzolo 1, 35131, Padova, IT
d
Inst. Inorganic and Applied Chem., Hamburg University, Martin-Luther-King-Platz 6 D-20146 Hamburg, D
e-mail: valeria.conte@uniroma2.it
Vanadium catalysis in oxidation carried out with peroxides is very well known and studied in
several research groups.[1] Several different functional groups can be oxidized with good yields
and selectivities. More recent is, however, the search for more efficient and sustainable
procedure which employs hydrogen peroxide as oxidant. In this respect also the search for more
environment friendly solvents is of primary interest for fundamental research.
In the last years very interesting results have also been obtained in applying MW activation in
metal catalysed
reactions carried out V(V) Catalyst, H2O2
"Sub" "Sub-O"
in ionic liquids. MW- Solvent, TOC
induced dielectric Sub = alkenes, hydrocarbons, thioethers Solvents: bmimPF6; bmimTf2N
heating is indeed
efficiently used by Catalysts
charged species.[2] O
O O O
In the present work OMe H 3C O
O V O V
O
results obtained the O O V
N
performance of N
N
O N N N N
H H
vanadium based CH3OH
H3 C
N
epoxidation catalysts Cat.1 Cat.2 Cat.3 H
in oxidations of
diverse substrates
O
with hydrogen N + N
O V
peroxide will be O NH O O O
presented. V O O O
O EtSO4-
In particular, N
V O
O
alkenes epoxidation N N
VO(SALen)EtSO4
and thioethers
oxidation will be
discussed. Emphasis
will be given to the Cat.4 Cat.5
results obtained in
reactivity and
N O N
selectivity
V
improvement O + O
observed when
hydrophobic ionic CF3SO3-
liquids and MW VO(3,5-diterzbutylSALOphen)TfO
activation are used.
[1] V. Conte, O. Bortolini, Transition metal Peroxides, Synthesis and role in oxidation reactions. In “The
Chemistry of Peroxides” Vol. 2, Part 1, Zvi Rappoport (Editor), ISBN: 0-470-86274-2, (2006), pag.1053-
1128.
[2] S. Berardi, M. Bonchio, M. Carraro, V. Conte, A. Sartorel, G. Scorrano, J. Org. Chem. 72(23) (2007)
8954-8957.

O2 Oral lectures
Directed evolution of C4-symmetric metal vanadate-centered

quadruplexes: synergistic metal-specific ion transport and asymmetric
catalysis
Ya-Hui Lin and Chien-Tien Chen
Department of Chemistry, National Taiwan Normal University; Taipei, Taiwan

email: chefv043@ntnu.edu.tw
We have developed a series of N-Salicylidene-based L-α-amino acids as chiral auxiliaries for

chiral vanadyl(V) methoxide complex synthesis. These configurationally well-defined complexes
have been examined for kinetic resolution of 2o alcohols. They serve as efficient and highly
enantioselective catalysts for asymmetric aerobic oxidation of α-hydroxy acid,1 phosphonic
acid,2 and ketone derivatives3 at ambient temperature. X-ray crystallographic analysis of an
adduct between N-benzyl-mandelamide and the catalyst allows for probing the origin of the
nearly exclusive asymmetric control in the oxidation process. In the case of the 3,5-di-tert-butyl
and -chloro analogs, pentanuclear C4-symmetric complexes were formed when a potassium salt
was employed. The complexes work synergistically in the asymmetric aerobic oxidations of
various racemic α-hydroxy acid derivatives with excellent selectivity factors.4
1.25 mol%
O O M+
OH 5 mol% OH Ph
Ph O Ph
N O O
catalyst N O O
O O O V
G P G P G P V
O O2/toluene O O OCH3 Cl O O
O O
Ph rt O
Ph Ph Br O
O OH 4
V O OH
H Cl O
G = Ar, hetero-Ar, (R) S Ph S Ph + S Ph
Br
alkenyl, alkynyl, alkyl 46-50% yield 48-50% yield O2, toluene
catalyst O O O
krel: 50 - >100 rt
H2O H2 O
w/M+VO3- w/M'+VO 3-
O O M+
CDCl3 CDCl3
N O O N O O
V V
Cl O OCH3 M = Li, Na, K, Cs M' = Li, Na, Cs Cl O O
H O V
Cl 4
Cl O
K:Cs = 92:8 (8 min)
K:Cs = 95:5 (1h)
An artificial directed evolution process to assemble C4-symmetric, vanadate-centered

quadruplexes, for the first time, from a given chiral vanadyl(V) complex allows for highly
efficient K+- and Ag+-specific transport from aqueous phase containing three other alkali metal
cations into organic solvents, reminiscent of the K+ specific transport exerted by four homochiral
glycine residues of the opening site in KcsA membrane protein.
Acknowledgements: We thank the National Science Council of Taiwan for generous financial support of this
research.
[1] S.-S Weng, M.-W.Shen, J.-Q. Kao, Y. S. Munot, C.-T. Chen, Proc. Natl. Acad. Sci. USA 103 (2006) 3522-
3527.
[2] V. D. Pawar, S.-S. Weng, S. Bettigeri, J.-Q. Kao, C.-T. Chen, J. Am. Chem. Soc. 128 (2006) 6308-6309.
[3] C.-T. Chen, S.-S. Weng, W.-Z. Lee, J. Org. Chem. 72 (2007) 8175-8184.
[4] C.-T. Chen, Y.-H. Lin, submitted to Angew. Chem. Int. Ed. 47 (2008) for publication.

Oral lectures O3
Vanadium-salen and salan complexes as catalysts for oxidation

reactions
Isabel Correia,a Pedro Adão,a Mannar R. Maurya,b Fernando Avecilla,c Maxim

Kuzvetsova and João Costa Pessoaa
[a]
Centro Química Estrutural, Instituto Superior Técnico - TU Lisbon, Av. Rovisco Pais 1049-001, Lisboa,
Portugal [b] Department of chemistry, Indian Institute of Technology Roorkee, Roorkee-247667, India
[c]
Departamento de Química Fundamental, Facultad de Ciencias, Universidade da Coruña,
Zapateira, s/n, 15071, A Coruña, Spain
email: icorreia@ist.utl.pt
The interest in vanadium complexes as catalysts has been promoted by its ability to catalyze
oxidations and oxo transfer reactions.[1] Vanadium complexes containing chiral ligands have
shown the capacity to catalyze enantioselectively the oxidation of prochiral sulfides to sulfoxides
(and sulfones, in some cases) by hydrogen peroxide or organic hydroperoxides. Moreover, it has
been reported that chiral ligands containing a secondary amine group are superior, in terms of
reactivity and enantioselectivity to imino analogues.[2] We report the synthesis and
characterization of chiral salen (salicylideneimine) and salan (salicylideneamine) type ligands
and their vanadium complexes, which are derived from salicylaldehyde or pyridoxal and chiral
diamines (1R,2R-cyclohexanediamine, 1S,2S-cyclohexanediamine and 1S,2S-diphenylethylene
diamine). The complexes are studied by UV-Vis, circular dichroism and EPR spectroscopy, which
provide information on the coordination R2 R2
geometry and conformational chirality of the
chelate rings, both being important factors in O
asymmetric catalysis. NH NH
The complexes were tested as catalyst in the V
oxidation of styrene, cyclohexene and cumene
with H2O2 as oxidant. Different products were
R1 O O R1
obtained and some catalysts showed good (VIVO-salan complex)
performance and selectivity.
Globally the conversions are better with the V-salan complexes than with the V-salen
complexes.
The complexes were also tested as catalysts for the enantioselective oxidation of methyl phenyl
sulphide. Good enantioselective oxidations were achieved and again the results are significantly
better with the V-salan complexes than with the V-salen complexes.
Possible mechanisms of reactions are outlined and several DFT studies are presented to support
the formation of proposed intermediates.
Acknowledgement: The authors gratefully acknowledge the financial support of FEDER, Fundação para a
Ciência e a Tecnologia, POCI 2010 and PPCDT/QUI/55985/2004 and PPCDT/QUI/56946/2004 projects. Prof.
M. R. Maurya acknowledges Fundação Oriente and the Department of Science and Technology, New Delhi
for the financial support received.
[1] L. Canali and D.C.Sherrington, Chem. Soc. Rev.,1999, 28, 85.

[2] J.T.Sun, C.J.Zhu, Z.Y.Dai, M.H.Yang, Y.Pan and H.W.Hu, J. Org. Chem., 2004, 69, 8500.

O4 Oral lectures
From Vanadium(V) to vanadium(IV) – and backwards?
Esther C. E. Rosenthal
Department of Chemistry, Secr. C 2, TU Berlin, Strasse des 17. Juni 135, 10623 Berlin, Germany
email: esther.rosenthal@tu-berlin.de
Recently we synthesised and characterised a series of oxovanadium(V) alkoxides with bidentate

ligands and investigated their catalytic behaviour.1 Alkoxy and aryloxyalkoxide ligands were
chosen due to their ability to stabilise vanadium complexes in high oxidation states by forming
chelate structures with the additional oxygen donor coordinated to the vanadium atom. Anyhow
not all complexes with alkoxyalkoxide ligands are indefinitely stable under inert conditions. They
decompose even in the dark and at low temperatures to the corresponding vanadium(IV)
complexes (Figure 1).
O
Cl
V !
Figure 1. From Vanadium(V) to Vanadium(IV) – and backwards?
Advanced reduction is observed by colour change from the yellow, orange or red vanadium(V)
compounds to the blue-green colour of vanadium(IV) in solution as well as with exposition to
sunlight. Reduction already takes place during the reaction with some of the alkoxy alcohols.
Sometimes the reduction products are stable and isolable, but reaction pathways are unknown
and often side products are observed. In the majority of cases the stable vanadium(IV)
complexes can be synthesised with higher yields by direct methods. Possible decomposition
pathways are the oxidation of the alcohol ligands or the formation of chlorine. No positive proof
of aldehydes as oxidation products could be made, which had been identified as those for simple
alcohols.2 While electrochemical methods are not conclusive on the reduction and oxidation
products formed, reaction of the vanadium(V) complexes with several Lewis bases gave
crystallographically characterised products with the oxidation state depending on the donor
atom. Finally mechanistic investigations showed reversibility for a certain reaction type.
[1] a) E. C. E. Rosenthal, F. Girgsdies, Z. Anorg. Allg. Chem. 628 (2002) 1917, b) E. C. E. Rosenthal, H.
Cui, K. C. H. Lange, S. Dechert, Eur. J. Inorg. Chem. (2004) 4681, c) E. C. E. Rosenthal, H. Cui, J. Koch, P.
Escarpa Gaede, M. Hummert, S. Dechert, Dalton Trans. (2005) 3108 d) E. C. E. Rosenthal, H. Cui, J. Koch
ACS Symp. Ser. 974 (2007) 70.
[2] a) H. Prandtl, L. Hess, Z. Anorg. Chem. 82 (1913) 103, b) H. Funk, W. Weiss, M. Zeising, Z. Anorg. Allg.
Chem. 296 (1958) 36.

Oral lectures O5
Chiral dinuclear Vanadium(V) catalyst

for dual activation of 2-naphthols in oxidative couplings
Hiroaki Sasai, Shinobu Takizawa, Tomomi Katayama
The Institute of Scientific and Industrial Research (ISIR), Osaka University

Mihogaoka, Ibaraki-shi, Osaka 567-0047, Japan, email: sasai@sanken.osaka-u.ac.jp
An efficient enantioselective oxidative coupling of 2-naphthol derivatives based on a concept of

dual activation catalysis is realized. A chiral dinuclear vanadium(IV) complex (Ra,S,S)-11
possessing (S)-tert-leucine moieties at the 3,3’-positions of the
(R)-binaphthyl skeleton was developed, which was found to
S
promote the oxidative coupling of 2-naphthol to afford (S)-BINOL N
O
VO
with 91% ee. To verify the dual activation mechanism, O Ra
O
mononuclear vanadium(IV) complex (S)-2 was also prepared. O VO O
O
Kinetic analysis revealed that the reaction rate of oxidative N
S
coupling of 2-naphthol promoted by (Ra,S,S)-1 is 48.3 times faster
(R a,S,S)- 1
than that of (S)-2. The two vanadium metals in the chiral complex
activate two molecules of 2-naphthol simultaneously in an intramolecular
coupling reaction, achieving a high reaction rate with high enantiocontrol.
Since (Ra,S,S)-1 was found to be readily oxidized to afford a
N
corresponding vanadium(V) species during preparation in air, a new O
V
O O
synthetic procedure using VOCl3 has been developed as shown in Scheme
O
1.2,3 The structure of (Ra,S,S)-3 was determined by X-ray
(S)-2
crystallographic analysis as a NaOH adduct. Corresponding dinuclear
vanadium(V) complex (Ra,S,S)-4, bearing octahydrobinaphthyl skeleton, was also prepared
from 3,3-diformyl-H8-BINOL. To the best of our knowledge, (Ra,S,S)-3 and (Ra,S,S)-4 show
considerably higher catalytic activity than previously reported vanadium complexes for the
oxidative coupling of 2-naphthols. Reaction mechanisms of the oxidative coupling reaction
promoted by either vanadium(IV) or vanadium(V) complexes will be also discussed.
Scheme 1. Preparation of Dinuclear Vanadium(V) Catalysts.
Catalyst (5 mol %) N
OH V
O
air, CH2Cl2 OH HO O O O
OH O OH
O VO
O
N
Cat 1: 76% (91% ee) (30 oC, 24 h)
Cat 3: 100% (90% ee) (0 oC, 72 h) (Ra,S,S)-4
Cat 4: 56% (97% ee) (0 oC, 72 h)
Scheme 2. Representative Results on Oxidative Coupling of 2-Naphthols.
[1] H. Somei, Y. Asano, T. Yoshida, S. Takizawa, H. Yamataka, H. Sasai, Tetrahedron Lett. 45 (2004) 1841-
1844.
[2] S. Takizawa, T. Katayama, H. Somei, Y. Asano, T. Yoshida, C. Kameyama, D. Rajesh, K. Onitsuka, T.
Suzuki, M. Mikami, H. Yamataka, D. Jayaprakash, H. Sasai, Tetrahedron, 64 (2008) 3361-3371.
[3] S. Takizawa, T. Katayama, C. Kameyama, K. Onitsuka, T. Suzuki, T. Yanagida, T. Kawai, H. Sasai,
Chem. Commun. 2008, 1810-1812.

O6 Oral lectures
[ONNO]-type amine bis(phenolate)-based Vanadium catalysts for

ethylene homo- and co-polymerization
Christian Lorber
Laboratoire de Chimie de Coordination du CNRS, 205 route de Narbonne, 31077 Toulouse, France
email: lorber@lcc-toulouse.fr
In the past fifteen years, a tremendous amount of effort has been devoted to the design of new
"non-metallocene" early transition metal complexes because of their importance as α-olefin
polymerization catalysts.[1] Particularly, chelating diamide, dialkoxide, or phenoxyimine ligands
have been extensively studied as rigid supporting environments for titanium and zirconium
complexes. resulting in the emergence of a great deal of novel and useful chemistry, including
the discovery of highly active olefin polymerization precatalysts. Among these new ligands,
chelating dianionic [ONNO]-type amine bis(phenolate) ligands associated to group 4 metal
complexes have proved to give highly active 1-hexene polymerization catalysts, and in some
cases even isospecific living polymerization was possible.[2]
As part of an ongoing study of vanadium chemistry with various supporting ligands, in particular
directed toward vanadium complexes for olefin polymerization, we have recently used ancillary
diamido with sterically demanding protecting groups[3] or imido ligands[4] on vanadium(IV)
complexes as a way to overcome the problem of deactivation by stabilization of the formal
oxidation state of the vanadium center. Following this concept, we wish to describe the
synthesis of a series of vanadium complexes with the ancillary amine bis(phenolate) [ONNO]-
type ligand and their use as ethylene homo- and co-polymerization catalyst.[5]
X
X
V O
O
N
N
R R
+
cocata: EtAlCl2
R R
α-olefin or cycloolefin - Linear Low Density PolyEthylenes and CycloOlefin Copolymers
- High co-monomer incorporation
- Good Molecular Weight Distribution
[1] V. C. Gibson, S. K. Spitzmesser, Chem. Rev. 2003, 103, 283-315.

[2] E. Y. Tshuva, I. Goldberg, M. Kol, J. Am. Chem. Soc. 2000, 122, 10706-10707.
[3] Lorber, C.; Donnadieu, B.; Choukroun, R. Organometallics 2000, 19, 1963-1966.
[4] Lorber, C.; Donnadieu, B.; Choukroun, R. J. Chem. Soc., Dalton Trans. 2000, 4497-4498.
[5] (a) F. Wolff, C. Lorber, R. Choukroun, B. Donnadieu Inorg. Chem. 2003, 42, 7839-7845. (b) F. Wolff, C.
Lorber, R. Choukroun, B. Donnadieu Eur. J. Inorg. Chem. 2004, 2861-2867. (c) C. Lorber, F. Wolff, R.
Choukroun, B. Donnadieu, Eur. J. Inorg. Chem. 2005, 2850-2859.

Oral lectures O7
On the reactivity of Bromoperoxidase I (Ascophyllum nodosum) in

buffered organic media – formation of carbon bromine bonds
Jens Hartung,a Diana Hach,a and Heiko Schulza
a
Fachbereich Chemie, Technische Universität Kaiserslautern,
Erwin-Schrödinger-Strasse 54,D-67663 Kaiserslautern, Germany
email: hartung@chemie.uni-kl.de
Vanadium(V)-dependent bromoperoxidase I was isolated from Ascophyllum nodosum

[VBrPO(AnI)].1,2 The enzyme was applied as catalyst for conducting sustainable brominations of
organic substrates in buffered organic media. In the absence of organic substrates, enzyme
stability gradually increased along the series phosphate (pH 6.2) < Tris (pH 9.0) < MES buffer
(pH 6.2), as documented with the triiodide assay. A decrease of VBrPO(AnI) stability was
furthermore noted by raising the volume percentage of added organic co-solvent. Least
pronounced effects on enzyme activity loss was found for co-solvents 1,4-dioxane and tert-
butanol in up to 50 % (v/v). Suitable conditions, that balanced VBrPO(AnI) lifetime in buffered
organic media, and enzymatic activity for bromide oxidation were applied for converting organic
substrates into bromo-derivatives.3 Pyrroles, for example, afforded bromopyrroles on a larger
scale. Hydrogen peroxide efficiency was essentially quantitative under newly established
conditions. VBrPO activity prevailed for reactions conducted under pH-controlled conditions. The
procedure was applied for selective bromohydrine synthesis from olefins. The target products
were subjected to detailed stereochemical analysis with the aid of a novel chiral phosphorous-
based derivatization reagent.4
Acknowledgements: The authors would like to thank particularly Dr. Hans Vilter for helpful discussions and
Prof. Dieter Rehder for donations of VBrPO(AnI) samples for conducting preliminary experiments as well as
for his interest in this work. We also wish to express our gratitude to Mrs. Yvonne Dumont for technical
assistance and Drs. Philipp Schmidt and Marco Greb for conducting preliminary VBrPO(AnI)-catalyzed
oxidations. Financial support was kindly provided by the Stiftung für Innovation (grant 818) des Landes
Rheinland-Pfalz and by the Deutsche Bundesstifung Umwelt (grant 2007/885).
[1] H. Vilter. Bot. Marina 26 (1983) 331–340.

[2] J. Hartung, O. Brücher, D. Hach, H. Schulz, H. Vilter, G. Ruick. Phytochemistry, submitted.
[3] D. Hach, H. Schulz, Y. Dumont, H. Vilter, J. Hartung. Manuscript in preparation.
[4] M. Amberg, U. Bergsträsser, G. Stapf, J. Hartung. J. Org. Chem. 73 (2008) 3907–3910.

O8 Oral lectures
Synthesis, characterisation, reactivity and catalytic potential of

oxovanadium(IV), oxovanadium(V) and dioxovandium(V) complexes
of monobasic tridentate ligand derived from pyridoxal and
2-aminoethylbenzimidazole
Mannar R. Maurya,a Manisha Bisht,a Amit Kumar,b Fernando Avecillac and

João Costa Pessoab
a
Department of chemistry, Indian Institute of Technology Roorkee, Roorkee-247667, India;b Centro
Química Estrutural, Instituto Superior Técnico - TU Lisbon, Av. Rovisco Pais 1049-001, Lisboa, Portugal;
c
Departamento de Química Fundamental, Facultad de Ciencias, Universidade da Coruña
Zapateira, s/n, 15071, A Coruña, Spain.
e-mail: rkmanfcy@iitr.ernet.in
Interest in the coordination chemistry with particular emphasis on the model character of
vanadium(V) complexes having O and N functionalities stems from the structural
characterization of three vanadate-dependent haloperoxidases (VHPO). Irrespective of their
origin they all have almost identical structural features, with vanadium(V) in a trigonal-
bipyramidal coordination environment.
In order to model structural features of haloperoxidases, [VO(acac)2] was reacted with two ONN
donor ligands, Hpydx-aebmz (I) (Hpydx = pyridoxal and aebmz = 2-aminoethylbenzimidazole)
to give oxovanadium(IV) complex, [VO(acac)(pydx-aebmz)] (1). In this complex, one
acetylacetonato group remained coordinated and the single crystal X-ray study confirms its
octahedral structure. Reaction of Hpydx-aebmz with VOSO4 in refluxing methanol gave
[{VO(pydx-aebmz)}2(SO4)] (2). Complex 1 has been used as precursor to prepare other
vanadium complexes. Thus, 1 in methanol reacts with aqueous 30 % H2O2 to give
oxoperoxovanadium(V) complex, [VO(O2)(pydx-aebmz)] (3), the formation of which has also
been established in solution by titrating methanolic solution of 1 with H2O2 dissolved in
methanol. Reaction of 1 with catechol (H2cat) and benzohydroxamic (H2bha) acid in refluxing
methanol gave octahedral complexes [VO(cat)(pydx-aebmz)] (4) and [VO(bha)(pydx-aebmz)]
(5), respectively. All these complexes have been characterised by various physico-chemical
techniques. Catalytic activities of some of these complexes for the oxidation of organic
substrates are also explored.
Acknowledgement: Prof. M. R. Maurya acknowledges Fundação Oriente for the financial support received.
Department of Science and Technology, New Delhi is also gratefully acknowledged for financial support of
the work, and the authors also thank FEDER, Fundação para a Ciência e a Tecnologia, POCI 2010
(PPCDT/QUI/55985/2004 and PPCDT/QUI/56946/2004 programs).

Oral lectures O9
Insulin enhancing complexes derived from 3-hydroxy-4-pyridinones
Maria Rangel,a Mª João Amorim,b Ana Nunes,b Andreia Leite,b Mariana Andrade,b Ana
Silva,b Paula Gameiro,b Carla Silva,c
a
REQUIMTE, Instituto de Ciências Biomédicas de Abel Salazar, Universidade do Porto, Largo Abel Salazar, 2,
4099-003 Porto, Portugal, email: mcrangel@fc.up.pt;
b
REQUIMTE, Departamento de Química, Faculdade de Ciências, Universidade do Porto, Rua do Campo
Alegre, 4169-007 Porto, Portugal
c
REQUIMTE, Faculdade de Ciências da Saúde, Universidade Fernando Pessoa, Rua Carlos da Maia, 4200-150
Porto, Portugal
Metal based drugs are currently in use for both therapeutic and diagnosis purposes. The
identification of abnormal levels of metal ions in the body as a cause of several diseases has
promoted the design of chelators and of metal ion containing molecules with suitable properties
for their use as therapeutic agents.
Since a few years, we have been working on the design of new chelators of the 3-hydroxy-
4-pyridinone family and their complexes with M(II) and M(III) metal ions1. Pyridinone
molecules, apart from its physico-chemical properties, which favour its further use as
therapeutic agents, are synthetically versatile allowing the preparation of polidentate and multi-
functionalized ligands which exhibit strong chelating properties. The work developed on
compounds with potential insulin-enhancing activity will be discussed from the chemical and
biological point of view.
00000
00
00000
000
Acknowledgements: I am most grateful to all colleagues and collaborators named in the references above
for their invaluable contributions to the research into this field. Financial support from FCT, contract
POCTI/QUI/35368/2000, POCI/QUI/56214/2004, PPCDT/QUI/56949/2004 is gratefully thanked.
[1] J. Burgess, B. de Castro, C. Oliveira , M. Rangel and W. Schlindwein, Polyhedron, 1997, 16, 789.;
M.M.C.A. Castro, C.F.G.C. Geraldes, P. Gameiro, E. Pereira, B. Castro and M. Rangel, J. Inorg. Biochem.,
2000, 80, 177; M. Rangel, A. Tamura, C. Fukushima, H. Sakurai, J. Biol. Inorg. Chem., 2001, 6(2), 128.; W.
Schlindwein, E. Waltham, J. Burgess, N. Binsted, A. Nunes, A. Leite and M. Rangel, Dalton Trans., 2006,
1313.

O10 Oral lectures
Computationally assisted design of asymmetric sulfoxidation catalysts

based on functional models for vanadium dependent Haloperoxidases
Curtis J. Schneider†, Giuseppe Zampella, ‡ Luca De Gioia, ‡ and Vincent L. Pecoraro†,§,
†
Department of Chemistry, University of Michigan, Ann Arbor, MI 48109
‡
Department of Biotechnology and Biosciences, University of Milano-Bicocca, Milano, Italy
§
Biophysics Research Division, University of Michigan, Ann Arbor, MI 48109,
Vanadium dependent haloperoxidases are a novel class of vanadium dependent enzymes that
catalyze the two electron oxidation of halides and the asymmetric oxidation of thioethers. Our
group has had a long standing interest in understanding the mechanism of oxidation for VHPOs
through the use of vanadium coordination complexes. We have established that
K[VO(O2)Hheida] is an effective functional model for bromide, iodide, and thioether oxidation.
Using this well defined model complex as a starting point, we have employed modern
computational methods to understand the factors controlling the stereoselectivity for the
oxidation of the synthetically useful and pharmaceutically relevant pro-chiral thioethers to chiral
sulfoxides. This information has assisted in the design of an asymmetric oxidation catalyst and
provided critical insight into the reactivity of this new chiral catalyst. The marriage of modern
computational methods and experimental techniques has developed a catalytic system that is
capable of stereoselective oxidation of thioethers and enhanced the understanding of the factors
controlling the reactivity of vanadium-based catalytic oxidations.
Acknowledgements: We thank the Luso-American Development Foundation for financial support.

Oral lectures O11
Aqueous Vanadium(V) speciation - the Umeå perspective
Lage Pettersson,a Ingegärd Andersson,a András Gorzsásb
a
Department of Chemistry, Umeå University, SE – 901 87 Umeå, Sweden,
email: lage.pettersson@chem.umu.se
b
Department of Forest Genetics and Plant Physiology, Umeå Plant Science Centre,
Swedish Agricultural University, SE – 901 83 Umeå, Sweden
Before studying the speciation in any aqueous vanadium(V) system, the hydrolysis of
pentavalent vanadium must be accurately known at a specific ionic medium and temperature.
The Umeå group was the first to report the complete speciation in one and the same ionic
medium (0.600 M Na(Cl)).1 Vanadates and peroxovanadates have shown insulin enhancing
properties. To elucidate their effects, it is vital to know the complete speciation in relevant
systems. Detailed and thorough potentiometric (glass electrode) and 51V NMR (Bruker AMX-500
MHz) spectroscopic studies have been performed of H+–H2VO4––L and H+–H2VO4––H2O2–L
systems at 25 °C in 0.150 M Na(Cl), a medium representing human blood. When studying the
ligand(L) systems, the complete speciation in the subsystems H+–H2VO4– and H+–H2VO4––
H2O2must be known under the same experimental conditions.2 The computer program LAKE,3
designed to simultaneously treat multimethod data, has been used to establish the entire
speciation.
The ligands we have studied so far include imidazole,2 alanylhistidine,4 alanylserine,5 lactate,6
picolinate,7 citrate,8 phosphate,9 maltol,10,11 and uridine.11 Moreover, studies on the ligands N-
hydroxyimino-2,2'-dipropionate (Amavadine ligand) and carbonate are ongoing.
The talk will focus on trends in the complexing ability of different ligands to vanadate and
peroxovanadate. A common feature is that isomeric species are formed in most systems. When
adding hydrogen peroxide, peroxovanadate species are in general formed from already existing
vanadate-ligand complexes. In the case of diperoxovanadate complexes, the following donor
atoms are preferred: aromatic N only > both aliphatic N and O > exclusively O.12 Equilibrium
conditions will be illustrated by distribution diagrams. Models of physiological conditions will also
be shown.
Acknowledgements: The authors would like to thank the Swedish Research Council and European Union
COST projects for financial support.
[1] L. Pettersson, B. Hedman, I. Andersson, N. Ingri, Chem. Scripta 22 (1983) 254-264.

[2] I. Andersson, S. Angus-Dunne, O. Howarth, L. Pettersson, J. Inorg. Biochem. 80 (2000) 51-58.
[3] N. Ingri, I. Andersson, L. Pettersson, A. Yagasaki, L. Andersson, K. Holmström, Acta Chem. Scand. 50
(1996) 717-734.
[4] H. Schmidt, I. Andersson, D. Rehder, L. Pettersson, Chem. Eur. J. 7 (2001) 251-257.
[5] A. Gorzsás, I. Andersson, H. Schmidt, D. Rehder, L. Pettersson, Dalton Trans. (2003) 1161-1167.
[6] A. Gorzsás, I. Andersson, L. Pettersson, Dalton Trans. (2003) 2503-2511.
[7] I. Andersson, A. Gorzsás, L. Pettersson, Dalton Trans. (2004) 421-428.
[8] A. Gorzsás, K. Getty, I. Andersson, L. Pettersson, Dalton Trans. (2004) 2873-2882.
[9] I. Andersson, A. Gorzsás, C. Kerezsi, I. Tóth, L. Pettersson, Dalton Trans. (2005) 3658-3666.
[10] K. Elvingson, A. González Baró, L. Pettersson, Inorg. Chem. 35 (1996) 3388-3393.
[11] A. González Baró, I. Andersson, L. Pettersson, A. Gorzsás, Dalton Trans. (2008) 1095-1102.
[12] L. Pettersson, I. Andersson, A. Gorzsás, Coord. Chem. Rev. 237 (2003) 77-87.

O12 Oral lectures
Simple peroxovanadate-amino acid complexes
Takeshi Higuchia, Masato Hashimotoa and Seichi Okeyaa
a
Department of Material Science and Chemistry, Faculty of Systems Engineering, Wakayama University,
930 Sakaedani, Wakayama 640-8510, Japan
email: mh1043@sys.wakayama-u.ac.jp
Several peroxovanadate or peroxovanadium complexes have been investigated mainly from

biological point of view, e.g. functional centre of haloperoxdase and insulin-mimetic properties.
Many peroxovanadate-organic ligand systems have been analysed and a number of structural
data of the complexes have been reported. However, according to CCDC databese, there have
not been many structural reports on peroxovanadate-amino acid complexes with rather simple
ligands. We therefore tried to examine formation and structural analyses of peroxovanadate
complexes bearing simple amino acids such as glycine, L-alanine, L-(+)-arginine, L-gultaminic
acid, L-histidine and L-cysteine. A nucleobase adenine was also chosen as a ligand.
The formation of complexes in each peroxovanadate-ligand systems were monitored by 51V,
13C and 1H NMR (and 15N for glycinato complexes). Similar tendencies of complex formation
were observed for the amino acids used except for L-gultaminic acid. Among the complexes
detected a diperoxoglycinatovanadate complex, [VO(O2)2(gly)]2-, was isolated as calcium and
strontium salts, and the structure was determined. The crystals of these complex salts were
soluble in water. The solubilities were enhanced by raising ionic strength of the solution up to
3.0 M by NaCl or KCl. The complex formation with adenine ligand has not been confirmed so
far. The overall tendency of complex formation as well as results of characterisations of isolated
complexes and analyses of behaviour of the complexes in solution after re-dissolution will be
discussed.
Zn(II) is known to be effective for the metabolic syndrome. Therefore researches on formation
of Zn-V mixed metal complexes with some amino acids and adenine ligands and on isolation of
the complexes formed are in progress. Formation of complexes were indicated by 51V NMR in
the L-histidine system, but their nature has not been confirmed. The result of this attempt will
also be discussed in the presentation.
Details of some parts of this talk will be presented at the poster entitled ‘Syntheses and
characterisation of novel [VO(O2)2L] (L=ligand) type complexes‘ presented by T. Higuchi.
Acknowledgements: The authors would like to thank Prof. Lage Pettersson, Umeå University, for his kind
discussion and suggestions.

Oral lectures O13
The Vanadium-MHCPE system: an evaluation towards bioavailability
Gisela Gonçalves,a João Costa Pessoa,a Isabel Tomaz,a,b M.Margarida C.A. Castro,c
Carlos F.G.C. Geraldes,c Fernando Avecillad
a
Centro de Química Estrutural, Instituto Superior Técnico – TU Lisbon, Av. Rovísco Pais,
1049-001 Lisbon – Portugal; bCentro de Ciências Moleculares e Materiais, Faculdade de Ciências da
c
Universidade de Lisboa, Campo Grande 1749-016 Lisbon - Portugal; Dpto. de Bioquímica e Centro de RMN,
d
Universidade de Coimbra, 3001-401 Coimbra - Portugal; Dpto. de Química Fundamental, Universidade da
Coruña, A Coruña 15071, Spain. email: isabel.tomaz@ist.utl.pt
The pharmacological potential of vanadium compounds has been demonstrated both in Diabetes
mellitus treatment, and (more recently) in cancer therapy[1]. VIVO complexes of maltol and
ethylmaltol are known for being currently under clinical trials for the oral treatment of type 2
diabetes[2]. Nevertheless the therapeutical use of vanadium-based compounds is still restrained
by the full understanding of the factors that account for the performance of the bio-active
entity. Vanadium absorption and possibly also its transport to the cells can be improved
through coordination by an appropriate ligand thus improving chelating ability, hydrolytic
stability and lipo-hydrophilic balance. However in vivo speciation does occur, and metal-protein
binding in the plasma serum seems to relate to effectiveness, promoting the cellular uptake and
eventualy improving the dose-response ratio[3]. Catecholate derivatives have been widely
studied due to their importance as chelating subunits in several ionophores, and these ligands
are effective candidates for the transport of vanadium into the cells.
We report herein the characterization of vanadium systems with a pyrimidinone-type ligand,
MHCPE (2-methyl-3H-5-hydroxy-6-carboxy-4-pyrimidinone ethyl ester), focusing on several
factors that can interfere with its performance as a drug candidate. As expected, MHCPE is an
efficient ligand for both V(IV) and V(V) in a wide pH range yielding stable and soluble
complexes. Serum protein binding of the complexes is studied by Circular Dichroism (CD) and
EPR. It is proposed that the MHCPE ligand improves the vanadium binding to apo-transferrin
(hTF) as can be concluded from CD spectroscopy (e.g. Fig. 1).
0.5
-1
Δε / M cm
-1
hTF
-0.5 hTF:VO(IV):L (1:0.5:0.5)
hTF:VO(IV):L (1:1:1)
hTF:VO(IV):L (1:1.5:1.5)
hTF:VO(IV):L (1:2:2)
-1
400 500 600 700 800 900 1000
λ / nm
Figure 1. Evolution of CD signal with increasing VIVO-MHCPE concentration

(pH 7.4 in HEPES buffer with 25 mM carbonate, [hTF]total= 750 μM; Δε values per
mole of hTf present).
Acknowledgements: The authors wish to thank the portuguese Fundação para a Ciência e Tecnologia, (for
grants SFRH/BD/32131/2006 and SFRH/BPD/34695/2007, FEDER, POCI 2010 program and project
PPCDT/QUI/56949/2004), the Spanish-Portuguese Bilateral Programme (Joint Action E-56/05) and the
University of La Coruña for financial support.
[1] a) A.Evangelou, Crit.Rev.Oncology/Hematology, 2002, 42, 249-265; b) H.Sakurai, H.Yasui, Y.Adachi,

Exp. Opin. Investig. Drugs, 2003, 12, 1189-1203.
[2] K. H. Thompson, C. Orvig, J. Inorg. Biochem. 100 (2006) 1925-1935.
[3] a) W.H.Ang, P.J.Dyson, Eur. J. Inorg. Chem, 2006, p4003-4018. b) K. Thompson, C. Orvig, 2006, J.
Soc. Chem. Dalton Trans., 761-764; c) C. G. Hartinger, S. Zorbas-Seifried, M. A. Jakupec, B. Kynast, H.
Zorbas, B. K. Keppler, J. Inorg. Biochem., 100 (2006) 891–904.

O14 Oral lectures
Comparative studies on the biospeciation of antidiabetic vanadium

and zinc compounds
Tamás Kiss, Éva Anna Enyedy, Tamás Jakusch
Biocoordination Chemistry Research Group of the Hungarian Academy of Sciences, Department of Inorganic
and Analytical Chemistry, University of Szeged, H-6701 Szeged, Hungary
e-mail: tkiss@chem.u-szeged.hu
Intensive studies have been carried out during the last two decades on the antidiabetic (AnD)
effects of several metal ions among others chromium, vanadium, tungsten and zinc. Vanadium
compounds seem to be the most effective, however their non-essential character is a great
disadvantage and their occurrence and potential accumulation in the organism may produce
strong aversion to their practical application. For this reason, the essential Zn compounds may
receive a more positive acceptance.
Due to the presence of numerous endogenous and exogenous metal ion binders the original
AnD complex may undergo transformations in the biological fluids and tissues and thus the real
biological/physiological activity may be bound to an entirely different chemical entity.
In order to say something about the actual solution state(s) of these metal ions during their
transport in the blood stream we studied their interactions with the relevant low molecular mass
(lmm) ligands, such as citrate, lactate, oxalate, phosphate, histidine and cysteine and high
molecular mass (hmm) protein components, such as albumin, transferrin and α-macroglobulin
of blood serum. In this work we give an overview of the work. Solution speciation and spectral
(EPR, UV-Vis) studies revealed that citrate for vanadium, while histidine and cysteine for zinc(II)
are the most important lmm binders, while transferrin for vanadium and α-macroglobulin and
albumin for zinc(II) are the most important hmm binders of the serum. Ultrafiltration studies
helped to separate and determine the two fractions bound metal content of the serum.
In vitro chromatographic separations made on human plasma confirmed our results obtained by
modeling speciation calculations.
Acknowledgements. This work was carried out in the frame of a COST and various bilateral collaborations
with Portugese, Japanese and Spanish research groups and supported among others by the Hungarian
Science Research Fund (OTKA T49417, NI61786 and PD 050011).

Oral lectures O15
Vanadium complexes with polipyridyl ligands as potential antiprotozoa

agents
Julio Benítez,a Lucía Guggeri,b Gabriel Arrambide,c Isabel Tomaz,c João Costa Pessoa,c Beatriz
Garat,b Dinorah Gambinoa
a
Cátedra de Química Inorgánica, Facultad de Química, UDELAR, Gral. Flores 2124, 11800 Montevideo,
Uruguay; bLaboratorio de Interacciones Moleculares, Facultad de Ciencias, UDELAR, Igua 4225, 11400
Montevideo, Uruguay; cCentro Química Estrutural, IST, Av Rovisco Pais, 1049-001 Lisbon, Portugal
email: dgambino@fq.edu.uy
Parasitic diseases represent a major health problem in Latin America. In particular, Chagas'
disease (American Trypanosomiasis), caused by the protozoan parasite Trypanosoma cruzi, is
the largest parasitic disease burden in the American continent. The morbidity and mortality
associated with this disease are in America more than one order of magnitude higher than those
caused by malaria, schistosomiasis or leishmaniasis. Chagas’ disease affects approximately 20
million people from southern United States to southern Argentina. Despite the progress
achieved in the study of T. cruzi´s biochemistry and physiology, in which several potential new
enzymatic drug targets have been identified, the chemotherapy of this parasitic infection
remains undeveloped. The treatment is based on old and quite unspecific drugs that have
significant activity only in the acute phase of the disease and give rise to severe side effects.
In the search for new therapeutic tools against Chagas' disease metal complexes appear to be a
promising approach. Through the strategy of including in a single molecule an organic bioactive
ligand and a metal with pharmacological potentiality we have previously developed different
bioactive metal complexes and studied their probable mechanism of action.1-4
It has been proposed that the metabolic pathways of kinetoplastid parasites (Leishmania and
Trypanosoma parasites) are similar to those present in tumor cells and those compounds that
efficiently interact with DNA, like intercalators, could show anti-trypanosomal activity. Under
this hypothesis we synthesized, characterized and biologically evaluated vanadyl complexes with
polypyridyl ligands capable of intercalate DNA. Vanadyl mixed-ligand complexes, VO(L1)(L2-2H),
where L1 = dppz (dipyrido[3,2-a: 2’,3’-c]phenazine) or bipy (2,2’-bipyridine) and L2 =
salicylaldehyde semicarbazone derivatives, and VO(dppz)(H2O)2(SO4) were synthesized. The
complexes were characterized by elemental analyses, electrospray ionization mass spectrometry
(ESI-MS), conductimetric and magnetic measurements and infrared (FTIR) and electronic
paramagnetic resonance (EPR) spectroscopies. Complexes were tested on epimastigotes of T.
cruzi, Dm28c strain. Results showed activity dependent on the nature of the ligands. Some of
the compounds showed excellent antiprotozoal activity, similar to that of the reference drugs
Nifurtimox and Benznidazol. Trying to provide insight into the mechanism of anti-trypanosomal
action compounds were tested for their DNA interaction ability on plasmid DNA by using gel
electrophoresis experiments.
Acknowledgements: The authors would like to thank RIDIMEDCHAG CYTED network and Grants of Fonacit
G-2005000827. DG would like to thank Technical University of Lisbon for financial support.
[1] L. Otero, M. Vieites, L. Boiani, A. Denicola, C. Rigol, L. Opazo, C. Olea-Azar, J. D. Maya, A. Morello, R.
Luise Krauth-Siegel, O. E. Piro, E. Castellano, M. González, D. Gambino, H. Cerecetto, J. Med. Chem 49
(2006) 3322-3331.
[2] M. Vieites, L. Otero, D. Santos, D. Gajardo, J. Toloza, R. Figueroa, E. Norambuena, C. Olea-Azar, G.
Aguirre, H. Cerecetto, M. González, A. Morello, J. D. Maya, B. Garat, D. Gambino, J. Inorg. Biochem. 102
(2008) 1033-1043.
[3] C. Urquiola, M. Vieites, G. Aguirre, A. Marín, B. Solano, G. Arrambide, M. L. Lavaggi, M. H. Torre, M.
González, A. Monge, D. Gambino, H. Cerecetto, Bioorg. Med. Chem. 14 (2006) 5503-5509.
[4] M. Vieites, P. Smircich, B. Parajón-Costa, J. Rodríguez, V. Galaz, C. Olea-Azar, L. Otero, G. Aguirre, H.
Cerecetto, M. González, A. Gómez-Barrio, B. Garat, D. Gambino, J. Biol. Inorg. Chem.
doi: 10.1007/s00775-008-0358-7.

O16 Oral lectures
Oscillating reaction of a vanadium compound. II

What triggers the chaotic reaction?
Kan Kanamori,a Keisuke Fujinami,a Yukie Sakai,a Kenji Kubo,b Naoki Wada,b Seiichi
Matsugo,b and Kenneth Kustinc
a
Department of Chemistry, University of Toyama, Gofuku 3190, Toyama 930-8555, Japan,
email: kanamori@sci.u-toyama.ac.jp ; bColledge of Science and Engineering, Kanazawa University, Japan;
c
Brandeis University, Emeritus, USA.
In the last symposium1 we reported that a new type of oscillating reaction occurred when
[V(IV)Cl2(bpy)] or [V(III)Cl3(CH3CN)(bpy)] was added to dichloromethane in a closed system. A
similar reaction also occurred for their phenanthroline (phen) analogues. It has been
demonstrated that the oscillating color change betwen light green and dark orange is due to a
redox reaction between V(IV) and V(V) states and formaldehyde. The latter is a contaminant of
dichloromethane; it works as a reducing agent and dissolved oxygen as an oxidizing agent. The
color change occurs chaotically rather than periodically, and we have examined what triggers
the chaotic reaction.
A small temperature change in the reaction system was found to be one of the factors that acts
as a trigger. Figure 1 shows the change in darkness of the color of the reaction solution and of
the ambient temperature as a function of time. Darkness of the solution was measured by
analyzing the darkness of pixels of captured video frames using a graphic software program
(Canvas 6). As shown in Fig. 1, there is a tendency to develop the dark orange color when the
temperature decreases. However, this phenomenon is not due to thermochromism, because (1)
an average temperature does not relate to the color change, and (2) the color change occurred
even when the temperature change was negligible. This observation may indicate that a
temperature decrease in the solution resulted in an increase of the concentration of dissolved
oxygen, and as a result the oxidation reaction from V(IV) to V(V) was promoted.
Figure 1. Temperature-dependent oscillating pattern for [V(IV)OCl2(bpy)] (0.55 mM in CH2Cl2).
Irradiation of UV light was also found to trigger the chaotic reaction. When UV light was
irradiated on the reaction solution, the dark orange color developed immediately, and the color
of the solution returned to light green when the irradiation was stopped. Irradiation for a long
period resulted in prevention of the reduction of the orange species, indicating a decomposition
of reducing species present in the solution.
[1] K. Kanamori and Y. Shirosaka, “ACS Symposium Series 974, Vanadium: The Versatile Metal”, Eds by
K. Kustin, J. Costa Pessoa, and D. C. Crans, American Chemical Society, 2007, pp. 424-432.

Oral lectures O17
New ternary and binary species in the structural speciation of insulin

mimetic vanadium(V) in the presence of the physiological citrate and
hydrogen peroxide
Athanasios Salifoglou, Catherine Gabriel
Department of Chemical Engineering, Aristotle University of Thessaloniki, 54124 Thessaloniki, Greece

email: salif@auth.gr
Vanadium has in the past years been investigated for its insulin mimetic capacity1. The
underlying premise in this endeavor has been the fundamental chemical reactivity of vanadium
to promote interactions with biotargets key to the uptake and catabolism of glucose. Poised to
comprehend the molecular chemistry of vanadium to promote interactions with low and high
molecular mass substrates, research efforts have been launched in our lab to investigate the
requisite chemistry at the cellular level. To this end, starting reagents containing vanadium in
the two biologically relevant oxidations states V(IV.V) have been employed in reactions
involving the physiological α-hydroxycarboxylic acids (citric and malic) under pH-dependent
conditions.2 Guided by the existing aqueous speciation schemes of the relevant binary systems,
synthetic efforts led to the isolation of new V(IV,V)-citrate compounds [VV2O4(C6HxO7)2]n-
(x=4,5,6; n=6,4,2), and [VIV2O4(C6HxO7)(C6H4O7)]n- (x=4,5; n=4,3) in the solid state.3 Further
reactivity toward the physiological reagent H2O2 led to the synthesis and isolation of ternary
V(V)-peroxo-citrate complexes [VV2O2(O2)2(C6HxO7)2]n- (x=2,4; n=2,6) and their corresponding
malate analogs. The derived materials were characterized by numerous spectroscopic (FT-IR,
UV-Visible, multinuclear solid state and solution NMR), electrochemical (cyclic voltammetric),
and ultimately X-ray crystallographic techniques. The structural characterization of these
species denotes the variable coordination geometries of V(V) and V(IV) interacting with citrate
and malate. Consistent with these is the chemical reactivity (Figure 1) of the aforementioned
systems in acid-base chemical and thermally induced transformations. Collectively, the
physicochemical properties of all investigated systems emphasizes the importance of pH-
dependent chemical reactivity of binary and ternary vanadium systems with low molecular mass
ligands in the structural speciation of vanadium, in biologically relevant fluids, and its potential
involvement in chemistries linking the biologically relevant V(IV,V) oxidation states with insulin
mimesis.
pH ~3.5
Figure 1. Acid-base transformation of pH-structural V(V)-peroxo-citrate structural variants.
Acknowledgements: This work was supported by and by a ‘‘PENED” grant co-financed by the E.U.-European
Social Fund (75%) and the Greek Ministry of Development-GSRT (25%).
[1] a) H. Sakurai, Y. Kojima, Y. Yoshikawa, K. Kawabe, H. Yasui, Coord. Chem. Rev. 226(2002) 187-198.
b) T. Sasagawa, Y. Yoshikawa, K. Kawabe, H. Sakurai, Y. Kojima, J. Inorg. Biochem. 88(2002) 108-
112.c) K. Kanamori, K. Nishida, N. Miyata, K. Okamoto, Y. Miyoshi, A. Tamura, H. Sakurai, J. Inorg.
Biochem. 86(2001) 649-656.
[2] M. Tsaramyrsi, M. Kaliva, T. Giannadaki, C. P. Raptopoulou, V. Tangoulis, A. Terzis, J. Giapintzakis, A.
Salifoglou, Inorg. Chem. 40(2001) 5772.
[3] M. Kaliva, C. P. Raptopoulou, A. Terzis, A. Salifoglou, Inorg. Chem. 43(2004) 2895-2905.

O18 Oral lectures
Stereospecific formation of dinuclear vanadium(V) tartrato complexes
Peter Schwendt,a Michal Sivák,a Jana Gáliková,a Jozef Tatiersky,a Zdirad Žák,b
a
Department of Inorganic Chemistry, Comenius University, Faculty of Natural Sciences, Mlynská dolina, 842
15 Bratislava, Slovak Republic b Department of Inorganic Chemistry, Masaryk University
Faculty of Natural Sciences, Brno, Czech Republic
email: schwendt@fns.uniba.sk
A study of the aqueous H3O+ (OH–) / H2VO4– /2R,3R-tartrate system1 revealed that besides a
series of minor species, two species are dominant in acidic solutions: [V4O8(R,R-tart)2]4– (1)
(tart = C4H2O64–; –524 ppm in 51V NMR spectrum) and dinuclear species formulated as “V2L2” (–
550 ppm). The species 1 was characterized in the solid state by X-ray diffraction of the
tetraethylammonium salt and an interesting tetranuclear structure was found. Using racemic
tartaric acid for the synthesis the compound Na8[V4O8(R,R-tart)2][V4O8(S,S-tart)2] · 24H2O was
isolated and characterized by X-ray diffraction as a typical racemic compound.
We made efforts to characterize also the “V2L2” species. After many attempts we isolated and
structurally characterized the yellow compound (N(CH3)4)2[V2O4(R,R-H2tart)2] · 6H2O (2) (Figure
1). When using racemic tartaric acid for synthesis the red compounds (NR4)2[V2O2(R,R-
tart)(S,S-tart)] (R = N(CH3)4 – 3; R = N(C2H5)4 – 4) with a profoundly different structure of the
anion (Figure 2) were obtained.
O O 2– O 2–
O O O
V O O
R O V
O O
H HO O O
O R S
R R
OH O R S
O O
O O
O V R O V O
O O O O
O H
O
[V2O4(R,R-H2tart)2]2– [V2O2(R,R-tart)(S,S-tart)]2–
yellow red
Figure 1. The structure of the anion in 2. Figure 2. The structure of the anion in 3.
The compounds 2 – 4 crystallized out of water-ethanol media. In the aqueous solution the
reaction (1) took place
2[V2O2(R,R-tart)(S,S-tart)]2– + 4H2O → [V2O4(R,R-H2tart)2]2– + [V2O4(S,S-H2tart)2]2– (1)
as proved by spectroscopic methods (51V NMR, Raman and UV-VIS spectra measured for H2O,
CH3CN and mixed H2O – CH3CN solutions of 2, 3 and 4).
Acknowledgements: The authors would like to thank the Ministry of Education of the Slovak Republic (grant
VEGA 1/4462/07) for the financial support. NMR measurements were performed on the equipment
supported by the Slovak State Programme Project No. 2003SP200280203.
[1] P. Schwendt, A. S. Tracey, J. Tatiersky, J. Gáliková, Z. Žák, Inorg. Chem. 46 (2007) 3971-3983.

Oral lectures O19
Chemical and biochemical studies of a 5-hydroxy-4-pyrimidinone V(V)

complex
M. Margarida Castroa,b, F. Avecillac, I. Tomazd, G. Gonçalvesd, H. Fanecaa,b,

L. Palacioc, M. Maestroc, M.C.P. Limaa,b, C.F.G.C. Geraldesa,b and João Costa Pessoad
a b
Dpt. of Biochemistry Center of Neuroscience and Cell Biology; University of Coimbra, 3001-401 Coimbra,
Portugal; email: gcastro@ci.uc.pt
c
Dpt. of Fundamental Chemistry, University of A Coruña, A Coruña, Spain;
d
Center of Structural Chemistry, Instituto Superior Técnico, TU Lisbon, 1049-001, Lisbon, Portugal,
The importance of Vanadium Compounds (VCs) has greatly increased in the last years since
they have shown pharmacological properties, in diabetes and cancer therapy. VCs exhibit anti-
cancer activity1 and their potential use as oral insulin mimetics2 has been demonstrated by in
vivo and ex vivo studies, as well as in clinical trials. At the present stage the use of VCs as
therapeutic agents is limited by the narrow range between beneficial and toxic effects. Thus
V(IV) and V(V) complexes containing adequate ligands have been synthesized searching for
properties to improve their pharmacological action, such as hydrolytic stability, water solubility,
neutral charge and/or lipophilicity, low toxicity and antidiabetic or anticancer activity.3
In this work we report a study of the interaction in aqueous solution of vanadate with a
pyrimidinone ligand, the 2-methyl-3H-5-hydroxy-6-carboxy-4-pyrimidinone ethyl ester
(MHCPE). Potentiometry and 51V NMR spectroscopy were used to identify and structurally
characterize the species formed in solution at different M/L ratios and pH values and the
respective formation constants were determined. The results obtained indicated the formation of
two main species with stoichiometries 1:1, (VVO2)L, and 1:2 (VVO2)L2 and their most probable
binding modes were established according to spectroscopic data.
The solution behaviour of these main V(V) species at physiological pH and in different cell
culture media was also studied, showing some favorable properties concerning solubility and
stability. Their cytotoxic effects were tested in the HeLa tumor cell line and the 3T3-L1 cell line
and were demonstrated to be concentration- and time- dependent, being correlated with VC
cellular uptake.
Acknowledgements: This work was carried out in the frame of a COST D21 Project. The authors thank the
financial support from FEDER and Fundação para a Ciência e Tecnologia (FCT), Portugal, POCI 2010, Project
PPCDT/QUI/56949/2004, the Spanish-Portuguese Bilateral Programme (Acção Integrada E-56/05) and
University of A Coruña.
[1] M.S.Molinuevo, D.A.Barrio, A.M.Cortizo et al., Cancer Chemotherapy and Pharmacol. 53 (2004) 163-
172
[2] H. Sakurai, Y. Kojima, Y. Yoshikawa, K. Kawabe, H. Yasui, Coord. Chem. Rev. 226 (2002) 187-198.
[3] D. C. Crans, J. J. Smee, E. Gaidamauskas, L. Yang, Chem. Rev. 104 (2004) 849-902.

O20 Oral lectures
How lipids interfaces affect the coordination chemistry of vanadium

compounds
Debbie C. Crans
Department of Chemistry, Colorado State University, Fort Collins, Colorado 80523

email: crans@lamar.colostate.edu
As a early transition metal vanadium is small and much of its chemistry is governed by ligand
size and geometry, and this presentation will explore how much a lipid/surface environment can
affect this chemistry. Multiple examples exist of vanadium compounds being able to expand
coordination number and complex with incoming ligands. The increase in coordination number
of the five coordinate triethanolamine complex with vanadate upon addition of an ethanol ligand
generates a six coordinate complex.[1] The four coordinate ethylene glycol complex that forms
upon addition to VOCl3 [2] can expand to a five coordinate species when the alkyl groups are
introduced on the ethylene glycol ligand.[3] The addition of a sixth ligand to the five coordinate
VO(acac)2 [4] and BMOV (bismaltolatooxovanadium(IV)) [5] occurs when dissolved in aqueous
or other polar media. The addition of hydroxylamine derivatives to the dioxodipicolinato
oxovanadium(V) expands the five coordinate vanadium to a seven coordinate species.[6].
Surface interactions are found to affect the properties of simple compounds such as ascorbic
acid, that is much more resistant to reduction in a microemulsion environment [7]. We have
recently been interested in examining the effects of such environments not only on reactivity
but also on the stability and geometry of vanadium coordination compounds.
Acknowledgement. We thank the Luso-American Development Foundation for partial travel funds. We also
thank NSF for funding this research.
[1] D. C. Crans, H. Chen, O. P. Anderson and M. M. Miller, J. Am. Chem. Soc. 115 (1993) 6769-6776.
[2] D. C. Crans, R. A. Felty, O. P. Anderson and M. M. Miller, Inorg. Chem. 32 (1993) 247-248.
[3] D. C. Crans, R. A. Felty and M. M. Miller, J. Am. Chem. Soc. 113 (1991) 265-269.
[4] S. S. Amin, K. Cryer, B. Y. Zhang, S. K. Dutta, S. S. Eaton, O. P. Anderson, S. M. Miller, B. A. Reul, S.
M. Brichard and D. C. Crans, Inorg. Chem. 39 (2000) 406-416.
[5] P. Caravan, L. Gelmini, N. Glover, F. G. Herring, H. L. Li, J. H. McNeill, S. J. Rettig, I. A. Setyawati, E.
Shuter, Y. Sun, A. S. Tracey, V. G. Yuen and C. Orvig, J. Am. Chem. Soc. 117 (1995) 12759-12770.
[6] J. J. Smee, J. A. Epps, G. Teissedre, M. Maes, N. Harding, L. Yang, B. Baruah, S. M. Miller, O. P.
Anderson, G. R. Willsky and D. C. Crans, Inorg. Chem. 46 (2007) 9827-9840.
[7] D. C. Crans, B. Baruah, E. Gaidamauskas, B. G. Lemons, B. B. Lorenz, M. D. Johnson, J. Inorg.
Biochem. 102 (2008) 1334-1347.

Oral lectures O21
Development of anti-diabetic vanadium complexes and

analysis of their molecular mechanism
Hiromu Sakuraia* and Makoto Hiromurab

a*
Faculty of Pharmaceutical Sciences, Suzuka University of Medical Science,
3500-3 Minani-Tamagaki-cho, Suzuka, Mie 513-0816, Japan, E-mail: sakuraih@suzuka-u.ac.jp
b
Metallomics Research Unit, RIKEN 2-1 Hirosawa, Wako, Saitama 351-0198, Japan
e-mail: mhiromura@riken.jp
There has been a dramatic worldwide increase in the prevalence of metabolic syndromes
involving diabetes mellitus (DM) since the 20th century. To overcome the defects of clinically
available pharmaceuticals to treat types 1 and 2 DM, new potent vanadium compounds with +3,
+4 and +5 oxidation states have been proposed by many researchers. Since 1990, our group
has proposed several types of vanadyl (+4, VO2+) complexes with different coordination
environments around vanadium in terms of high anti-diabetic activity, low toxicity, and high
bioavailability, that are supported by metallokinetic analysis using BCM-EPR, in types 1 and 2
model animals.
Based on the study of structure-activity relationship in vanadyl complexes with picolinate and 3-
hydroxy-pyronate as leading compounds, we recently found that vanadyl complexes of 4X-
picolinate (X = electron donating and withdrawing substituent) and allixin (alx) are the most
potent anti-diabetic complexes.
We thus analyzed the molecular mechanism of such complexes with respect to the insulin
signaling pathway in cultured adipocytes. The common mechanism of vanadyl complexes have
been found to involve the induction of the Akt/PKB and IRβ or PTPase activities leading to the
translocation of GLUT4 to the cell membrane. In addition, vanadyl-alx complex regulates the
activation of the FoxO transcription factor, which controls the gene expression of G-6-Pase and
PEPCK.
The obtained results will provide us the development method of novel and more active anti-
diabetic vanadyl complexes.
Acknowledgements: This study was supported by a Grant-in-Aid for Specially Promoted Research from the
Ministry of Education, Culture, Sports, Science and Technology (MEXT) of the Japanese Government to H.S.
H. Sakurai, Expert Opin. Drug Discov. (2007) 2, 873-887.

O22 Oral lectures
Chemical and biological variability in anti-diabetic and

anti-apoptotic effects of vanadium complexes
Gail R. Willsky a, Michael Godzala III a, Paul J. Kostyniak a, Barbara A. Bistram a,

Rebecca Z. Grayson a, Lai-Har Chi a, Martha Clark a, Jason J. Smee b, Debbie C. Crans b
a b
University at Buffalo (SUNY), Buffalo, NY 14214. USA. Department of Chemistry, Colorado State
University, Ft. Collins CO 80523 USA, email: gwillsky@buffalo.edu
The biological effects of vanadium (V) vary greatly as the chemical environment of the V or the
biological system is modified1. We have previously reported the anti-diabetic effects of V
dipicolinic acid complexes with different oxidation states2. We here report the result of
modifications of the dipicolinic acid ligand environment on the effects of treatment with V-
compounds in oxidation state +5 on hyperglycemia and hyperlipidemia in STZ-diabetic rats. The
four V complexes tested in this study are shown in Figure 1 and deviate in structure and
electronic properties. Administration of [V(V)O2(dipic)]- lowered diabetic hyperglycemia to levels
close to normal, while administration of the other V complexes had a small but often significant
effect in lowering the elevated blood glucose. Treatments with all complexes were effective in
significantly lowering diabetic hyperlipidemia to near normal levels, as monitored by
measurement of serum cholesterol, triglycerides and free fatty acids. The most effective V
complex in lowering diabetic hyperlipidemia was [V(V)O(dipic-OH)(NH2O)] which lowered free
fatty acids and triglycerides to below normal levels levels and cholesterol to near normal levels.
[V(V)O2(dipic)]
- These results show that
O
[V(V)O(dipic)NMe2O)] subtle alterations of the
O
O O
V environment in
O O
O O
dipicolinic acid
O O
M HO
+
N V M+ O
N V
O
O
O O
N V
O HO N V complexes with the same
O O N CH3 NH2
H O
O O
H2O 2
+5 oxidation state have a
CH3 O
+
M = NH , Na , K
4
+ + + M+ = NH4+, Na+
O
O
O significant effect on the
anti-diabetic properties
-
[V(V)O2(dipic-OH] [V(V)O(dipic-OH)(NH2O)]
of the metal.
Figure 1. V complexes used in the study of diabetic rats
The effects of changes of the biological system were also monitored using the simple salt
vanadate, V(V) in two cell culture systems and the details are given in a separate presentation.
V inhibited cell growth in muscle myoblasts (L6) and rat hepatoma cells (H4IIE) cells, affecting
cell adhesion before killing the cells. V treatment induced apopoptosis in muscle cells; but not in
liver cells. The differences observed appear to be directly related to the different cell types since
V as the simple salt vanadate in the +5 oxidation state was administed to both cell lines and the
cells were grown in the same type of medium. These results imply that V growth inhibition is
mediated via the apoptotic pathway in muscle but not in liver.
Varying effects on biological endpoints of V in different tissues and the effects of modification of
the V complex, can be effectively used when designing potential therapeutic V compounds.
Acknowledgements: We thank the NIH and Luso-American Development Foundation for financial support.
[1] A.Tracey,G. Willsky, E.Takeuchi, (2007) Vanadium: Chemistry, Biochemistry, Pharmacology and
Technical Applications, CRC Press , Boca Raton FL. 250 pp.
[2] P. Buglyó, D. Crans, E. Nagy, R. Lindo, L. Yang, J. Smee, W. Jin, L.-H. Chi, M. Godzala III, and G.
Willsky, Inorgan. Chem. 44 (2005)5416-5427.

Oral lectures O23
Coordination of oxovanadium(IV) to human serum apo-transferrin: a

calorimetric comparison study
Chris Orvig,a Khalegh Bordbar,a,b A. Louise Creagh,c Cheri A. Barta,a Katherine H.

Thompson,a Charles A. Haynesd
a
Medicinal Inorganic Chemistry Group, Department of Chemistry, University of British Columbia, Vancouver,
BC, V6T 1Z1 Canada; b Present address: Department of Chemistry, Isfahan University, Isfahan, 81746-
73441, I.R. Iran; c Centre for BioThermodynamics, Laboratory for Molecular Biophysics, University of British
Columbia, Vancouver, BC V6T 1Z4 Canada; d Michael Smith Laboratories and the Department of Chemical
and Biological Engineering, University of British Columbia, Vancouver, BC V6T 1Z4 Canada.
email: orvig@chem.ubc.ca
Bis(maltolato)oxovanadium(IV) (BMOV), and its ethylmaltol analog, bis(ethylmaltolato)-

oxovanadium(IV) (BEOV), are candidate insulin-enhancing agents for the treatment of type 2
diabetes mellitus;1 BEOV is currently undergoing phase IIa trials. Results of previous solution
studies of the interaction of BMOV with the most common plasma proteins apo-transferrin and
(to a lesser extent) albumin indicated an in vivo biomolecular transformation that favors small
molecule, readily dissociable, binding for optimal pharmacological efficacy.2 In order to rule out
intact binding by complexed vanadium, as in BMOV, to apo-transferrin, we have undertaken a
thorough calorimetric determination of heats of association, comparing binding of BMOV to that
of vanadyl ion V(IV), and its oxidized counterpart, vanadate ion V(V). Differential scanning
calorimetry (DSC) thermograms obtained for all three transferrin-ligand complexes were
superimposable. We can conclude from these studies that BMOV dissociates rapidly under the
aerobic conditions of calorimetric determination of formation constants, and that the vanadyl
ions readily oxidize to vanadate ions. Thus, the formation constant obtained is for vanadate-
transferrin binding, and is not strictly relevant to the physiological biodistribution of BMOV. The
DSC derived binding constants, both in the range of log K ≈ 5 for vanadate-transferrin binding,
are consistent with earlier EPR studies of 0.1 M vanadate binding to apo-transferrin at pH 7.4 at
25° C.3
Acknowledgement is made to NSERC and CIHR (both of Canada) for funding.
[1] K. H. Thompson, C. Orvig, J. Inorg. Biochem. 100 (2006) 1925-1935.

[2] B. D. Liboiron, K. H. Thompson, G. R. Hanson, E. Lam, N. Aebischer, C. Orvig, J. Am. Chem. Soc. 127
(2005) 5104-5115.
[3] W. R. Harris, C. J. Carrano, J. Inorg. Biochem. 22 (1984) 201-218.

O24 Oral lectures
VO(IV) complexes of maltol and ethylmaltol for oral treatment of type 2

diabetes mellitus: lessons from speciation studies and phase I and II
clinical trials
Katherine H. Thompson,a Paloma F. Salas,a John H. McNeill,b Jay B. Lichter,c Michael S.

Scaife,c Chris Orviga
a
Medicinal Inorganic Chemistry Group, Department of Chemistry, University of British Columbia, 2036 Main
Mall, Vancouver, BC, Canada V6T 1Z1; bFaculty of Pharmaceutical Sciences, University of British Columbia,
2146 East Mall, Vancouver, BC, Canada V6T 1Z3; Akesis Pharmaceuticals, Inc., La Jolla, CA, USA 93037
email: kthompso@chem.ubc.ca
3-Hydroxy-2-methyl-4-pyrone and 2-ethyl-3-hydroxy-4-pyrone (maltol and ethylmaltol,

respectively) have proven especially suitable as ligands for vanadyl ions, with the resultant
compounds having the desired intermediate stability for prodrug use. Both
bis(maltolato)oxovanadium(IV) (BMOV), and the ethylmaltol analog,
bis(ethylmaltolato)oxovanadium(IV) (BEOV), are candidate insulin-enhancing agents for the
treatment of type 2 diabetes mellitus.1 BEOV has successfully completed phase I clinical trials
and is now undergoing phase IIa trials. In preliminary data from the phase II trial, fasting
blood glucose (FBG) of some treated diabetic subjects has been observed to decrease markedly.
BEOV is being orally administrated at a dose of 20 mg once per day. In one case, a subject had
a baseline of 276 mg/dl and dropped to 130 mg/dl after 7 days of treatment. Additional data
will be presented. In human volunteers (phase I trial), feeding a standard breakfast
immediately following oral dosing with 75 mg BEOV (11 mg V) resulted in an order of
magnitude lower maximal concentration of vanadium in serum, when compared to fasted
subjects (Cmax= 34.0 ± 25.1 ng/mL vs. 426.1 ± 126.6 ng/mL, fed vs. fasted, respectively, p <
0.0001). Availability of stored vanadium, based on our previous studies of biodistribution and
speciation of orally administered BMOV and BEOV,2 will thus vary widely depending on
interaction with ligands in food, or lack thereof. A re-examination of these results in light of
current Upper Limits of Intake (IOM, FNB) guidelines will be considered.
Acknowledgements: The authors would like to thank the Natural Sciences and Engineering Research Council
of Canada (NSERC) and Akesis Pharmaceuticals, Inc. for funding.
[1] K. H. Thompson, C. Orvig, Vanadium in Diabetes: 100 Years from Phase 0 to Phase I, J. Inorg. Biochem.
100 (2006) 1925-1935.
[2] K. H. Thompson, B. D. Liboiron, G. R. Hanson, C. Orvig, In Vivo Coordination Chemistry and
Biolocalization of Bis(ligand)oxovanadium(IV) Complexes for Diabetes Treatment, In: Medicinal Inorganic
Chemistry (J. L. Sessler, S. R. Doctrow, T. J. McMurry, S. J. Lippard, Eds.) ACS Symposium Series, Vol. 903
(2005) 384-399.

Oral lectures O25
Evaluation of insulin-mimetic activities of vanadyl complexes from the

viewpoint of heterocyclic bidentate ligands
Akira Katoh,a Yuriko Matsumura,a Yutaka Yoshikawa,b Hiroyuki Yasui,b

and Hiromu Sakuraic
a
Department of Materials and Life Science, Seikei University, Kichijoji, Musashino-shi, Tokyo 180-8633,
b
Japan, Department of Analytical and Bioinorganic Chemistry, Kyoto Pharmaceutical University, Misasagi,
c
Kyoto 607-8414, Japan , and Faculty of Pharmaceutical Sciences, Suzuka University of Medical Science,
3500-3 Minami-Tamagaki-cho, Suzuka, Mie 510-0293, Japan. e-mail: katoh@st.seikei.ac.jp
The numbers of patients that suffer from diabetes mellitus (DM) in the world have been
forecasted to increase to approximately 333 million in 2025 from 194 million in 2003.
Untreated DM sometimes causes many severe secondary complications and ocular disorders.
The available treatments for both type 1 and 2 DM have undesirable defects. Therefore, the
developments of new synthetic therapeutics are being explored to improve the lives of diabetic
patients. Over a decade we focused on heterocycles such as hydroxymonoazines,
hydroxydiazines, and 3-hydroxy- thiazole-2(3H)-thiones as bidentate ligands toward a vanadyl
ion. In this paper, we would like to review on synthesis of vanadyl complexes of various
heterocycles and their insulin-mimetic activities.
The following points became clear [1-7]; a) a vanadyl complex with heterocycle 1 showed
the highest insulin-mimetic activity in terms of IC50 value, which is a 50% inhibitory
concentration of the free fatty acid release from isolated rat adipocytes, among four kinds of
vanadyl complexes with heterocycles 1-4, b) blood glucose levels in STZ-induced diabetic rats
apparently were lowered from hyperglycemic to subnormal levels after treatment of vadadyl
complex with 1, c) vanadyl complexes with heterocycles 5 exhibited in vitro insulin-mimetic
activities, in which a correlation between the activity and the Hammett’s substituent constants
of R was found, d) the activity of vanadyl complexes with heterocycles 6 and 7 could not be
observed because they are insoluble in KRB buffer, and e) by plotting IC50 values vs. molecular
weights of 63 samples of vanadyl complexes, it was found that two vanadyl complexes with
molecular weights higher than 1000 (porphyrin structure) showed insulin- mimetic activities and
that a large number of vanadyl complexes with molecular weights of 300~400 showed high
insulin-mimetic activities in terms of IC50 values.
O Me
X Y
OH
V N 4.5
Y X 4
Me N O N O
vanadyl complexes 3.5
1 OH Me 2 3
IC 50 (m M )
O S 2.5
OH Me N Me S 2
N 1.5
OH 1
N Me Me N O
R 5 0.5
Me 3 OH 4 0
OH 0 200 400 600 800 1000 1200 1400
M olecular W eight
R N S
N S Figure 1 Plots of IC50 values vs. molecular weights of vanadyl complexes
6 Me OH R 7
[1-7] A. Katoh et al.: Chem. Lett. 29, 866-867 (2000), 31, 114-115 (2002), and 33, 1274-1275 (2004);
Heterocycles, 60, 1147-1159 (2003), 73, 603-615 (2007); J. Inorg. Biochem., 100, 260-269 (2006), Bull.
Chem. Soc. Jpn.(Accounts), 79, 1645-1664 (2006).

O26 Oral lectures
The insulin-mimetic properties of vanadium with its effects on the

gene expression profiling of the insulin signaling pathway in diabetic
mellitus
Wenjun Ding,a Dan Wei, Ming Li, Jianhong Yang

a
College of Life Sciences, Graduate University of Chinese Academy of Sciences, No. 19A Yuquan Road,
Beijing 100049, P. R. China email: dingwj@gucas.ac.cn
The insulin-mimetic properties and antidiabetic effects of vanadium compounds have been
widely documented. Vanadium and its compounds stimulate glucose transport and oxidation,
glycogen synthesis, lipogenesis, and they inhibit lipolysis and gluconeogenesis. In vitro and in
vivo studies demonstrated that vanadium has a clear role in the effect on the insulin signaling
pathway, such as increases of insulin receptor binding, stimulation of down-regulation of insulin
receptors, inhibition of protein phosphotyrosine phosphatases, activation of nonreceptor protein
tyrosine kinases and inhibition of glucose-6-phosphatase.
Vanadium compounds appear to have a profound impact on insulin action through the insulin
signaling cascade, but the underlying mechanism is not fully understood. Several previous
studies also showed that the gene transcripts were up-regulated in diabetic rats. It has been
reported that the activities of MAPK, ERK1/2 and S6 kinase were stimulated by vanadyl
sulphate. Also, the PI3K pathway in vivo and in vitro was activated by vanadium compounds. In
vitro studies showed that vanadium compounds could increase ERK1/2 protein level and inhibit
cell proliferation via the MAPK pathway in a dose-response manner. In our previous study, of 96
genes surveyed, transcriptional patterns of 19 genes (20%) showed alterations in diabetic rats
compared with controls. Although most of these changed gene expressions were improved after
treatment with NaVO3 (14, 74%) and insulin (16, 84%), NaVO3 and insulin treatment resulted in
the alteration of 20 and 12 additional gene transcripts compared with no treatment. Comparison
of the gene expression profiling indicates that there is a significant difference between the
NaVO3-treated group and the insulin-treated group. Several candidate genes of the insulin
signaling pathway involved in the effect of vanadium treatment on hyperglycemia. We believe
that these findings in the gene expression advance the current of level of understanding of
glucose-lowering action of vanadium in diabetes mellitus.
Acknowledgements: The authors acknowledge the financial support received from NSFC (20571084) and
“Hundred Talents Program” of CAS.
[1] M. Z. Mehdi, S. K. Pandey, J. F. Theberge, et al, Cell Biochem Biophys 44 (2006) 73-81
[2] H. Sakurai, K. Tsuchiya, M. Nukatsuka, et al, J. Endocrinol. 126(1990) 451-459
[3] R. Sreekumar, P. Halvatsiotis, J. C. Schimke, K.S. Nair, Diabetes 51(2002) 1913-1920
[4] G. Willsky, L. Chi, Y. Liang, D. Gaile, Z. Hu, D. Crans, Physiol Genomics 26(2006) 192-201
[5] J. H. McNeill, H. L.Delgatty, M. L. Battell, Diabetes 40(1991) 1675-1678

Oral lectures O27
Arylalkylamine vanadium salts as a new generation of antidiabetic

compounds
Antonio Zorzano
Institute for Research in Biomedicine. Universitat de Barcelona. CIBERDEM.
Vanadium compounds show insulin-like effects which has been demonstrated both in vivo and
in vitro. The most widely studied compounds in animal models are vanadyl sulfate and sodium
orthovanadate. Some clinical studies have been performed using vanadium compounds and
they have shown efficacy in type 2 diabetic subjects. A major concern is safety, which calls for
the development of more potent vanadium compounds.
The semicarbazide-sensitive amine oxidase (SSAO)/vascular adhesion protein-1 (VAP-1) is a
bifunctional membrane protein highly expressed in adipose cells. On one hand, SSAO/VAP-1 is a
copper-containing ectoenzyme with amine oxidase activity and produces hydrogen peroxide. On
the other hand, SSAO/VAP-1 is an inflammation-inducible endothelial molecule involved in
leukocyte subtype-specific rolling under physiological shear. In this regard, substrates of SSAO,
such as benzylamine, in combination with low concentrations of vanadate strongly stimulate
glucose transport and GLUT4 recruitment in 3T3-L1 and rat adipocytes and show antidiabetic
effects in different animal models of diabetes. Chronic administration of benzylamine and
vanadate exerts potent antidiabetic effects in streptozotocin (STZ)-induced diabetic rats or in
Goto-Kakizaki diabetic rats. As far as mechanisms of action, we have found that
benzylamine/vanadate causes enhanced tyrosine phosphorylation of proteins and reduced
protein tyrosine phosphatase activity in adipocytes. In addition, incubation of human
recombinant SSAO, benzylamine, and vanadate generates peroxovanadium compounds in vitro.
Based on these data, we have proposed that benzylamine/vanadate administration generates
peroxovanadium locally in pancreatic islets, which stimulates insulin secretion and also produces
peroxovanadium in adipose tissue, activating glucose metabolism in adipocytes and in
neighboring muscle. This opens the possibility of using the SSAO/VAP-1 activity as a local
generator of protein tyrosine phosphatase inhibitors in antidiabetic therapy.
We have recently characterized a novel class of arylalkylamine vanadium salts that exert potent
insulin-mimetic effects downstream of the insulin receptor in adipocytes. These compounds
trigger insulin signaling, which is characterized by rapid activation of insulin receptor substrate-
1, Akt, and glycogen synthase kinase-3 independent of insulin receptor phosphorylation.
Administration of these compounds to STZ diabetic rats or to ob/ob mice lowered glycemia and
normalized the plasma lipid profile. In addition, arylalkylamine vanadium salts exerted
antidiabetic effects in STZ-diabetic rats with undetectable levels of plasma insulin. The use of
arylalkylamine vanadium salts represents a novel therapeutic approach in diabetes.

O28 Oral lectures
Can Vanadyl chelates help to detect cancer?
Marvin W. Makinena, Shengrong Shena, Suzanne D. Conzenb, Antonio J. Machado IIc,

Dong Yund, Qing Guo Xiec, Chien-Min Kaoc, and Chin-Tu Chenc
a b
Department of Biochemistry & Molecular Biology, Section on Hematology & Oncology, Department of
c d
Medicine, Department of Radiology, The University of Chicago, Chicago, Illinois 60637 and Department of
Biomedical Engineering, Illinois Institute of Technology, Chicago, Illinois 60616 USA
email: makinen@uchicago.edu
Detection of malignant tumors by positron emission tomography (PET) with 2-(fluorine-18)-2-

deoxy-D-glucose (FDG) as the tracer molecule is based on the high rate of glucose uptake and
increased glycolytic activity associated with cancer. In the clinical setting, PET detection of neo-
plasms is dependent on the intensity contrast between tumor sites and surrounding normal
tissue and is generally limited to tumors of ca. 10 mm in maximum dimension. Increased FDG
uptake by neoplastic tissue could lead to improved detection of small tumors and enhanced
diagnostic capability. To this end we have investigated the capacity of
bis(acetylacetonato)oxovanadium(IV) [VO-(acac)2] to increase uptake of FDG by cultured MDA-
MB-231 cells, a well defined breast carcinoma cell line. MDA-MB-231 cells, grown in Dulbecco’s
modified Eagle medium and Ham's F-12 containing 10% (v/v) fetal calf serum, penicillin,
streptomycin, D-glucose, vitamins, salts, and essential amino acids, were trypsinized and
transferred to Krebs-Ringer buffer containing 0.3 mM BSA and varying concentrations of
D-glucose according to assay conditions. In contrast to cultured 3T3-L1 adipocytes [J. Biol.
Inorg. Chem. 2005, 10, 874-886], SDS PAGE and phosphotyrosine immunoblots showed only
low levels of phosphorylated insulin receptor and insulin receptor substrate-1 when MDA-MB-
231 cells were incubated in the presence of 1–300 nM insulin. Addition of 50–250 µM VO(acac)2
markedly increased the levels of these tyrosine phosphorylated proteins. The uptake of
radioactive FDG by MDA-MB-231 cells in the absence of D-glucose showed that 100 µM
VO(acac)2 greatly enhanced FDG uptake within the initial 30 min incubation period compared to
cells in the absence of added VO(acac)2. In the presence of 5 mM D-glucose, equivalent to a
normal fasting blood glucose level in adult patients, 250 µM VO(acac)2 enhanced FDG uptake
within the initial 30–60 min period of incubation. PET imaging of single layers of MDA-MB-231
cells in culture flasks in the presence of 5 mM D-glucose showed increased intensity due to FDG
uptake when incubated in the presence of 250 µM VO(acac)2 compared to cells incubated
without VO(acac)2. The results of these preliminary investigations suggest that VO(acac)2 and
possibly other organic chelates of VO2+ may facilitate increased FDG uptake by neoplasms in
vivo, enhancing the sensitivity of PET imaging for detection of cancer. The ultimate applicability
2+
of VO -chelates to enhance FDG uptake in human cancer will depend on the relative sensitivity
of tumor versus normal tissue to VO(acac)2 activity. Therefore, future experiments will be
directed towards PET imaging of transgenic and xenograft models of human breast cancer in
mice with and without administration of VO(acac)2.
Acknowledgements: We thank the Luso-American Development Foundation for travel support. This research
was supported by grants from the National Institutes of Health (P50 CA125183, P30 CA14599, and S10
RR022520).

Oral lectures O29
Lewis bases in Vanadium(V) catalyzed oxygen transfer catalysis
Silvia Lovat, Miriam Mba, Marta Pontini Giulia Licini* and Cristiano Zonta*
a
Dipartimento di Scienze Chimiche, Università di Padova, via Marzolo 1, 35131 Padova, Italy
email: cristiano.zonta@unipd.it
Oxidation mediated by vanadium compounds has been revitalized by vanadium dependent

enzymes haloperoxidases, producing an ever growing number of studies on biomimetic
complexes.1 The main interest has been directed toward oxidations of sulfides, halides, and
olefins.2 In the oxidation pathway performed by these complexes it has been largely accepted
that the mechanism follows an electrophilic activation of the peroxide followed by a nucleophilic
attack by the substrate on the η2 coordinated peroxide.3 During the course of these studies we
noticed that the presence in solution of a LB was distinctively enhancing the catalytic activity of
the complex (Figure 1).
ROOH O
O O
S VV complex S S
+
Lewis Base
Figure 1. Vanadium metal complexes used in sulfoxidations with the addition of Lewis Bases.
The Lewis Base (LB) is able to bind to the metal in addiction to the ligand, and capable to
selectively modify the catalytic properties of the complex. This approach not only offers the
opportunity to module the catalytic systems with a defined reactivity and selectivity profile, but
also to better understand the basic principles behind metal activation in synthetic and biological
systems.
Acknowledgements: The authors would like to thank FIRB-2003 CAMERE-RBNE03JCR5 project, COST Action
D40 ‘Innovative Catalysis, MIUR and University of Padova for their financial support.
[1] D.C Crans, J. Smee, E. Gaidamauskas, L. Yang Chem.Rev. 104 (2004) 849.
[2] A.G.J. Ligtenbarg, R. Hage, B.L. Feringa Coord. Chem. Rev. 237 (2003) 83
[3] C. J. Schneider, J. E.Penner-Hahn, V. L. Pecoraro 130 (2008) J. Am. Chem. Soc. 2712.

O30 Oral lectures
Octahedral-square pyramidal equilibrium in bis-chelated VIVO species:

spectroscopic and DFT characterization
Eugenio Garribba,a Giovanni Micera,a Daniele Sanna,b
a
Dipartimento di Chimica, Università di Sassari, Via Vienna 2, 07100 Sassari, Italy; email: garribba@uniss.it
b
Istituto C.N.R. di Chimica Biomolecolare, Trav. La Crucca 3, 07040 Li Punti, Sassari, Italy
The “additivity rule” assumes that an axial ligand does not contribute to 51V anisotropic
hyperfine coupling constant along z axis (Az), so that its presence cannot be demonstrated by
EPR spectroscopy;1 therefore, the possibility of an equilibrium between the VIVO species with
and without a solvent (or ligand) molecule in the sixth coordination position usually is not taken
into account. Few exceptions to the “additivity rule” have been reported: the octahedral
complexes [VOX(capca)] where Hcapca is N-{2-[(2-pyridylmethylene)amino]phenyl}pyridine-2-
carboxamide and X is Cl−, SCN− or CH3COO−,2 and the bis-chelated complexes formed in DMF by
several amidrazone derivatives3 and in water by 6-methylpicolinate.4
In this work we demonstrate the existence of an equilibrium between the octahedral and the
trans square-pyramidal forms of bis-chelated VIVO complexes. The characterization was
performed through the combined application of EPR spectroscopy and DFT methods. The
complexes studied were formed in aqueous solution by 6-methylpicolinate (6-mepic) and 6-
methyl-2,3-pyridinedicarboxylate (6-me-2,3-dpc).
EPR spectra of the VIVO bis-chelated species of 6-mepic and 6-me-2,3-dpc consist of two set of
resonances, the inner with an anomalously low value of Az (~148x10−4 cm−1) and the outer with
a “normal” value (~161x10−4 cm−1). With increasing the ionic strength, the inner signals
disappear and the outer ones increase in intensity. This result has been explained postulating an
equilibrium between the octahedral and square-pyramidal form, similar to the octahedral-square
planar transition of the tetra-aza NiII complexes.5
CH3 CH3
O –
O –
N O O N O O
Ionic strength
V V + H2O
O – N O – N
O O
OH2
H3C H3C
Figure 1. Equilibrium between the six and five-coordinated bis-chelated VIVO complex of 6-methylpicolinate.
DFT calculations performed with Gaussian 03 software allow to prove these assumptions. We
reached a consistent improvement in the prediction of Az, calculating it for 24 representative
VIVO complexes with different charge, geometry, coordination mode and donor sets; deviations
< 5% and, in most of the cases, < 3% with respect to the experimental values were obtained.
The calculated values of Az for the octahedral species [VO(6-mepic)2(H2O)] and [VO(6-me-2,3-
pdc)2(H2O)]2−, and for the square-pyramidal [VO(6-mepic)2] and [VO(6-me-2,3-pdc)2]2− are in
good agreement with those measured.
Moreover, DFT methods correctly predict the unusual low value of Az for [VOX(capca)] and for
[VOL2(dmf)]2+ formed by the amidrazone derivatives in DMF.2,3 This suggests that the
disagreement with the “additivity rule” is probably due to an incompleteness of the EPR theory
rather than to a real anomaly of the Az value.
[1] N. D. Chasteen, in Biological Magnetic Resonance; Plenum Press: 1981, vol. 3, pp. 53-119.
[2] E. J. Tolis, K. D. Soulti, C. P. Raptopoulou, A. Terzis, Y. Deligiannakis, T. A. Kabanos, J. Chem. Soc.,
Chem. Commun. (2000) 601-602.
[3] M. T. Cocco, V. Onnis, G. Ponticelli, B. Meier, D. Rehder, E. Garribba, G. Micera, J. Inorg. Biochem. 101
(2007) 19-29.
[4] E. Kiss, E. Garribba, G. Micera, T. Kiss, H. Sakurai, J. Inorg. Biochem. 78 (2000) 97-108.
[5] A. Anichini, L. Fabbrizzi, P. Paletti, R. M. Clay, Inorg. Chim. Acta 24 (1977) L21-L23.

Oral lectures O31
Vanadium in Life
Dieter Rehder
Department Chemie, Universität Hamburg, 20146 Hamburg, Germany

email: rehder@chemie.uni-hamburg.de
As summarised in the phylogenetic tree, Fig. 1,1 vanadium is employed by a plethora of

organisms. There are at least three different levels, on which vanadium can act in living
organisms:
(1) The ease of exchange between the oxidation states +V and +IV (and, to some extent, also
+III) classifies this element as a redox catalyst: Amavadin from Amanitae mushrooms (e.g. the
fly agaric) may be a relic of an evolutionary overcome oxygenase. Several protobacteria gain
energy from respiration based on vanadate(V) as electron acceptor. Further, the presence of
vanadium in alternative nitrogenases in Azotobacter and Anabaena reflects its ability to take
part in the activation and electron delivery to N2.
(2) The VV centre in vanadate-dependent peroxidases from marine macro algae, fungi and
lichens exerts Lewis acidity and thus activates peroxide in the 2e- oxidation of substrates such
as halides and sulphides.
(3) The similarity between vanadate and phosphate makes vanadate an apt regulator for
phosphate-metabolising enzymes, essentially through the inhibition of phosphatases, also in
high developed organisms, viz. plants and animals, a fact which has implications for the insulin-
mimetic/enhancing effect of vanadium.
EEuuccaarryy ao t a
109 a
Ani ma le s
Plantae 0.5
Chlorophyta
Halimeda
Rhodophyta
Corallina
Lichen
B a c te ria Xanthoria
Basidiomycota
Amanita
Proteobacteria Fungi
Pseudomonas Ascomycota
Shewanella Curvularia
Geobacter Phaeophyta
Azotobacter Ascophyllum 1.2
Thioalkalivibrio Arc ha e a
2.1
Cyanobacteria
Anabaena 3.0
3.5
LUCA
Figure 1. The phylogenetic tree, including organisms (in italics) which (can) use vanadium in life processes.1
LUCA = last uniform common ancestor. In plants and animals, vanadium may have a regulatory function.
[1] D. Rehder, Org. Biomolec. Chem. 6 (2008) 957-964.

O32 Oral lectures
Biological Effects and Cytotoxicity of a complex of Vanadium(V) with

salicylaldehyde semicarbazone in osteoblasts in culture
Josefina Rivadeneiraa,b, Daniel A. Barrioa, Gabriel Arrambidec, Dinorah Gambino c,

Liliana Bruzzonea, Susana B. Etcheverrya,b*
a
Facultad de Ciencias Exactas, UNLP. 47 y 115 (1900) La Plata, Argentina
b
CEQUINOR (CONICET-UNLP), Facultad de Ciencias Exactas, UNLP, La Plata, Argentina
c
Facultad de Química, Universidad de la República, Montevideo, Uruguay
* Corresponding author e-mail: etcheverry@biol.unlp.edu.ar
Interaction of simple vanadium species with ligand groups bearing pharmacological activity,
particularly those with antitumoral and insulin-mimetic properties, is of growing scientist
interest. Vanadate mimics various insulin actions on different cell types and also in cell free
systems. Semicarbazones are versatile compounds of considerable interest because of their
chemistry and potentially beneficial pharmacological effects, such as antitumor, antibacterial,
antiviral and antimalarial activities. The biological effects of these ligands are considered to be
related to their ability to form chelates with metals. Biological activities of metal complexes
differ from those of either ligands or the metal ions, and increased or decreased biological
activities have been reported for several transition metal complexes. In the frame of our
continuing studies devoted to the biological and potential pharmacological properties of
vanadium compounds we report herein the biological actions of
VVO2(salicylaldehydesemicarbazone) (V(V)-SalSem) on two osteoblast cell lines in culture
(MC3T3E1 and UMR106). Cell proliferation, differentiation, morphological alterations, oxidative
stress, activation of the extracellular regulated kinases (ERK) cascade and apoptosis have been
investigated. V(V)-SalSem inhibited cell proliferation in a dose response manner as determined
by the crystal violet bioassay, with the same potency and efficacy in both cell lines (IC50: >100
μM). The inhibition at high doses (100μM) could be partially reversed by the free radical
scavengers NAC (N-acetylCysteine) and a mixture of vitamins E and C. Changes in cell
proliferation correlated with morphological alterations as could be determined by ligt microscopy
with Giemsa staining. Alterations began at 10 μM and increased with complex concentration.
Stress fibers were also desorganized in a dose response manner being the network lost between
50-100 μM. Specific activity of alkaline phosphatase (ALP) and collagen content, two mature
osteoblast phenotype markers, were inhibited in a dose response manner by the complex in
UMR106 cells. In an atempt to elucidate the mechanisms of action involved in the toxicity
actions of V(V)-SalSem, the oxidative stress and the activation of ERK pathway were analyzed.
The determination of oxidative stress through the fluorometric measurement of free radical
levels, showed that complex promoted the production of free radicals (Dihydrorhodamine
oxidation to rhodamine) in a dose response manner reaching a two-fold value at 100 μM in
comparison with basal conditions. This effect could be partially reversed by free radical
scavengers. ERK cascade was activated by the complex as it was determined by Western blot
using two specific inhibitors (PD98059) and wortmannin. These events correlated with the
enhancement of apoptosis over necrosis as could be seen using AnnexinV-Propidium Iodide.
In conclusion, the complex formed between vanadium(V) and salicylaldehyde semicarbazone
displays cytotoxic effects on osteoblasts in culture through the production of free radicals and
the activation of ERK cascade. These mechanisms triggered the apoptotic events that convey to
cell death.
Acknowledgements: S. B. Etcheverry thanks the Reitoria da Universidade Técnica de Lisboa, Portugal, the
financial support for travelling.

Oral lectures O33A
Interaction of Dioxovanadium(V) with Iminodiacetic Acid and

Phenylalanine Using SIT
Kavosh Majlesi,a Karim Zare,a,b Saghar Rezaienejad a
a
Chemistry Department, Islamic Azad University, Science & Research Campus, Tehran, Hesarak, Iran
b
Chemistry Department, Shahid Beheshti University, Tehran, Evin, Iran
email: kavoshmajlesi@gmail.com
When the required Pitzer parameters are evaluated accurately from extensive data, the Pitzer
model is a preferred, standard method in presentation of experimentally determined
thermodynamic properties of electrolytes. However, the specific ion interaction theory(SIT)
because of its advantages in mathematical simplicity and its less parameterized nature, may
find application when the experimental data are less extensive, or the accuracy provided by the
SIT model is deemed to be satisfactory, or in systems where complex formation occurs. This is
especially true in cases in treatment of equilibrium constants. The shortcoming of the SIT model
is its rather low accuracy in reproduction of mean activity coefficients in comparison with Pitzer
model. However, the error is usually less than 10% at ionic strength up to 6-10 m at 25 ºC. The
less-parameterized SIT model gives quite reasonable estimations of equilibrium constants in
different media at various ionic strengths, provided that the necessary interaction coefficients
are known. Consequently, the SIT model has the potential to become a useful method to
estimate medium effects on equilibrium constants in concentrated solution in high temperature
chemistry. There is a project on the IUPAC web site about the ionic strength corrections for
stability constants using SIT which has been completed in 2005, but to our knowledge no
reports of the ionic strength dependence of dioxovanadium(V) complexes with iminodiacetic
acid(IDA) and phenylalanine has appeared. Therefore this research has been undertaken to
show the application of specific ion interaction theory1 for the aforementioned complexes at
different ionic strengths from 0.1 to 1.0 mol dm-3 of sodium perchlorate and pH range 1.00 to
4.00. The temperature was kept constant at 25 ºC. Stoichiometry and stability constants of the
formed complexes were determined2 from a combination of potentiometric and UV
spectroscopic measurements based on the relationship A=f(pH). The semi-empirical
parameters3-5 for ionic strength dependence have been calculated on the basis of minimizing the
error function using Gauss-Newton nonlinear least squares method in Microsoft Excel 2000
program. Debye-Huckel theory applies well for both of the complexes but phenylalanine
complex data fit better in the specific ion interaction theory. Finally the values of interaction
coefficients ∆ε= -0.7643, 0.7389 have been calculated for the IDA and phenylalanine complexes
respectively.
[1] K. Majlesi, S. Rezaienejad, Chin. J. Chem. 25 (2007) 1815-1820.

[2] K. Majlesi, K. Zare, J. Mol. Liq. 125 (2006) 62-65.
[4] K. Majlesi, K. Zare, F. Najafi, Russ. J. Inorg. Chem. 52 (2007) 1299-1303.
[5] K. Majlesi, K. Zare, Phys. Chem. Liq. 44 (2006) 257-268.

O33 B Oral lectures
Complexation of dioxovanadium(V) with nitrilotriacetic acid in different

sodium perchlorate aqueous solutions using SIT
Saghar Rezaienejad,a Kavosh Majlesi,a Karim Zarea,b
a
b
email: saghar.rezaeinejad@gmail.com
In investigations of systems where complex formation takes place, a method of

constant ionic medium is usually adopted. There are difficulties in determination of
activity coefficients of reaction species in a constant ionic medium. Usually only a
value of equilibrium constant in a certain medium can be determined, and the number
of equilibrium constants obtained is generally small. Second, the accuracy of
equilibrium constants is relatively low in comparison with that of mean activity
coefficients and osmotic coefficients. Accordingly, owing to these two facts, it is
sensible to use an activity model with fewer parameters when dealing with
experimental equilibrium constants, as it is often impractical to determine more than
one or two empirical parameters from a small number of such constants with limited
accuracy. The specific ion interaction theory (SIT) model can be regarded as a
simplified version of the Pitzer formalism without consideration of triple interactions
and interactions between ions of the same charge sign. The SIT model is most useful
in the ionic strength range up to 3.5-4.0 mol dm-3 and successful applications of the
SIT model at 25 ºC in NaCl solutions up to the saturation of halite have also been
demonstrated. Thus, ionic strength effects for dioxovanadium(V) complexes with
nitrilotriacetic acid(NTA) have been studied in an ionic strength range of 0.1 to 1.0
mol dm -3 of sodium perchlorate at 25 ºC using SIT.1 Acidic solutions of
dioxovanadium(V) were titrated with basic solutions of NTA at different ionic
strengths. The absorbance data in the UV range(245 to 280 nm) and pH = 1.00-2.50
were used for minimizing the error function on the basis of Gauss-Newton nonlinear
least squares method in Microsoft Excel 2000 program. Two species, VO2H2L and
VO2HL-, have been detected according to curve fitting, which allows us to calculate the
formation constants. There are descending patterns for the dioxovanadium(V)
complexes with NTA according to the SIT model without any maximum or minimum,
but there are combination of ascending and descending patterns on the basis of
extended Debye-Huckel model.2-6 Ultimately it can be concluded that SIT model
applies well for the NTA complexation with dioxovanadium(V).
[1] K. Majlesi, S. Rezaienejad, Chin. J. Chem. 25 (2007) 1815-1820.

[2] K. Majlesi, K. Zare, S. M. Shoaie, J. Chem. Eng. Data 50 (2005) 878-881.
[3] K. Majlesi, K. Zare, Phys. Chem. Liq. 44 (2006) 257-268.
[6] K. Majlesi, K. Zare, F. Najafi, Russ. J. Inorg. Chem. 52 (2007) 1299-1303.

Oral lectures O34
Recent advances in decameric vanadate biochemistry
Manuel Aureliano
CCMAR, University of Algarve; Dept. Chemistry and Biochemistry and Pharmacy, FCT, University of Algarve;
email: maalves@ualg.pt
Great care is needed when utilising vanadate solutions because decavanadate species can occur
even at physiological pH values through a slight acidification of the medium. Few studies point
out that that the effects cannot be taken as evidence that monomeric vanadate is the inhibiting
species and that individual vanadate species can differently affect the biological processes,
being in some cases decavanadate the only effector. Decavanadate interacts with the
polyphosphate, nucleotide, inositol 3-phosphate binding sites of enzymes either in the substrate
domain or in an allosteric effector site does not tend to follow a simple model of action1,2.
Recently in vivo vanadium toxicological studies following decavanadate administration point out
to specific effects induce by this vanadium oxoanions. Apparently, in hepatic and cardiac muscle
cells, the degree of vanadate toxicity depends on the mode of administration such as
intraperitoneal or intravenous, and is also dependent; at some extend, at the vanadate species
such as decavanadate3, which induces different changes in vanadium accumulation, lipid
peroxidation and oxidative stress markers, than the ones observed for vanadate4.
V10
Figure 1. Cellular targets and Δψ
ADP
cellular responses for V10: Pumps, V10 ATP
Ca2+
ionic channels, contractile system,

cytoskeleton, mitochondria, V10 ⇔ V1 V10 Ca2+
extracellular matrix and ROS

RS
changes. RS, sarcoplasmic ROS V10 in CS ADP
Ca2+
reticulum, CS, Contractile system, ATP
ROS, reactive oxygen species, V10

decameric and V1, monomeric Δψm V10
vanadate species. Membrane V10
potential, Δψm.
Ca2+ V10
In mitochondria, where vanadium was shown to be particularly accumulated following

decavanadate in vivo administration, nM concentration of decavanadate induces membrane
depolarization besides oxygen consumption inhibition5. Other recent studies from ours and
others research groups, included, for instance, the use of decavanadate or decavanadate
compounds as a probe in comprehension of muscle contraction6,7, modulation of ionic
channels8,9, interaction with lipid interfaces10, calcium homeostasis11 cytoskeleton structures
dynamics12, cell growth and extracellular matrix mineralization13, and as a prodrug of insulin
mimetics14 or in mechanisms of cell death15 induce by vanadate. We believe that these and
other recent studies with decavanadate species and compounds described in the present review
will allow a better understanding of decavanadate targets in cellular biology (Figure 1).
[1] D.C. Crans, Comments Inorg. Chem. 16 (1994) 1-33; [2] M. Aureliano, V.M.C Madeira, In Vanadium in the
Environment; John Wiley & Sons, New York, 1998, 333-357 ; [3] M. Aureliano, and R. M. C. Gândara, J. Inorg.
Biochem., 99 (2005) 979-985; [4] S.S Soares, H. Martins, J. Coucelo, C Gutiérrez-Merino, and M. Aureliano, J.
Inorg. Biochem. 101, (2007) 80-88 ; [5] S.S. Soares, C. Gutiérrez-Merino, and M. Aureliano, J. Inorg. Biochem.
101 (2007) 789-796. ; [6] T. Tiago, M. Aureliano, C. Gutiérrez-Merino, Biochemistry 43 (2004) 5551-5562.; [7] T.
Tiago, P Martel, C. Gutiérrez-Merino, M. Aureliano Biochem. Biophys. Acta, 1771 (2007) 474-480.; [8] B. Nilius, J.
Prenen, A. Janssens, T. Voets, and G. Droogmans, J. Physiol.- London, 560 (2004) 753-765. ; [9] M. Gutierrez-
Aguilar, Perez et al, Biochem. Biophys. Acta 1767 (2007) 1245-1251 ; [10] D.C. Crans in: Vanadium Biochemistry,
Research Signpost, Kerala, India, 2007 ; [11] M. Aureliano, S. S Soares, T. Tiago, S. Ramos, C. Gutierrez-Merino
In: Vanadium: The versatile metal, ACS Symposium Series. 974, (2007), 249-263; [12] S Ramos, M. Manuel, T.
Tiago, R. O., Duarte, J Martins, C Gutiérrez-Merino, J.J.G Moura, M. Aureliano, J. Inorg.Biochem.100 (2006) 1734-
1743.; [13] D.M. Tiago, M.L. Cancela, M. Aureliano and V. Laize, FEBS Lett., 582 (2008) 1381-1385.; [14] F.
Yraola et al, Chem Biol Drug Des. 69 (2007) 423-428 ; [15] S.S. Soares, F. Henao, M. Aureliano, C. Gutiérrez-
Merino, Chem. Res. Toxicol. 21 (2008) 607-618.

O35 Oral lectures
A novel function of Vanabin2 and the relationship among proteins

involved in the accumulation and reduction of vanadium by ascidians
Hitoshi Michibata,Tatsuya Ueki, Norifumi Kawakami
Department of Biological Science, Graduate School of Science, Hiroshima University, Higashi-Hiroshima 1-3-
1, Hiroshima 739-8526, Japan, e-mail: hmichi@hiroshima-u.ac.jp
Ascidians, known as sea squirts, accumulate high levels of vanadium ions. Their blood cells can
contain vanadium ions at concentrations up to 350 mM, a 107-fold increase over its dissolved
concentration in seawater (35 nM). Accumulated vanadium ions (VV) are first reduced to VIV in
ascidian vanadocytes and stored in their vacuoles containing high levels of protons and sulfate
ions where they are finally reduced to VIII and seem to exist as free ions[1]. Ongoing research
over the last decade has identified many proteins involved in the accumulation and reduction of
vanadium in vanadocytes, blood plasma and digestive tract of ascidians, such as H+-ATPase,
chloride channels, AsSUL1 (sulfate transporter), enzymes of the pentose-phosphate pathway,
AsGST (glutathione transferase), Vanabin1–4, VanabinP, CiVanabins, VBP-129 (vanadium-
binding protein 129), VIP1 (Vanabin-interacting protein 1) and metal-ATPase. To elucidate
overall mechanisms of vanadium accumulation and reduction in ascidians, not only individual
functions of the proteins but also the relationship between the proteins should be clarified from
now on. Thus, in this talk, we will describe a novel function of Vanabin2 as a VV reductase in
which the thiol-disulfide exchange reactions are involved and the relationship among NADPH,
GSH, Vanabin family, AsGST, VBP-129, VIP1, AsSUL1 which may provide sufficient knowledge
how these proteins and coenzymes share their roles to accumulate vanadium in ascidians.
Figure 1. Schematic representation of

vanadium accumulation and reduction
by ascidians. The concentration of
vanadium dissolved in sea water is
only 35 nM in the +5 oxidation state.
While, the highest concentration of
vanadium in ascidian blood cells
VIP1 attains up to 350 mM. In addition
Vanabin1 4 500 mM of sulfate is contained. The
Metal-ATPase
contents of vacuoles are maintained in
an extremely low pH of 1.9 by H+-
AsGST
ATPases. Under the environment,
almost all vanadium accumulated is
VanabinP
H+-ATPase Sulfate Transporter
reduced to VIII via VIV. The first step
VBP-129
of vanadium uptake may occur at a
branchial sac or digestive organs,
where AsGST was identified as a
major vanadium carrier protein. VBP-
129 and VanabinP were isolated in the
blood plasma. Vanabin1-4 and VIP1
were in the cytoplasm of vanadocytes.
The pentose phosphate pathway,
which produces NADPH, was disclosed
to localize in the cytoplasm. A metal-
ATPase and AsSUL1 were also found
in vacuolar membrane.
[1] H. Michibata, M. Yoshinaga, M. Yoshihara, N. Kawakami, N. Yamaguchi, T. Ueki, In “Vanadium the

Versatile Metal”, K. Kustin, J. C. Pessoa, D. C. Crans Eds., ACS Symp. Ser., 974, Oxford University Press:
(2007) pp. 264-280.

Oral lectures O36
Vanadium induces AIH: implications for the pulmonary immune

system
Mitchell D. Cohena, Ph.D. and Andrew J. Ghiob, M.D.
a
NIEHS Center of Excellence, Dept. of Environmental Medicine, NYU School of Medicine, Tuxedo, NY 10987
USA (mitchell.cohen@nyumc.org) and bClinical Research Branch, Human Studies Division, U.S. EPA,
Research Triangle Park NC 27711 USA (ghio.andy@epamail.epa.gov)
Residents of urban centers are routinely exposed to airborne pollution containing a variety of
particles, gases, biologics, and acids. While risk to human health from pollution is correlated
with the cumulative concentration of all pollutants present, many of the individual constituents
have their own potential to induce alterations in pulmonary inflammatory status and
immunocompe-tence. We believe one mechanism leading to these outcomes could be an
induction of altered iron homeostasis (AIH) in the lungs wherein airway and cellular levels of
biologically active iron (Fe) are affected. We propose that an AIH in the lungs following pollution
exposure is mediated by effects on proteins critical to Fe import, storage, and/or export. Among
the metals commonly associated with particulate matter (PM) is vanadium (V), a known
pulmonary immunomodulant. To determine whether V could induce changes in Fe homeostasis
in lung epithelial (BEAS-2B) cells and in alveolar macrophages (NR8383 cells), in vitro studies
were performed to assess effects of V on cell Fe import. The impact of V on select Fe-dependent
proteins and on the production of specific cytokines whose genes contain a promoter that can
be activated during states of cell Fe deficit were also assessed. To attempt to relate outcomes of
the in vitro studies to potential effects in situ, in vivo inhalation studies using V (soluble and
insoluble forms) were performed. Following their exposures (100 µg V/m3, 5 hr/d, 5 consecutive
days,), F344 rats were assessed for lung V burden as well as lavage concentrations of Fe, Fe-
dependent proteins, as well as select cytokines and chemokines, or infected with Listeria
monocytogenes and monitored for pathogen clearance over a 72-hr period. The in vitro study
results indicated that the presence of V significantly reduced the ability of the cells to maintain
normal Fe status. With both penta- and tetravalent V, cell Fe levels were reduced in comparison
to those when cells were presented Fe alone. Further evidence of V-induced effects were
reflected in reductions in levels of the major Fe storage protein ferritin, increases in the
expression/binding activity of iron response protein-1 (IRP-1), and the increased
formation/release of IL-8 whose gene contains a promoter (i.e., HRE) whose activation is
affected by low cell Fe levels. Effects of V upon Fe delivery out of the lung lining fluid and into
resident cells were noted in the in vivo studies. Further, the lavages of rats that inhaled the V
agents consistently had higher concentrations of non-heme Fe and ferritin. The lavages also
contained significant amounts of TNFα and MIP-2, AM and epithelial cell products whose genes
also contain an HRE promoter. Lastly, those rats that were exposed to soluble V had
significantly reduced abilities to clear viable bacteria; oddly, rats that had inhaled the insoluble
form of the metal had no change in (or actually even lower) bacterial levels compared to air-
exposed infected counterparts. The results of these studies demonstrate that V can affect iron
homeostasis in the lungs, and in particular, among cells critical to maintaining pulmonary
immunocompetence. Further studies are needed to clarify whether the presence of V in the
lungs also affects proteins critical to cell Fe storage and efflux. These results illustrate that
commonly-encountered airborne V compounds have a potential to induce AIH in situ, and thus
should be considered toxicologically-significant pollutants during assessments of daily risk to
health among the citizens of urban areas.
Acknowledgements: The Authors would like to thank Dr. João Costa Pessoa and the Fundação Luso-
Americana para o Desenvolvimento (Luso-American Development Foundation) for their help and financial
support in making this presentation possible.

O37 Oral lectures
DNA cleavage activity of VO(acac)2 and derivatives
Isabel Cavaco,a,b Ofelia Nouri,a Vera Ribeiro,c Esther Escribano,d Virtudes Moreno,d
Sofia Gama,e Isabel Tomaz,f João Costa Pessoab
a
Departamento de Química, Bioquímica e Farmácia, Universidade do Algarve, Campus de Gambelas, 8005-
b
139 Faro, Portugal, email: icavaco@ualg.pt; Centro de Química Estrutural, Instituto Superior Técnico, TU
c
Lisbon, Av Rovisco Pais, 1049-001 Lisboa, Portugal; Centro de Biomedicina Molecular e Estrutural,
d
Universidade do Algarve, Campus de Gambelas, 8005-139 Faro, Portugal; Universidad de Barcelona,
Departamento de Química Inorgánica, Martí i Franquès 1-11, 08028-Barcelona, Spain; e Química Inorganica
e Radiofarmacêutica, Instituto Tecnológico e Nuclear, Estrada Nacional 10, 2686-953 Sacavém, Portugal
f
Centro de Ciências Moleculares e Materiais, Faculdade de Ciências – Univ. Lisboa, Campo Grande 1749-
016 Lisbon - Portugal;
Inorganic nucleases are inorganic compounds which have demonstrated activity in DNA
cleavage, as is the case of some vanadium complexes1,2. In previously reported cases of DNA
cleavage by vanadium complexes, this activity must be initiated by an activating agent, usually
an oxidant (KHSO3, H2O2), or UV radiation. Studies of nuclease activity are carried out at
micromolar metal concentrations, at which metal speciation is unknown. Our objective is to
determine which species are actually active towards DNA cleavage.
We are particularly interested in analysing the nuclease activity of vanadium compounds that
have been proposed as therapeutic agents for diabetes mellitus, due to their known insulin-like
properties. Evaluating the possibility and extent of DNA damage is an important preliminary
step when considering these new therapeutic compounds. We compared the nuclease activity of
several insulin-mimetic vanadium complexes.
VO(acac)2 (1) is a known insulin-mimetic compound which shows a remarkably high nuclease
activity in the apparent absence of activation by radiation and oxidizing or reducing agents. In
order to understand this process, derivatives 2 – 6 were prepared and their nuclease activity
was studied by plasmid gel electrophoresis, atomic force microscopy and circular dichroism.
H2N NH2 N N
O O O O
O O O O O O O O
V V V V
O O O O O O O O
1 2 3 4
O
O O
O V
O O
V O O
O O
5 6
It is concluded that VO(acac)2 and derivatives are very efficient DNA cleavers. Unlike all
previously reported cases of vanadium nucleases, except for vanadium phenanthroline
complexes, VO(acac)2 complexes require no activating agents to degrade DNA. It is proposed
that the bichelated complexes, or possibly their monochelated equivalents, interact directly with
DNA to promote cleavage.
Acknowledgements: The authors wish to thank the Fundação para a Ciência e Tecnologia, FEDER, POCI
2010 and PPCDT/QUI/56949/2004 for financial support.
[1] Q. Jiang, N. Xiao, P. Shi, Y. Zhua, Z. Guoa, Coord Chem Rev 251 (2007) 1951-1972
[2] D.C.Crans, J.J. Smee, E. Gaidamauskas, L.Yang, Chem. Rev., 104 (2004) 849-902

Oral lectures O38
Vanadium Haloperoxidases as versatile biological matrix:

Mechanistic aspects towards cofactor and substrate specificity
Winfried Plass
Institut für Anorganische und Analytische Chemie, Friedrich-Schiller-Universität Jena,

Carl-Zeiss-Promenade 10, 07745 Jena, Germany; email: sekr.plass@uni-jena.de
Vanadium haloperoxidases (V-HPOs) are enzymes capable of the two electron oxidation of
halides and organic sulfides. The x-ray structure of the resting state and peroxide bound forms
of the enzyme have been previously reported and indicate that their general reactivity is
governed by the hydrogen bonding network provided by the protein matrix.1 Implications of this
hydrogen bonding network on the structure of the resting state have been deduced, indicating a
two-fold protonation in the resting state of the enzyme.2,3 Nevertheless, the mode of action for
the formation of the initial peroxo species still remains unclear as to what extend a dissociative
or an associative mechanism is employed in the catalytic cycle of the enzyme.
Experimental, spectroscopic and computational methods are employed to understand the

reactivity appropriate model systems,4,5,6 with special emphasize on the modeling of hydrogen
bonding interactions and the formation of peroxo species. Attempts to rationalize the cofactor
and substrate specificity will be discussed.
[1] R. Wever, W. Hemrika in Handbook of Metalloproteins, Vol. 2 (Eds.: A. Messerschmidt, R. Huber, T.

Poulos, K. Wieghardt), John Wiley and Sons Ltd., Chichester, 2001, pp. 1417–1428.
[2] M. Bangesh, W. Plass, J. Mol. Struct. Theochem 725 (2005) 163-175.
[3] W. Plass, M. Bangesh, S. Nica, A. Buchholz, ACS Symp. Ser. 974 (2007) 163-177.
[4] I. Lippold, H. Görls, W. Plass, Eur. J. Inorg. Chem. (2007) 1487–1491.
[5] S. Nica, A. Buchholz, M. Rudolph, A. Schweitzer, M. Wächtler, H. Breitzke, G. Buntkowsky, W. Plass,
Eur. J. Inorg. Chem. (2008) 2350–2359.
[6] A. Schweitzer, T. Gutmann, M. Wächtler, H. Breitzke, A. Buchholz, W. Plass, G. Buntkowsky, Solid State
Nucl. Magn. Reson. (2008) doi:10.1016/j.ssnmr.2008.02.003.

O39 Oral lectures
Vanadium Haloperoxidases – a biocatalyst for iodination reactions
Marisa Nicolaia, Gisela Gonçalvesb, Filipe Natálioc, Marise Almeidad,

Madalena Humanesa
a
Centro de Química e Bioquímica do Departamento de Química e Bioquímica da Faculdade de Ciências da
Universidade de Lisboa, Edifício C8, Campo Grande, 1749-016 Lisbon, Portugal.
b
Centro de Química Estrutural, IST, TU, Av. Rovisco Pais, 1049-001 Lisbon, Portugal.
c
Institut für Physiologische Chemie, Abteilung Angewandte Molekularbiologie, Mainz Universität,
Duesbergweg 6, D-55099 Mainz, Germany.
d
UICOB- Faculdade de Medicina Dentária de Lisboa, Cidade Universitária, 1649-003 Lisbon, Portugal,
email: marise.almeida@fmd.ul.pt
The iodinated compounds are recognized for many years as important and versatile
intermediates in organic synthesis. Their applications cover several processes as diverse as
nucleophilic displacement and radical or transition metal mediated coupling reactions. The
synthesis of iodinated compounds is often carried out using elemental iodine but due to its low
electrophilicity, an extra increment of reactivity is necessary what is usually accomplished by a
solvent, an acid and more recently by the introduction of several oxidation systems1. The
discovery of enzymes that are able to catalyze halogenation reactions which containing
vanadium as active site was a breakthrough in the biocatalysis field. Here, we show the high
versatility of the reactions performed by the vanadium haloperoxidase (V-HPO) extracted from
the brown algae Laminaria saccharina, at the expense of hydrogen peroxide and in the presence
of iodide and several aminoacids and related molecules.
We have previously demonstrated that this enzyme catalysed the conversion of L-tyrosine to
the iodotyrosine derivatives, monoiodo- and diiodotyrosine and it can also acts directly upon
monoiodotyrosine producing the diiododerivative. The kinetic data suggest, for the
monoiodotyrosine formation, a sequential mechanism for the binding of the two substrates
(hydrogen peroxide and iodide). The experimental data also support the existence of an L-
tyrosine binding site in the enzyme2.
The versatility of this enzyme is demonstrated since a totally different reaction was obtained
when the V-HPO catalyse the peroxidative iodination of the amino acid L-DOPA. A melanin type
black precipitate was obtained. The reaction is a multistep one with a crucial role developed by
the iodide as in the initial quinone formation, which is supported by similar results with cathecol
and guaiacol, as well as in the subsequent enzyme catalysed peroxidative production of
dopachrome, a well known intermediate in the synthesis of melanin. Dopachrome is then
converted to a synthetic form melanin3. This black precipitate, characterized by FT-IR and XPS
and SEM shows some similar properties to the commercially available melanin.
The reaction with epinephrine was also studied showing some similarities with the reaction with
L-DOPA, except that no black precipitate was observed.
Other amino acids such as L-phenylalanine, L-hystidine and L-tryptophan were also studied in
this context, but at a preliminary level. They showed quite distinct reactional behaviour when
compared with L-tyrosine and L-DOPA.
Despite their evident synthetic utility, the production of iodinated compounds, specially
containing aromaticity, remains a synthetic challenge. The demand for efficient, tuneable and
ecofriendly procedures are still ongoing development1. In this context, V-HPO from L. saccharina
revealed a significant contribution due to its intrinsic and interesting features, e.g., its capability
to catalysed iodination reactions with a high operational stability.
[1] G. David, C. Boyer, J. Tonnar, B. Ameduri, P. Lacroix-Desmazes, B. Boutevin, Chem. Rev. 106 (2006)
3936-3962.
[2]- M.Almeida, C. Duarte, A. Alexandre, M. Humanes, J.J.R. Fraústo da Silva J. Inorg. Biochem. 86 (2001)
321.
[3] S. Ito, K. Wakamatsu, Photochem. Photobiol. 84 (2008) 582-592.

Oral lectures O40
Directed evolution of Vanadium Chloroperoxidase: a mutant with high

bactericidal activity at alkaline pH
Rokus Renirie,a Zulfiqar Hasan,a Anny de Wilde,b Christel Pierlot,c Didier Hober, b
Jean-Mary Aubry,c and Ron Wevera
a
Van ′t Hoff Institute of Molecular Sciences, University of Amsterdam, The Netherlands
Amsterdam, Nieuwe Achtergracht 129, 1018 WS Amsterdam, The Netherlands. bDépartement Universitaire
de Microbiologie. Faculté de Médecine UPRES-EA3610, Universite de Lille 2, Laboratoire de Virologie, Lille,
France, cLCOM, Equipe ‘Oxydation et formulation’, UMR CNRS 87009, ENSCL, Villeneuve d’Ascq, France,
email: rwever@science.uva.nl
Vanadium haloperoxidases (VHPO’s) catalyze the oxidation of halides to hypohalous acids (Eqn.
1), an industrially interesting reaction: these enzymes can be used to halogenate various
organic compounds (Eqn. 2). In addition they may provide an alternative biocide in antifouling
applications, or may be used as a component in disinfectants and in detergent-formulations for
bleaching purposes.
H2O2 + X- + H+ → HOX + H2O [1]
HOX + AH → AX + H2O [2]
X = Cl, Br, I and A = organic nucleophilic acceptor
The major drawback of the VHPO’s is that they are mainly active at mildly acidic pH values,
whereas for many applications activity at mildly alkaline pH values is required. In this study we
have used directed evolution techniques on vanadium chloroperoxidase from the fungus
Curvularia inaequalis to increase its brominating activity at mildly alkaline pH. After successful
expression of the enzyme in Escherichia coli, two rounds of screening and selection, saturation
mutagenesis of a ‘hot spot’ and rational recombination, a triple mutant (P395D/L241V/T343A)
was obtained that showed a 100-fold increase in activity at pH 8 (kcat = 100 s-1). The
brominating activity at pH 5 was increased by a factor of 6 (kcat = 575 s-1) and the chlorinating
activity at pH 5 by a factor of 2 (kcat = 36 s-1), yielding the ‘best’ vanadium haloperoxidase
known thus far. The mutations are in the first and second coordination sphere of the vanadate
cofactor and the catalytic effects suggest that fine-tuning of residues Lys353 and Phe397, along
with addition of negative charge or removal of positive charge near one of the vanadate
oxygens, is very important. Lys353 and Phe397 were previously assigned to be essential in
peroxide activation and halide binding. The antimicrobial activity of the triple mutant obtained
(P395D/L241V/T343A) was investigated at pH 8 and the activity of this mutant and its wild type
counter part was compared towards the Gram-negative Pseudomonas aeruginosa and the
Gram-positive Staphylococcus aureus. Strong microbial reduction was observed and the
bactericidal activity was three to six order of magnitude higher than the wild type enzyme. The
observed activity is an important step forward in the application of this robust enzyme as a
component in disinfection formulations.
[1] Z. Hasan, R. Renirie, R. Kerkman, H.J. Ruijssenaars. A.F. Hartog and R. Wever, J. Biol. Chem. 281
(2006) 9738-9744
[2] R. Renirie, A. Dewilde, C. Pierlot, R. Wever, D. Hober, and J.-M.Aubry, J. Appl. Microbiol.(2008)
doi:10.1111/j.1365-2672.2008.03742.x

O41 Oral lectures
Vanadium containing Bromoperoxidase – Insights into the enzymatic

mechanism using X-ray crystallography
Jennifer Littlechild
Henry Wellcome Building for Biocatalysis, School of Biosciences, University of Exeter, Exeter, EX4 4QD, UK
email: JALittle@exeter.ac.uk
The vanadium bromoperoxidase enzymes from two members of the red algal species, Corallina,
have been studied in detail at a structural level1,2. These enzymes forms a large dodecameric
structure with 12 protein subunits each containing vanadium V which is essential for its activity.
The structural information has allowed an understanding of the halide specificity of the enzymes
and a mutant enzyme has been constructed which also has chloroperoxidase activity3. The
crystal strucure of this mutant protein has been determined and differences in the active site
will be discussed in the context of its altered halide specificity.
With knowledge of the overall structure of the dodecameric enzyme an active mutant dimeric
enzyme has been made where a substantial portion of the N-terminus of each monomer has
been deleted4. This enzyme can be over-expressed in Escherichia coli in the soluble fraction
whereas the dodecameric form is only overexpressed as inclusion bodies. However it has been
possible to refold this fraction in vitro to produce an active dodecameric form that resembles the
wild type enzyme isolated from the Corallina species5.
Structural studies in the presence of potential substrates of the bromoperoxidase enzyme have
demonstrated that the substrates do bind to a site close to the active site of the enzyme and
that the binding site of the halide can be located close to the vanadate in the active site. The
binding of the halogen involves the displacement of a specific leucine amino acid residue
towards the incoming ion to establish a hydrophobic interaction, excluding solvent from the
active site cavity. This is accompanied by the rotation by 25 degrees of a nearby phenylalanine
residue. In the non-halide bound structure the positions of the halogen and the leucine are
occupied by water. Once the halide is bound this is accompanied by exclusion of solvent and a
reduction in the entrance to the active site6.
Figure 1. Bromine in the active site of the vanadium haloperoxidase enzyme, shown as a sphere bound
between the vanadate and residue Arg397 at a H-bonding distance of 2.8-3.1Å.
These studies have increased our understanding of the structure of the bromoperoxidase
enzymes and the role of the vanadium which is essential for the enzymatic mechanism.
Acknowledgements: The author would like to thank the BBSRC UK for their help and financial support.
[1] M. Isupov, A. Dalby, A. Brindley, T. Izumi, T. Tanabe, and J.Littlechild, J. Mol. Biol., 299,(2000) 1035-
1049.
[2] J. Littlechild and E. Garcia-Rodriguez Coordination Chemistry Reviews, 237, (2003) 65-76.
[3] T. Ohshiro, J. Littlechild, E. Garcia-Rodriguez and M. Isupov, Y. Iida , T. Kobayashi and Y. Izumi, Protein
Science 13, (2004) 1566-1571
[4] E. Coupe, R. Hall and J. Littlechild, Protein Engineering, 2008, manuscript in preparation.
[5] E. Coupe, M.G. Smyth, A. Fosberry, R. Hall and J. Littlechild, Protein Expression and Purification 52,
(2007) 265-272
[6] E. Garcia-Rodriguez, PhD thesis Exeter, 2005

Oral lectures O42
The organizers
are sorry that
no Title or Abstract
are available
for this
Lecture

O43 Oral lectures
Crystallographic statistical studies of the decavanadate anion: toward

a prediction of the non-covalent interactions.
Anne Spasojević-de Biré,a Nada Bosnjaković-Pavlović,a,b Nour Eddine Ghermani,a,c
a
Laboratoire SPMS UMR CNRS 8580, Ecole Centrale Paris, 92295 Châtenay-Malabry, France
b
Faculty of Physical Chemistry, University of Belgrade, P.O.Box 137, 11001 Belgrade, Serbia
c
Laboratoire de Physique Pharmaceutique UMR CNRS 8612, Faculté de Pharmacie, 92296 Châtenay-Malabry,
France, email :anne.spasojevic@ecp.fr
A large number of crystal structures containing the [V10O28 Hx]6-x anion has already been
published. We have retrieved from the inorganic database (ICSD), the organic-organometallic
database (CSD), the protein data base (CSD) and an extensive bibliographic search has lead to
about 100 different structures. From a geometric point of view, the decavanadate anion appears
very rigid with really small variations in interatomic distances or bond angle values.
In a previous study1, we have experimentally determined the electron and electrostatic
properties of Na3V10O28(C4N3OH5)3(C4N3OH6)3 ·10H20. From these results we have predicted the
preferential non-covalent interactions (figure 1) with the different oxygen atoms of the
decavanadate anion. These predictions are confirmed, in this study, by the observation of the
non-covalent interactions existing in the almost 100 crystalline structures found in the
literature. The non-covalent interactions are strongly different depending on the oxygen atom
type. The Ob and Oc oxygen atoms, for which the electrostatic potential in the vicinity have the
lowest value, are involved mainly in the strong O-H…O, N-H…O while Of or Og are mainly
involved in weakest hydrogen bonds such as C-H…O or cation interactions. The cation with the
highest positive charge forms a coordination polyhedron with the water molecule. The less
positive cation includes the decavanadate anion in its coordination polyhedron. This occurs
generally with the Of oxygen atom. The main protonation sites for the protonated decavanadate
anion are Ob and Oc.
These results are important in the context of the various biological applications of the
decavanadate such as, for example, inhibition of the Ca2+ ATPase2, myosin ATPase3, and new
development in insulin mimetic4.
Figure 1. Schematic representation of the main expected non-covalent interactions with a decavanadate
anion.
[1] N.E. Ghermani, N. Bosnjaković-Pavlović, I. Tomaz, N. Bouhmaida, F. Avecilla, A. Spasojević-de Biré, U.

Mioc, and J.Costa Pessoa, 6th International Vanadium Symposium, 17-19 July 2008, Lisboa, Portugal
[2] D.L. Stokes, N.M. Green, Biophys. J. 78 (2000) 1765-1776
[3] T. Tiago, P. Martel, C.G.Merino, M. Aureliano, Bioch. Bioph. Acta 1774 (2007) 474-480
[4] S. Garcia-Vicente, Yraola F., L. Marti L., E. Gonzalez-Munoz, M.J. Garcia-Barrado, C. Canto, A. Abella, S.
Bour , R. Artuch, C. Sierra, N. Brandi, C. Carpéne, J. Moratinos, M. Camps, M. Palacin, X. Testar, A. Guma,
F. Alberici, M. Royo, A. Mian, A. Zorzano, Diabetes, 56 (2007) 486-493

Oral lectures O44
Influence of polydentate ligands in the structure of dinuclear V(V)

compounds
Fernando Avecilla,a Pedro Adão,b Isabel Correiab and João Costa Pessoab
a
Departamento de Química Fundamental, Universidade da Coruña, Campus da Zapateira s/n, 15071, A
Coruña, Spain. email: avecil@udc.es
b
Centro de Química Estrutural, Instituto Superior Técnico, TU Lisbon, Av. Rovisco Pais,
1049-001 Lisboa, Portugal
A variety of vanadium complexes have been introduced as structural and/or functional models
for biologically active vanadium compounds.[1] Schiff base complexes with functional amine
groups constitute a specific subfamily within this group.
A wide range of asymmetric Schiff base compounds containing primary amine functions can be
prepared in one step by the reaction of corresponding aldehyde and the appropriate diamine.
Although the initial mixture contain VIV and Schiff base ligands, a VV complex with the half
Schiff-base monoanionic ligand were obtained in some cases, where one of the imine bonds
hydrolyzed.[2] The oxidation of VIV was probably due to diffusion of air into the solution. The
resulting VO2L complexes contained tridentate ligands with phenolate, imine, and amine
coordination to the dioxovanadium(V) ion. X-ray structures of these compounds demonstrate
that they form dimers in the solid state with a V2O4 core, which is in equilibrium with the
monomer in solution.
There have been many O-bridged dinuclear vanadium (IV and/or V) complexes the structures of
the which have been determined by X-ray diffraction, although those involving the OVV(μ-O)VVO
unit (V2O3 core) with tridentate or tetradentate ligands are relatively rare.[3] Water molecules
can block the second μ-O bridge such as in the complex [{VO(van-L-ser)H2O}2-μ-O],[4] but this
effect can be exercised by the ligand itself when it acts as polydentate.
We present the structures of a series of dinuclear vanadium complexes with Schiff base and
functional amine ligands. This work illustrates the high propensity of the vanadium center to
increase its coordination number via dimerization of two pentacoordinate monomers if the steric
control exercised of the ligands allow it.
Acknowledgements: The authors thank FEDER, Fundação para a Ciência e a Tecnologia, POCI 2010
[1] D. Rehder, Coord. Chem. Rev. 1999, 182(1), 297-322.

[2] I. Correia, J. Costa Pessoa, M. T. Duarte, R. T. Henriques, M. F. M. Piedade, L. F. Veiros, T. Hakusch, T.
Kiss, A. Dörnyei, M. M. C. A. Castro, C. F. G. C. Geraldes and F. Avecilla, Chem. Eur. J. 2004, 10, 2301-
2317.
[3] I. Cavaco, J. Costa Pessoa, M. T. Duarte, R. T. Henriques, P. M. Matias and R. D. Gillard, J. Chem. Soc.,
Dalton Trans., 1996, 1989-1996.
[4] C. Grüning, H. Schmidt and D. Rehder, Inorg. Chem. Commun. 2, 1999, 57-59.

O45 Oral lectures
Hexavanadate core and discovery of double stranded octadecavanadate
Yoshihito Hayashi, and Kiyoshi Isobe
Departament of Chemistry, Graduate School of Natural Science, Kanazawa University,

Kanazawa 920-1192, Japan
email: hayashi@kenroku.kanazawa-u.ac.jp
The chemistry of polyoxovanadates have been explained by the equilibrium between

metavanadate and decavanadate which has a structure with fused hexavanadate, one of the
well-established hexametalate core in polyoxometalate chemistry. The growing process that
turns monovanadate into decavanadate, are not fully rationalized in terms of step-by-step
reaction mechanisms, and there are certain possibilities of an involvement of un-realized
intermediate such as hexavanadate in those processes. In vanadate chemistry, the negative
charge build up through the formation of hexavanadate may result in the failure of isolation.
The efforts to isolate the hexavanadate core had been established by the introduction of
protecting ligand such as organometallic groups or multidentate-alkoxo ligands for
compensation of the build up negative charge. In this study, we disclose a simple method to
synthesize a hexaalkoxohexavanadate from the infinite vandate sheets. The hexavanadate was
stabilized by symmetrically coordinated hexamethoxo ligands. The hexamethoxo-hexavanadate
was unstable in terms of isomerization as well as hydrolysis reaction. By the utilization of the
hydlorytic nature of the hexavanadate core, we could condensate the units into the bowl-type
dodecavanadate in dichloromethane. The resulting dodecavanadate has unlike predecessor, no
acetonitrile template was included at the center, instead, a dichloromethane molecule was
located on top of the open mouse of the bowl. In other view, we synthesized the empty bowl
which may be suitable for the insertion of the other type of template. The condensation
reaction can be viewed as the transition of two hexavanadate core into the one decavanadate
core, the 6+6 addition reaction. In this structure, the open-end of the bowl was constructed by
cyclic octavanadate. The octavanadate ring was also observed in reduced decavanadate. The
reduced decavanadate can be converted to octadecavanadate species with nitrate template.
The discovery of the octadecavanadate which has a double stranded octavanadate ribbons in
the spherical molecule capped by two square pyramidal VO5 units at the both end of the
strands, may lead a new bioinorganic vanadate chemistry. The valence state of the two
octavanadate ribbons are V(V), while the capping two VO5 pyramidal groups are V(VI). This
molecule is a pure inorganic chiral molecule, and the chirarity arose from the inorganic structure
itself. The absolute structure has been determined for a given crystal in a solid state. However,
we could not optically resolve those crystals by hand-picking, except for the crystallography
which need only one crystal. To address the question whether the inorganic chiral core is
maintained or not in a solution, we tried the structural investigations in an acetonitrile through
the XAFS studies. The XAFS absorption edge show a clear splitting according to the different
oxidation state of V(V) and V(VI). The EXAFS interpretation supports the existence of DNA-like
inorganic molecule in a solution. The vanadium K-edge signals of a solid state sample and a
sample in acetonitrile has an close match. The corresponding Fourier transform also show close
match through the region less than 2.8 Å which are attributable to V=O, V-O and V-V distances,
but 3-4 Å region show a slight shifts.
Figure 1. Polyhedral representation of double stranded octadecavanadate. Capped square-pyramidal V(VI)

group are showed in hatched pyramid, the octavanadate ribbons are represented as a gray ribbon and a
white ribbon. Both ribbon are constructed by the edge sharing of eight VO5 pyramids.

Oral lectures O46
Structural and electrostatic properties of a decavanadate-cytosine

co-crystallized complex
Nour Eddine Ghermani,a,f Nada Bosnjakovic-Pavlovic,a Isabel Tomaz,b Nouzha

Bouhmaida,c Fernando Avecilla,d Anne Spasojević-de Biré,a Ubavka Mioce and
João Costa Pessoab
a
Ecole Centrale Paris, Laboratoire SPMS UMR CNRS 8580 1, Grande Voie des Vignes
92295 Châtenay-Malabry, France
b
Centro de Quimica Estrutural, Instituto Superior Tecnico, TU Libon,
Av. Rovisco Pais, 1049-001 Lisboa, Portugal
c
Laboratoire des Sciences des Matériaux, LSM, Université Cadi Ayyad, Faculté des Sciences Semlalia,
Boulevard Prince Moulay Abdallah, BP 2390, 40000 Marrakech, Morocco
d
Departamento de Química Fundamental, Facultad de Ciencias, Universidade
da Coruña, Campus da Zapateira s/n, 15071 A Coruña, Spain
e
f
Laboratoire de Physique Pharmaceutique UMR CNRS 8612, Faculté de Pharmacie 5 rue Jean-Baptiste
Clément, 92296 Châtenay-Malabry, France ; email: noureddine.ghermani@u-psud.fr
Polyoxometalates (POM’s) of general formula: H6-xAxM10O28⋅nH2O, (A = K, Na, M = W, V, n = 0-

30) crystallize with a various (generally large) number of water molecules. The primary
structure of POM’s is formed by polyanions, whereas the secondary structure corresponds to an
arrangement of interacting polyanions, cations, protons and water molecules. The interest on
POM’s recently increased due to their medicinal applications (antiviral and antitumoral activity).
Since the biological properties result from interactions with viral enzymes or with viral cell
envelope, the understanding of these interactions at a molecular level is essential for the
interpretation and the development of potent compounds with selective enzymatic affinity.
For a better understanding of these interactions, accurate structure determinations from a
single-crystal X-ray diffraction experiment are more than necessary. In our investigations,
among the polyoxometalate compounds, we focused on the study of polyoxovanadates (POV’s);
vanadium being less toxic than tungsten in biological mediums. POV’s interact with biomolecules
with various and versatile activities (enzymes inhibitor or activator). For example, POV’s inhibit
many phosphate-metabolizing enzymes like kinases [1], phosphorilases [2], Ca2+ ATP-ase [2],
aldolase.
In this context, the decavanadate-cytosine complex Na3V10O28(C4N3OH5)3(C4N3OH6)3 ·10H20
has been synthesized and its crystal structure has been determined from a single-crystal X-ray
diffraction experiment at different temperatures. At room temperature, the crystal structure is
dominated by an extensive network of hydrogen bonds involving the protonation-deprotonation
of the cytosine molecules. We have observed a phase transition occurring below 200K from P-1
to P1 space group due to the protonic stabilization of one cytosine molecule in the unit cell. A
high resolution X-ray diffraction experiment at 210K (in P-1 space group phase) was carried
out. The data were refined using a pseudo-atom multipole model [3] in order to obtain the
charge density distribution and the electrostatic properties of the decavanadate-cytosine DNA
base complex. The nature of interactions between decavanadate anions and the cytosine base
were carefully highlighted and analyzed.
[1] D.W.Boyd, K.Kustin, M.Niwai, Biochim. Biophys.Acta (1985) 827, 472-475.

[2] P. Csermely, A. Martonosi, G.C. Levy and A.J. Ejchart, Biochem.J (1985) 230, 807-815.
[3] N. Hansen, P. Coppens, Acta Crystallogr. (1978) A34, 909-921.

O47 Oral lectures
A new oxo-Vanadium complex employing an imidazole rich tripodal

ligand
Octávio A. C. Antunes, Tatiana L. Fernandez, Lorenzo C. Vinsetin and

Marciela Scarpellini
Departamento de Química Inorgânica, IQ/UFRJ, Av.Athos da Silveira Ramos, 149, Rio de Janeiro,
RJ, Brazil, email: octavioantunes@terra.com.br
Vanadium complexes have been investigated for several applications including biomimetic
model compounds, insulin mimics and catalysts. Aiming to develop new vanadium catalysts for
oxidation processes we have used the imidazole rich tripodal ligand BMIMAPY1, [(bis(1-
methylimidazol-2-yl)methyl)(2-(pyridyl-2-yl)ethyl)amine]. The reaction of stoichiometric
amounts of BMIMAPY, [VO(acac)2] and NaClO4, in methanol, afforded slightly violet single
crystals of [VO(acac)(BMIMAPY)]ClO4 suitable to X-ray analysis. The crystal structure (Figure 1)
reveals a mononuclear oxovanadium cation complex in a distorted octahedral geometry. The
two imidazole nitrogen atoms and the two oxygen atoms from the acac ligand comprise the
equatorial plane, in an arrangement where the atoms of the same nature are cis to each other.
Completing the coordination sphere are the tertiary amine nitrogen atom and one oxygen at
1.590 (4) Å, indicating the oxo character of the bond. It is also observed that the pyridine group
stays uncoordinated.
Figure 1. Ortep view of the cation complex [VO(acac)(BMIMAPY)]+.
The infrared spectrum of the complex [VO(acac)(BMIMAPY)]ClO4 presents typical bands of the
ligand skeletal overloaded with those from the acac coordinated in a bidentate mode. It is also
observed two strong bands at 1092 cm-1, typical of the perchlorate anion, and at 990 cm-1
tentatively attributed to the stretching of the V=O bond. Analytical calculated for VC22H32ClN6O7
(found): C, 45.64 (45.06); H, 5.57 (5.28); N, 14.52 (14.07).
Electronic spectrum recorded in acetonitrile solution (1x10-2 molL-1) shows two weak bands at
736 nm (ε = 30 mol-1Lcm-1) and 547 nm (ε = 10 mol-1Lcm-1) assigned to d-d transitions.
The redox behavior of [VO(acac)(BMIMAPY)]ClO4 is under investigation by cyclic voltammetry,
and the results will be presented.
Acknowledgements: The authors would like to thank Faperj and Capes for their help and financial support.
[1] M. Scarpellini et al. Inorg. Chim. Acta 357 (2004) 704-715.

Oral lectures O48
Oxovanadium(V) compounds with bis(hydroxyamino)-triazines:

Synthesis, structural, and physical studies
Vladimiros A. Nikolakis,a John T. Tsalavoutis,b Michael P. Sigalas,b Marios Stylianou,c

Evgenios Evgeniou,c Artem Melman,d Tamas Jakusch,e Tamas Kiss,e Anastasios D.
Keramidas,c and Themistoklis A. Kabanosa
a
Department of Chemistry, Section of Inorganic and Analytical Chemistry,
University of Ioannina, 45110 Ioannina, Greece.
b
Department of Chemistry, Laboratory of Applied Quantum Chemistry,
Aristotle University of Thessaloniki, 54124 Thessaloniki, Greece,
c
Department of Chemistry, University of Cyprus, 1678 Nicosia, Cyprus
d
The Institute of Chemistry, The Hebrew University of Jerusalem, Givat Ram, Jerusalem 91904, Israel,
e
Department of Inorganic and Analytical Chemistry, Attila Joszef University, Szeged, Hungary.
Bis-(hydroxyamino) triazines constitute a new, general and highly versatile group of

tridentate vanadium(V) chelating agents exhibiting higher affinity to vanadium(V) than
other tridentate vanadium(V) chelators. Two vanadium(V) compounds of
hydroxyamino-1,3,5,-triazine ligand 1,2 were synthesized and characterized both in
solution and in the solid state. Compound 2 is very stable in a large region of the pH
scale, from 2.0 to 11.5, as it was evidenced by multinuclear NMR and potentiometric
studies.
1 2
Acknowledgement. This research is part of the PENED03 research project, implemented within the
framework of the “Reinforcement Program of Human Research Manpower” (PENED) and co-financed by
National and Community Funds (25% from the Greek Ministry of Development-General Secretariat of
Research and Technology and 75% from E.U.-European Social Fund).

O49 Oral lectures
Ring-substituted vanadocene(IV) and molybdenocene(IV) complexes
Jan Honzíček,a Carlos C. Romãoa and Jaromír Vinklárekb
a
Instituto de Tecnologia Química e Biológica da Universidade Nova de Lisboa, Av. da República, EAN, 2780-
157, Oeiras, Portugal, email: hohonza@post.cz; b The Department of General and Inorganic Chemistry,
University of Pardubice, nám.Čs. Legií 565, 532 10 Pardubice, Czech Republic.
Among other applications, bent metallocene complexes of the type [Cp2MCl2] (M = Ti, V, Nb,
Mo) have also been investigated for biological applications ever since their antitumor activity
was discovered.[1] Due to the particular requirements of such applications considerable attention
has been given in the last few years to the synthesis of modified complexes.[2] Substitution of
halide ligands leaves the “Cp2M” moiety unchanged and the properly chosen substituents can
help overcoming some problems that complicate application of the parent compounds such as
low water solubility or biological incompatibility. However, modification of the Cp rings seems to
be a more promising approach for solving the above-mentioned problems. Such modification
enables the fine tuning of cytostatic properties. Moreover, it allows the introduction of reactive
groups that offer an anchor to append biologically active molecules capable of directing the final
complex to the target receptors or diseased tissues.
Ring-substituted vanadocene compounds were prepared using the reaction between (acac)2VCl
and MgCl salt of appropriate substituted cyclopentadiene (Cp’MgCl). The obtained monochloride
complexes (Cp’2VCl) were then oxidized to desired dichlorides (Cp’2VCl2). This method is
suitable for synthesis of symmetrically disubstituted (Cp’2VCl2) and ansa-bridged vanadocene
compounds (A-(C5H4)2VCl2), see Fig.1b, c. Compounds containing amines and ethers in the side
chain were prepared using this pathway.
Molybdenocene compounds were prepared using multistep route starting from allyl complex
[(η3-C3H5)Mo(CO)2(NCMe)2Cl]. Subsequent bonding of Cp ring together with mild reaction
conditions enable to assembly of the Cp’CpMo moiety containing ether and carboxylic acid ester
function groups in the side chain (Fig.1a). This route is even suitable for synthesis of
compounds with reactive function groups. Haloethyl-substituted compounds were obtained
applying ring-opening reaction of spiro[2.4]hepta-4,6-diene.[3]
a) b) c)
Figure 1. a) monosubstituted compound b) 1,1’-disubstituted compound; c) ansa-metallocene.
Acknowledgements: We are grateful to Fundação para a Ciência e Tecnologia (FCT, Portugal) for supporting
through postdoctoral project SFRH/BPD/24889/2005.
[1] H. Köpf, P. Köpf-Maier, Angew. Chem.-Int. Edit. Engl. 18 (1979) 477-478.

[2] P. M. Abeysinghe, M. M. Harding, Dalton Trans. (2007) 3474-3482.
[3] J. Honzíček, F. A. A. Paz, C. C. Romão, Eur. J. Inorg. Chem. (2007) 2827-2838.

Oral lectures O50
Vanadium catalysts for the partial oxidation of alkanes

under mild conditions
Armando J.L. Pombeiro, Telma F. S. Silva, Gopal S. Mishra, Marina V. Kirillova,

Elisabete C.B.A. Alegria, Luísa M.D.R.S. Martins, Alexander M. Kirillov, Maria F.C.
Guedes da Silva, Maxim L. Kuznetsov, António Palavra, José A.L. da Silva, João J. R.
Fraústo da Silva
Centro de Química Estrutural, Complexo I, Instituto Superior Técnico,

Av. Rovisco Pais, 1049-001 Lisboa, Portugal.
e-mail: pombeiro@ist.utl.pt
Partial oxidation reactions of saturated hydrocarbons under mild conditions are expected to
provide promising methods towards the use of such unreactive compounds as raw materials for
organic syntheses. This general aim constitutes a challenge to modern Chemistry and the field
is also of biological significance in view of the ability of a few enzymes to catalyse the partial
oxidation of alkanes.
Our initial studies by using, as a catalyst, Amavadin, a natural bare vanadium complex with a
still unknown biological role, have been extended to other vanadium catalysts which are shown
to be particularly active for the following general types of oxidation reactions:
- Peroxidative oxidations of alkanes to alcohols and ketones, typically with aqueous
hydrogen peroxide (a “green” oxidant), at room temperature.
- Oxidations of alkanes with dioxygen (the ideal oxidant) in solvent free systems, by
using supported catalysts on modified silica.
Such reactions will also be compared with alkane carboxylations leading to carboxylic acids.
Some of the V-systems provide the highest catalytic activity so far reported in the field of
alkane functionalization under mild or moderate conditions. They are compared with those
based on other metals, and plausible radical mechanisms are discussed on the basis of radical
13
trap and C-labelled experiments, and of DFT theoretical studies.
Acknowledgements: This work has been partially supported by the Fundação para a Ciência e a Tecnologia
and its POCI 2010 programme (FEDER funded).
[1] T.F.S. Silva, E.C.B.A. Alegria, L.M.D.R.S. Martins, A.J.L. Pombeiro, Adv. Synth. Cat., 2008, 350,706.
[2] G.S. Mishra, J.J.R. Fraústo da Silva, A.J.L. Pombeiro, J. Mol. Cat. A: Chem., 2006, 265, 59-69.
[3] M.V. Kirillova, M.L. Kuznetsov, P.M. Reis, J.A.L. Silva, J.J.R. Fraústo da Silva, A.J.L. Pombeiro, J. Am
Chem. Soc., 2007, 129, 10531.
[4] M.V. Kirillova, M.L. Kuznetsov, J.A.L. Silva, M.F.C. Guedes da Silva, J.J.R. Fraústo da Silva, A.J.L.
Pombeiro, Chem. Eur. J., 2008, 14, 1828.
[5] M.V. Kirillova, J.A.L. da Silva, J.J.R. Fraústo da Silva, A.F. Palavra, A.J.L. Pombeiro, Adv. Synth. Cat.,
2007, 349, 1765.
[6] M.V. Kirillova, A.M. Kirillov, P.M. Reis, J.A.L. Silva, J.J.R. Fraústo da Silva, A.J.L. Pombeiro, J. Cat., 2007,
248, 130.

O51 Oral lectures
Oxovanadium (IV) complexes of carbohydrates.

Some recent advances
Enrique J. Baran
Centro de Química Inorgánica (CEQUINOR; CONICET/UNLP), Facultad de Ciencias Exactas,

Universidad Nacional de La Plata, C. Correo 962, 1900-La Plata, Argentina
email: baran@quimica.unlp.edu.ar
Carbohydrates and their derivatives are the most abundant class of biomolecules and have a
large variety of biological functions. The interaction of these poly-functional molecules with
metal cations in living organisms is of special interest as it occurs during many important
biological processes. In particular, the interaction of carbohydrates with different vanadium
species has great relevance for vanadium biochemistry, especially in relation to its metabolism
in the higher forms of life1,2 and to its biological detoxification1-4. Therefore, it constitutes an
area of increasing research interest. In fact, most sugars can reduce vanadium (V) to
oxovanadium (IV), VO2+, and strongly complex this cation. Some years ago we analyzed the
most interesting and characteristic aspects of these complexes5. In this communication we
present some relevant results from recent studies in this field, which include:
1) Synthesis and characterization of some new oxovanadium (IV) complexes derived from a
variety of carbohydrates and related species.
2) First studies on the formation of VO2+ complexes with conduritols.
3) Spectroscopic investigation of the interaction of VO2+ with chitosan.
In all cases, the complexes were characterized by a combination of spectroscopic techniques,
including infrared, Raman and UV-visible measurements.
Acknowledgements: The author acknowledges the continuous support from the “Consejo Nacional de
Investigaciones Científicas y Técnicas de la República Argentina” (CONICET).
[1] E.J. Baran, J. Inorg. Biochem. 80 (2000) 1-10.

[2] E.J. Baran, J. Braz. Chem. Soc. 14 (2003) 878-888.
[3] E.J. Baran, In Vanadium in the Environment (J.O. Nriagu, Edit.), Vol. 2, 317-345, J. Wiley, New York
(1998).
[4] E.J. Baran, Chem. Biodivers., in the press.
[5] E.J. Baran, J. Carbohydr. Chem. 20 (2001) 769-788.

Oral lectures O52
Vanadis Awardee
Vanadium-catalyzed oxidative bromination reaction

under molecular oxygen
Toshikazu Hirao, Toshiyuki Moriuchi, and Kotaro Kikushima
Department of Applied Chemistry, Graduate School of Engineering, Osaka University, Yamada-oka, Suita,
Osaka 565-0871, Japan.
email: hirao@chem.eng.osaka-u.ac.jp
Bromination of organic compounds is one of the most important reactions in organic

synthesis. Conventional bromination involves the use of hazardous and tedious elemental
bromine. To avoid the use of bromine, an alternative environmentally friendly method is
required. From these points of view, considerable efforts have been focused on to develop an
efficient bromination reaction based on function of vanadium bromoperoxidase (VBrPO), which
is found in marine algae. We have already demonstrated the efficient bromination reaction
under relatively mild conditions by using NH4VO3 catalyst combined with H2O2, KBr, and HBr in
an aqueous media.1 This result prompted us to develop a more environmentally favorable
catalytic bromination reaction as described herein.
The oxidative bromination reaction of 1,3,5-trimethoxybenzene with 10 mol% of NH4VO3,
200 mol% of tetrabutylammonium bromide (TBAB), and 200 mol% of p-toluenesulfonic acid
monohydrate (PTS·H2O) in MeCN under oxygen smoothly proceeded to afford the corresponding
bromination product in a high conversion. In the case of α-methylstyrene as an alkene
substrate, the corresponding dibromo and bromohydrin derivatives were obtained in 100%
conversion at room temperature.
NH4VO3 10 mol%
OMe TBAB 200 mol% OMe
PTS·H2O 200 mol% Br
MeCN, O2, reflux, 40 h
MeO OMe MeO OMe
79%
NH4VO3 1 mol%
TBAB 200 mol% Br OH
PTS·H2O 200 mol%
+
MeCN, O2, rt, 6 h
Br Br
33% 62%
[1] T. Moriuchi, M. Yamaguchi, K. Kikushima, T. Hirao, Tetrahedron Lett. 48 (2007) 2667-2670.

O53 Oral lectures
Electron Paramagnetic Resonance of Vanadium(III) coordination

complexes
Jurek Krzystek
National High Magnetic Field Laboratory, Florida State University, Tallahassee, Florida, 32310 USA
email: krzystek@magnet.fsu.edu
Vanadium has long been an appealing transition metal for study due to its wide range of
oxidation states and associated beautiful colors of its complexes. Among these oxidation states,
V(III) has traditionally been less studied than V(IV) or V(V), which have better defined
biological/physiological roles. However, V(III) has recently become more intensely investigated
due to the its observation in marine organisms, namely in the blood cells of ascidians. An exotic
biological role for a given metal ion is sure to pique the interest of the inorganic community, and
if that metal ion happens to be also of the open-shell type, it will surely make an odd EPR
spectroscopist interested, too. At the same time V(III) (3d2 “non-Kramers” configuration)
complexes, which have long been considered “EPR-silent” due to the typically large zero-field
splitting in their ground spin triplet state, have now become amenable to EPR detection through
the availability of high microwave frequencies, and magnetic fields [1, 2].
Indeed, our interest in V(III) also stems from a biological role, however quite different from the
above; it is due to the presence of vanadium-containing nitrogenase (V-N2ase). An EPR study of
V(III) in this enzyme is still ahead of us; however, we concentrate on V(III) complexes with
sulfur-rich ligands that are model compounds for V-N2ase. In the course of high-frequency and -
field EPR investigations of these systems, we also realized the need for comparison studies on
complexes of V(III) with more “innocent” ligands, as complexes of sulfur donors can often
exhibit ambiguous oxidation states and are decidedly “non-innocent”. We will thus cover two
other classes of V(III) complexes containing only oxygen- and nitrogen-donating ligands:
aminocarboxylates such as EDTA and related compounds, and heterocycles. Of particular
interest to us is the relationship between magnetic properties of the investigated complexes,
and their electronic and geometric structure. Experimental investigations will be complemented
by preliminary calculations of the spin Hamiltonian parameters using DFT-related methods.
Acknowledgements: I am greatly indebted to my collaborators on this project: Joshua Telser (Roosevelt

University, Chicago, USA), Hua-Fen Hsu (National Cheng Kung University, Tainan, Taiwan) and Marcin
Brynda (University of California, Davis, USA).
[1] J. Krzystek, S. A. Zvyagin, A. Ozarowski, S. Trofimenko, J. Telser, J. Magn. Reson. 178 (2006) 174-183.
[2] J. Krzystek, A. T. Fiedler, J. J. Sokol, A. Ozarowski, S. A. Zvyagin, T. C. Brunold, J. R. Long, L. C.
Brunel, J. Telser, Inorg. Chem. 43 (2004) 5645-5658.

Oral lectures O54
Structure and spectroscopic properties of new VIV/V semiquinone and

hydroquinone complexes
Anastasios D. Keramidas,a Chryssoula Drouza,b Marios Stylianoub
a
Department of Chemistry, University of Cyprus,1678 Nicosia, Cyprus, email: akeramid@ucy.ac.cy;
b
Department of Agriculture Production, Biotechnology and Food Science, Cyprus University of Technology,
3603, Limasol, Cyprus, email: Chryssoula.drouza@cut.ac.cy
The investigation of the association between the electron and proton transfer in the metal ion -
hydroquinone/semiquinone/quinone interacting systems is particularly important in order to
understand the factors which regulate the redox potentials and the pathways in electron
transfer reactions between transition metal centers and p-semiquinone radicals. The interaction
of p-hydroquinones with vanadium in high-oxidation states presents additional interest due to
[1]
the participation of vanadium in redox reactions in biological systems such as the reduction of
[2, 3]
vanadium(V), present in sea water, to vanadium(III) in the blood cells of tunicates .
Our focus in this work is on the synthesis and characterization in solid state and solution of
stable complexes of vanadium with p-semiquinonate radicals as well as the investigation of the
H+ induced electron transfer between the VIV/VV metal centers and the coordinated
semiquinonate/hydroquinonate ligands. Substituted hydroquinones with chelate groups
(Scheme 1) were used to stabilize vanadium complexes. The VIV/VV –
semiquinonate/hydroquinonate tetranuclear and dinuclear species produced from this electron
transfer were isolated from aqueous or acetonitrile solutions and the oxidation states of the
ligand were indisputably determined by X-ray crystallography. UV-Vis and NMR spectroscopies
and electrochemistry were employed for the investigation of the speciation and redox properties
of these complexes in aqueous solution.
Scheme 1. Hydroquinone ligands.
Acknowledgements: The authors would like to thank PRF of Cyprus (TEXNO/0506/19) for their financial
support .
[1] D. Rehder, Coordination Chemical Reviews 182(1999) 197.

[2] P. Frank, P., K.O. Hodgson, Inorganic Chemistry 39(2000) 6018.
[3] C. Drouza, V. Tolis, V. Gramlich, C. Raptopoulou, A. Terzis, M.P. Sigalas, T.A. Kabanos, A.D. Keramidas,
Chem. Commun. (2002) 2786.

O55 Oral lectures
Vanadium coordination complexes with the [CpP(OEt,OEt)Co]- ligand :

Towards catalysis
Craig C. McLauchlan, Michael P. Weberski, Jr.
Department of Chemistry, Illinois State University, Normal, IL 61790-4160 USA,

email: ccmclau@ilstu.edu
Broadly stated, my laboratory is interested in vanadium coordination chemistry. In the course

of our investigations of vanadium-containing compounds for use as potential oxidation catalysts,
we have generated a series of metal coordination complexes with tridentate ligands that
effectively oxidize catechols to quinones. We recently communicated some of the preliminary
work focusing on complexes with the [CpP(OEt,OEt)Co]- ligand, specifically
(OEt,OEt)
[CpP Co]VCl2(DMF), 1, where DMF is N,N-dimethylformamide.1 Here we discuss the
reactivity of 1 and clarify the products produced. X-ray structural analysis has allowed us to
positively identify products 5-7 in the shown reaction scheme, but crystallization of complexes
2-4 remain elusive. These octahedral vanadium(III) phosph(on)ate cluster complexes with a
V4P4O12core can be synthesized by varying the phosphonate salt used (RPO(O)2, R = Me, tBu,
Ph). In a parallel project more focused on bioinorganic chemistry, we are also investigating
complex 1 for its alkaline phosphatase inhibition properties using enzyme kinetics studies. Our
most recent results will be presented here.
Figure 1. Reactivity scheme for CpP(OEt,OEt)Co]VCl2(DMF), 1.
Acknowledgements: The authors would like to thank the National Science Foundation (U.S., CHE-0645081)
and the American Chemical Society- Petroleum Research Fund (46064-B3) for financial support.
[1] M. P. Weberski, Jr., C. C. McLauchlan, Inorg. Chem. Commun. 10 (2007) 906-908.

Oral lectures O56
Bio-inspired synthesis of bionanocomposites elastomers via a complex

coacervation process between gelatin and decavanadates
Florent Carn,a Olivier Durupthy,a Nathalie Steunou,a,* Thibaud Coradin,a,* Madeleine

Djabourov,b Bruno Fayolle,c François Ribot a and Jacques Livage a
a
Laboratoire de Chimie de la Matière Condensée de Paris, UPMC Univ. Paris 6, Collège de France, France,
b
Laboratoire de Physique Thermique, E.S.P.C.I., Paris, France,
c
Laboratoire d’Ingénierie des Matériaux, E.N.S.A.M. Paris, France.
*email : nathalie.steunou@upmc.fr ; Thibaud.Coradin@courriel.upmc.fr
Vanadium (V) oxide materials are well-known for their physical properties such as redox, semi-
conducting and intercalation properties. Thus, they are currently used as antistatic coatings,
cathode for Li-batteries or catalytic materials. A possible challenge consists i) in improving the
conduction, mechanical and/or intercalation properties by combination with an organic polymer
with specific functionalities and ii) in optimizing the morphology at different length scales. Such
hybrid materials with tailored morphologies can be obtained in soft reaction conditions via bio-
inspired strategies where the inorganic network growth is spatially directed by an organic
polymer. Besides, this biopolymer may improve or even induce some new physical properties.
Following this approach, we have synthesized a new vanadium oxide-gelatin hybrid material
showing a striking rubber-like elastic character (figure 1). This elastomer is formed at a
temperature higher than 25°C whereas the sol-gel transition of gelatin occurs at T<25°C.
6
a) b)
Experimental
σ = F/S0 (MPa)
4 data
2
Neo-Hookeen
behavior
0
1 2 4 6
λ
Figure 1. a) Photopraph of a decavanadate-gelatin bionanocomposite showing a rubber-like character ; b)

Cauchy stress (F/S0) as a function of the drawing ratio (λ). The red curve presented is a fit corresponding to
a neo-hookeen behavior with a rubbery modulus of 0.6 MPa.
First of all, we have studied the influence of pH, gelatin and vanadate relative concentrations on
nanocomposite formation. Then, the material structure and morphology has been fully
characterized by 51V MAS NMR, XRD, SEM, TEM while its mechanical behavior has been
quantified under tensile load.
51
V MAS NMR spectroscopy suggests that the cohesion of this hybrid material arises from
electrostatic interactions between decavanadate anions [H2V10O28]4- and positively charged
chains of gelatin.
Under aging conditions, we have observed by XRD and TEM that these interactions at the
organic-inorganic interface strongly affect the V2O5 network growth by slowing down the
condensation process and preventing the regular layers stacking in the material. Finally, we
have proposed a mechanism of formation based on an analogy with complex coacervation
process1 in good agreement with 51V NMR, DLS, rheological and calorimetric measurements.
[1] F. Carn, N. Steunou, M. Djabourov, T. Coradin, F. Ribot, J. Livage, Soft Matter, 4 (2008) 735-738.

Poster
Presentations

Poster presentations

Poster Presentations P1
DFT model studies of vanadium chloroperoxidase: dissociative or

associative enzymatic mechanism and its dependency on the degree of
protonation
Daniel Geibig, Winfried Plass
Friedrich-Schiller-Universität Jena, Institut für Anorganische und Analytische Chemie

Carl-Zeiss-Promenade 10, 07745 Jena, Germany, email: sekr.plass@uni-jena.de
It has been shown that for particular modes of action of vanadium chloroperoxidase different pH
optima are observed:1 At the one hand the enzyme shows its highest activity at pH 5.0 but on
the other hand the reaction rate of the formation of the peroxovanadate species is higher at pH
8.3. Although doubly protonated form of the vanadate cofactor is commonly accepted,2,3 it
remains unclear whether the first reaction step of the enzymatic cycle proceeds in a dissociative
or associative manner. There are molecular dynamics simulations which imply an associative
mechanism4 as well as DFT model studies suggesting a dissociative mechanism.5
The results of our DFT model studies point towards a pH dependency for the reaction
mechanism of the formation of the initial peroxovanadate species: Whereas a high degree of
protonation promotes a dissociative pathway, this kind of reaction mechanism can be ruled out
for a lower degree of protonation because of the high reaction barrier. Further studies
concerning the influence of the degree of protonation on an associative mechanism are in
progress.
Figure 1. With TURBOMOLE/RI-DFT/BP86/TZVP optimized structures of the native site (left) and the
peroxovanadate species (right).
As model system a cutout of the active site of the vanadium chloroperoxidase crystal structure
(1IDQ)6 containing the important hydrogen bonds in the direct environment of the vanadate
cofactor is utilized (see Figure 1). All heavy atoms of the backbone are fixed for maintaining the
enzymatic structure while side chains and all hydrogen atoms are free to move.
[1] R. Renirie, W. Hemrika, S.R. Piersma, R. Wever, Biochemistry 39 (2000) 1133-1141.

[2] M. Bangesh, W. Plass, J. Mol. Struct. Theochem 725 (2005) 163-175.
[3] W. Plass, M. Bangesh, S. Nica, A. Buchholz, ACS Symp. Ser. 974 (2007) 163-177.
[4] S. Raugei, P. Carloni, J. Phys. Chem. B 110 (2006) 3747-3758.
[5] G. Zampella, P. Fantucci, V.L. Pecoraro, L. De Gioia, Inorg. Chem. 45 (2006) 7133-7143.
[6] A. Messerschmidt, L. Prade, R. Wever, Biol. Chem. 378 (1997) 309-315.

P2 Poster Presentations
Anion “complexes” of diperoxo-vanadate Model compounds for

haloperoxidase enzyme?
Tamás Jakusch, Tamás Kiss
Departament of Analitical and Inorganic Chemistry Department, SZTE, H-6721 Szeged, Dóm tér 7, Hungary,
email: jakusch@chem.u-szeged.hu
The vanadium dependent haloperoxidase enzymes and their active sites are very well known.
The X-ray structures revealed that the anionic cofactor, vanadate, is mainly bound via
electrostatic interaction and a hydrogen-bond network from the positively charged amino acid
residues, except of a single coordinating bond from Nε2 of a histidine to the metal center.1
Although almost in all functional model compounds of these enzymes, developed until now, the
ligand(s) coordinate(s) via 2-4 covalent bound to the central vanadium atom. The typically
oxoperoxo vanadium(V) compounds does not have hydrogen-bound network environment.
These complexes practically capable oxidize just iodine and bromine but not chlorine and only in
special condition: non-aqueous solutions and in presence of strong acid.2,3 However the enzyme
are oxidize chlorine in water at pH ~5.5.1
Based on the vanadate-phosphate structural analogy, phosphate receptors/sensors can be used
vanadate/peroxo-vanadate binders too, as earlier works showed already.4-6 Since the vanadate
speciation is quite complicated in aqueous solution and the monoperoxo-vanadate is not stabile
in such conditions, we focused on the diperoxo-vanadate which has more simple speciation in
water.7
A 1.0 B 1.0
10 mM 10 mM
[HVO4]2-
[H2VO2(OO)2]-
[HVO2(OO)2]2- [H2V10O28]4- [HV10O28]5-
0.8 0.8 [V4O12]4-
V fraction
V fraction
0.6 0.6
[V5O15]5-
[H3V10O28]3-
0.4 0.4 VO2+
[HV2O3(OO)4]3- [H2VO4]2-
6- [H2V2O7]3- [HV2O7]3-
0.2 [V2O5(OO)3] 0.2 [V10O28]6-
[V2O7]4-
0.0 0.0
2 4 6 8 10 12 2 4 6 8 10 12
pH pH
Figure 1. A: Speciation of diperoxo-vanadate7, B: Speciation of vanadate
A promising ligand can be seen in Figure 2. The detailed studies are still in progress in our
laboratory.
O N H
H N
N
N
H N
O N H
Figure 2. A potentian diperoxo-vanadate binder8
Acknowledgements: The author (TJ) would like to thank the “Magyary Zoltán Felsőoktatási Közalapítvány”
for the financial support.
[1] R. Wever, W. Hemrika, Vanadium haloperoxidases. Handbook of Metalloproteins (2001), 2 1417-1428.

[2] J.Y. Kravitz,; V.L. Pecoraro, Pure and Appl. Chem. 77(9) (2005) 1595-1605.
[3] A. Butler, M.J. Clague, G.E. Meister, Chem. Rev. 94(3) (1994) 625-38.
[4] X. Zhang, M. Meuwly, W.D. Woggon, J. Inorg. Biochem. 98(11) (2004) 1967-1970.
[5] X. Zhang, W.D. Woggon, J. Am. Chem. Soc. 127(41) (2005) 14138-14139.
[6] S. Tapper, J.A. Littlechild, Y. Molard, I. Prokes, J.H.R. Tucker, Supramol. Chem. 18(1) (2006) 55-58.
[7] I. Andersson, S. Angus-Dunne, O. Howarth, L. Pettersson, J. Inorg. Biochem. 80 (2000) 51–58
[8] H.F.M. Nelissen, D.K. Smith, Chem. Commun. (2007) 3039–3041.

Decameric vanadate reduction by physiological concentrations of

glutathione in mitochondrial assay conditions
Sandra S. Soaresa,b, Rui O. Duartec, Carlos Gutiérrez-Merinod, José J.G. Mourac,

Manuel Aurelianob,e
a
FCMA, University of Algarve, Portugal; bCCMAR, University of Algarve; cREQUIMTE, Dept. Chemistry, FCT,
d
University Nova of Lisbon; Dept. Biochemistry and Molecular Biology, University of Extremadura, Spain;
e
Dept. Chemistry and Biochemistry, FCT, University of Algarve; email: maalves@ualg.pt
It is well known that vanadate and vanadyl interconvert easily under physiological conditions1.
Vanadate seems to be more toxic for living systems and its conversion to vanadyl can be seen
as an intracellular detoxification mechanism2. Moreover, the characterization of the composition
of vanadate solutions is of extreme importance in order to correlate the vanadate promoted
effects in biological systems with the oligomeric species and/or oxidation states present in these
solutions3,4. The aim of this work is to determine if specific in vitro experimental conditions,
such as the usual composition of mitochondrial assay buffers, physiological concentrations of
reduced glutathione (GSH) or the presence of mitochondrial protein in the assay media, may
contribute to vanadate reduction particularly at the polymerized state of vanadate, the
decameric vanadate species. Changes in absorbance at 700 nm, for reduced vanadium form,
were monitored by spectrophotometry, as previously described5. The reduction of decameric
and monomeric vanadate species (1 mM total vanadium) was recorded in a reaction medium
containing mitochondrial respiration buffer (0.2 M sucrose, 5 mM KH2PO4, 10 mM KCl, 5 mM
MgCl2 and 10 mM Tris-HCl, pH 7.4 plus 5 mM pyruvate and 0.5 mM malate) and a physiological
concentration of GSH (5 mM), in the absence or presence of rat hepatic mitochondria (0.5-2.0
mg protein/ml) (Figure 1). Vanadate reduction products were also recorded by Electron
Paramagnetic Resonance (unpublished results).
Reduction of vanadate to a 700 nm-absorbing blue
0.08 Decavanadate colored product, a form of vanadyl, was demonstrated
Metavanadate
_in the absence or presence of rat hepatic
Absorbance (700 nm)
0.06
mitochondria using GSH as the reducing agent6. It
0.04
was also observed that the increase in absorbance at
700 nm depends on the presence of decameric
0.02 vanadate species, whereas no reduction of monomeric
vanadate was noticed under the same experimental
0.00
conditions. Reduction of decameric vanadate is
0 50 100 150 200 250 300 350
accompanied by the loss of absorbance at 400 nm,
Time (min)
pointing out that it induced decameric vanadate
decomposition (not shown). The presence of a tetravalent form of vanadium in these
experimental conditions was confirmed by EPR, nevertheless, the weak signals obtained
correspond to amounts of reduced products below the detection limit of the EPR instrument
used (<10 µM). Note that, once vanadyl radical concentration keep lower than 10 µM it means
that the vanadyl radical must be rapidly reacting with another vanadyl radical or with other
chemical specie(s) present in the medium once formed by the reaction between GSH and
vanadate, thus leading to a fairly low steady-state concentration. Therefore, in the presence of
physiological concentrations of GSH the redox state of vanadate in neutral pH appears to be
dependent on the decamerization of vanadate. Putting it al together, we can not exclude the
possibility of a cross talk between oligomerization of vanadate and decavanadate reduction in
biological systems, which can account, at least in part, for the role of vanadium in biological
systems.
Acknowledgements: Portuguese Foundation for Science and Technology (SFRH/BD/8615/2002 to SSS and
project POCTI/38191/QUI/2001 to MA), joint Spanish-Portuguese Grant (HP2004-0080 to CG-M and MA).
[1] D.C. Crans, Comments Inorg. Chem. 16 (1994) 1-33. [2] N.D. Chasteen, Struct. Bonding 53 (1983)
105-138. [3] M. Aureliano, and R. M. C. Gândara, J. Inorg. Biochem., 99 (2005) 979-985;[4] S.S. Soares,
F. Henao, M. Aureliano, C. Gutiérrez-Merino, Chem. Res. Toxicol. 21 (2008) 607-618. [5] T. Ramasarma,
A.V.S. Rao, Mol. Cell. Biochem. 281 (2006) 139-144. [6] I.G. Macara, K. Kustin, L.C.C. Cantley Jr., Biochim.
Biophys. Acta 629 (1980) 95-106.

Template synthesis of a spherical polyoxovanadate(V) by oxidative

coupling reaction
Shogo Kamiya, Yoshihito Hayashi, Kiyoshi Isobe
Department of Chemistry, Graduate School of Natural Science, Kanazawa

University, Kakuma, Kanazawa 920-1192, Japan
Redox coupling of polyoxovanadates in non-aqueous solvent under mild conditions may be

suitable for conversion of certain series of polyoxovanadates into larger species. With the
utilization of redox chemistry of vanadium, the isolation of a series of reduced polyoxovanadates
with reductive coupling have been investigated. Alternatively, the oxidative coupling of
polyoxometalates may be possible for the synthesis of fully oxidized polyoxovanadates. The
nucleophilic species and electrophilic V(V) species produced by the controlled oxidation may
prompt to couple two species into a larger polyoxovanadate. In this study, the structure and the
coordination ability of the template molecules are also important for the synthesis of novel
polyoxovanadates. By the addition of the template anions to the condensation reaction, we
isolated a spherical triacontavanadate (V30) with V(V) oxidation state.
Figure. V30 structure of the left-handed type (left) and that of the right-handed type (right).
The shape of the V30 vanadate looks like reflecting the structure of the template anion.
Furthermore, we found that this V30 vanadate has optical isomer. By the asymmetric
crystallization, we characterized both structures with single crystal X-ray structural analysis.

Asymmetric oxidation of thioanisole catalysed by reduced Schiff base

oxovanadium(IV) complexes
Isabel Correiaa, Pedro Adãoa, João Costa Pessoaa, Fernando Avecillab
a
Centro de Química Estrutural, Instituto Superior Técnico,TU Lisbon, 1049-001 Lisboa, Portugal,
email: pedro.m.adao@ist.utl.pt
b
Departamento de Química Fundamental, University of Coruña, Spain
Vanadium complexes of the chiral reduced Schiff base ligands, prepared from 1S,2S-
cyclohexanediamine or and 1S,2S-diphenylethylenediamine and 2-hydroxybenzaldehydes,
[VO(sal(1S,2S-chan))] or [VO(sal(1S,2S-dpan))], catalyze the sulfoxidation of thioanisole
with hydrogen peroxide, showing high conversions and moderate enantioselectivities1.
Various parameters were tested such as solvent, temperature, catalyst loading, catalyst
concentration and phenolic ring substituent effect on overall conversion and
enantioselectivity. Methoxy substituents adjacent to the phenolate group improve chiral
induction2. Lower temperatures also have a positive effect on chiral induction. The catalyst
concentration also required optimization. Catalyst loadings higher or lower than 1 mol %
seem to slow down the catalysis and decrease enantioselectivity. In the case of vanadium
catalyzed sulfoxidations, it is very likely that the active species is an
oxomonoperoxovanadium(V) complex3.
S
H2O2, 0-10ºC S
*
NH NH
M
R' O O R'
R R
2+
1: R=H-; R'=H-; M=VO
2: R=MeO-; R'=H-; M=VO2+
3: R=t-Bu-; R'=t-Bu-; M=VO2+
Scheme 1 – Asymmetric sulfoxidation of thioanisole catalysed by VO(sal(1S,2S-chan)) complexes.
Acknowledgements. We thank the financial support of Fundo Europeu para o Desenvolvimento Regional,
Fundação para a Ciência e Tecnologia, POCI 2010, project PPCDT/QUI/55985/2004 and the grant
SFRH/BD/40279/2007.
[1] G. Romanowski, E. Kwiatkowski, W. Nowicki, M. Kwiatkowski, T. Lis, Polyhedron, 27 (2008) 1601-

1609
[2] K. Nakajima, K. Kojima, M. Kojima, J. Fujita, Bull. Chem. Soc. Jpn., 63 (1990) 2620-2630
[3] A. Butler, M.J. Clague, G.E. Meister, Chem. Rev., 94 (1994) 625-638.

Oxidation of p-chlorotoluene and cyclohexene catalysed by polymer-

anchored oxovanadium(IV) and copper(II) complexes of amino acid
derived tridentate ligands
Amit Kumar,a Mannar R. Maurya,b Maneesh Kumar,b and João Costa Pessoaa
a
Centro Química Estrutural, Instituto Superior Técnico, TU Lisbon, Av Rovisco Pais, 1049-001 Lisboa,
Portugal, email: amit.kumar@ist.utl.pt
b
Department of Chemistry, Indian Institute of Technology Roorkee, Roorkee-247667, India
3-Formylsalicylic acid (Hfsal) covalently bound to chloromethylated polystyrene (PS) cross-

linked with 5% divinylbenzene reacted with DL-alanine (DL-Ala) and L-isoleucine (L-Ile) to give
the Schiff-base tridentate ligand PS-H2fsal-DL-Ala and PS-H2fsal-L-Ile, respectively. These
polymer-anchored ligands upon reaction with VOSO4 and Cu(CH3COO)2 form the polymer-bound
complexes PS-[VO(fsal-DL-Ala)(H2O)], PS-[Cu(fsal-DL-Ala)(H2O)], PS-[VO(fsal-L-Ile)(H2O)] and
PS-[Cu(fsal-L-Ile)(H2O)] (see Scheme). Structures of these immobilized complexes have been
established on the basis of scanning electron micrographs, FTIR, UV-Vis, EPR, thermo
gravimetric and elemental analyses studies. Non-polymer-bound CuII- and VIVO-complexes have
also been prepared with these ligands, namely the vanadium complexes [VIVO(fsal-DL-
Ala)(H2O)] and [VIVO(fsal-L-Ile)(H2O)].
These complexes have been used with success
as catalysts for the oxidation of p-chlorotoluene O O
O
and cyclohexene by H2O2 and reaction O O
conditions have been optimised to obtain
V
OH2 O
maximum conversion. N
EPR studies were especially useful to confirm
R
that the VIVO- and CuII-complexes are
magnetically diluted and well dispersed in the Proposed structure for the polymer-bound
vanadium complexes: R = -CH3 (DL-Ala) or R
polymer matrix, and to give evidence for the
= -CH(CH2CH3)CH3 (L-Ile). The ball represents
binding modes proposed.
the polystyrene matrix.
Recycling studies indicated that these catalysts
can be reused at least three times without any
significant loss in their catalytic potential. However, EPR studies indicated that while the
polymer supported VIVO-complexes did not change upon use, the EPR spectra of the Cu-
complexes showed significant changes. Several EPR, 51V NMR and UV-Vis studies have been
carried out to detect intermediate species, and outlines of the mechanisms of the catalytic
reactions are proposed.
Acknowledgements: The authors thank the financial support from FEDER, Fundação para a Ciência e a
Tecnologia, POCI 2010 (PPCDT/QUI/55985/2004 and PPCDT/QUI/56946/2004 programs) and grant
SFRH/BPD/34835/2007. Prof. M. R. Maurya acknowledges the financial support received from the Council of
Scientific and Industrial Research, New Delhi

Organometallic chemistry of vanadium with B(C6F5)3
Christian Lorber and Robert Choukroun
Laboratoire de Chimie de Coordination du CNRS, 205 route de Narbonne, 31077 Toulouse, France,
email: lorber@lcc-toulouse.fr
Vanadocene, which is the unique, stable, and easily accessible metallocene of the early
transition metals, is an electronically and coordinatively unsaturated molecule. Other
metallocenes of the early transition metals, such as titanocene and zirconocene do not exist in
their original sandwich structure and need subtle ligand (alkyne, butadiene) to stabilize the
metallocene fragment. A contrario the reactivity of the vanadocene [VCp2] compound, in spite of
its accessibility, was scarcely studied probably due to the formation of various paramagnetic VIII
and VIV compounds which prevent further spectroscopic informations.[1,2]
The chemistry of the strongly Lewis acidic tris(pentafluorphenyl)borane B(C6F5)3 is the subject
of numerous applications. Although the main interest was its established role in the formation of
cationic derivatives for polymerization, different organic, organometallic, and catalytic
applications have been reported the last few years.[3]
As part of our long term interest in the organometallic chemistry of early-transition metal group
4 and 5 complexes,[4] in particular directed towards olefin polymerization and small molecule or
unsaturated bond activation, we have investigated the reactivity of several vanadium
compounds (including Cp2V) with B(C6F5)3. Some of these studies will be presented here,[5] with
sometimes a comparison with group 4 metal analogue complexes.
- Reactivity of Metallocenes towards small molecules and/or unsaturated C-X bonds

C6F5 C6 F5
B(C6F5)3 B(C6F5)3 B B(C6F5)3 Cp Cp
F CO
Cp2 V(CO) CO F + CO + V [HB(C6F5 )3] + V H B(C6 F5) 3
V V F V CO
H CO Cp Cp
Cp Cp F Cp
F
R' BR3
C N
Cp2V + R'C≡N•BR3 V BR3 = BCl3, BPh3, B(C6F5)3
Cp2
- Reactivity of B(C6F5)3 with oxo, alkyl or alkoxide complexes

C6F5 R R
C6F5 OR
C6F5 B O
RO O RO O
V V C6F5 V V C6F5 Me
O adduct C6F5 O OR
C6F5 O OR Cp2V [B(C6F5)4]-
O RO L
V R R
NEt2
Et2N -C6F5 transfer alkyl abstraction
NEt2
- TCNE- and TCNQ-vanadium complexes as structural models for molecule-based magnet.

(C6F5)3B
(C6F5)3B B(C6F5)3 N B(C6F5)3
n V N
N N
TCNQ TCNE N
+ N VCp2
n=2 n=1 Cp2V N
N N 2 B(C6F5)3 N
Cp2V VCp2 N
(C6F5)3B
N
B(C6F5)3
[1]. R. Choukroun, C. Lorber Eur. J. Inorg. Chem. (2005), 4683. (Review on Vanadocene).
[2]. C. Lorber, ‘Vanadium’ in Comprehensive Organometallic Chemistry III, Eds. Robert H. Crabtree and D.
Michael P. Mingos, Elsevier: Oxford (2007), Vol. 5, pp. 1-60 (ISBN: 008044590X).
[3]. W. E. Piers, Adv. Organomet. Chem. (2005), 1-76.
[4] (a) C. Lorber et al, Organometallics (2000), 19, 1963. (b) C. Lorber et al, Dalton Trans. (2000), 4497.
(c) F. Wolff et al, Inorg. Chem. (2003), 42, 7839. (d) F. Wolff et al, Eur. J. Inorg. Chem. (2004), 2861. (c)
C. Lorber et al, Eur. J. Inorg. Chem. (2005), 2850. (d) R. Choukroun et al, Chemistry- Eur. J. (2002), 8,
2700. (e) R. Choukroun et al, Organometallics (2002), 21, 1124. (f) C. Lorber et al, Inorg. Chem., (2002),
41, 4217 (g) C. Lorber et al, Inorg. Chem. (2007), 46, 3192.
[5] (a) F. Wolff et al, Eur. J. Inorg. Chem. (2003), 628. (b) R. Choukroun et al, Organometallics (2003), 22,
1995. (c) C. Lorber et al, Organometallics (2004), 23, 5488. (d) R. Choukroun et al, Organometallics
(2006), 25, 1551. (f) R. Choukroun et al, Organometallics (2006), 25, 4243. (g) R. Choukroun et al,
Organometallics (2006), 25, 4243. (h) R. Choukroun et al, Organometallics (2007), 26, 3604.

Vanadium(V) complexes as oxidation catalysts
Silvia Lovat, Miriam Mba, Marta Pontini and Cristiano Zonta* and Giulia Licini*
Dipartimento di Scienze Chimiche, Università di Padova, via Marzolo 1, 35131 Padova, Italy
email: silvia.lovat@unipd.it
Vanadium(V) centres are usually strong Lewis acids, which makes them suitable for the
activation of peroxidic reagents.1 Accordingly, vanadium(V) complexes have been found to act
as catalysts in various oxidation reactions like epoxidations of alkenes and allylic alcohols,
hydroxylations of alkanes and arenes, oxidations of primary and secondary alcohols to the
corrisponding aldehydes and ketones, haloperoxydation and oxidations of sulphide ethers.2
More recently we have studied the coordination chemistry of various ligands, such as
trialkanolamines 1, and triphenolamines 2, with vanadium(V). We have demonstrated that
these ligands form thermally robust tetradentate, C3-symmetric, V(V)complexes.
In addition to these ligands, we have recently expanded our attention to silsequioxane ligands.
These ligands are a a class of three-dimensional oligomeric organosilica compounds with a cage
framework 3.3
The preliminary results on the capability to transfer oxygen of these complexes will be
presented.
R O
O
R O Si O V
O O
R O R
O Si O Si R O
OV O
R
O V O R
O O R Si O Si
R O O
N N R R
Si O
R O Si
R
1 2 3
Figure 1. Vanadium metal complexes used in catalytic oxidations.
Acknowledgements: The authors would like to thank FIRB-2003 CAMERE-RBNE03JCR5 project, COST Action
D40 ‘Innovative Catalysis, MIUR and University of Padova for their financial support.
[1] D.C Crans, J. Smee, E. Gaidamauskas, L. Yang Chem.Rev. 104 (2004), 849.
[2] A.G.J. Ligtenbarg, R. Hage, B.L. Feringa Coord. Chem. Rev. 237 (2003) 83
[3] F. Carniato, E. Boccaleri, L. Marchese, A. Fina, D. Tabuani, G. Camino 9 (2007) Eur. J. Inorg. Chem 585.

Vanadium diamine bisphenolate complexes: synthesis, structures and

catalytic activity in sulfoxidations
Sónia Barroso,a Pedro Adão,a João Costa Pessoa,a Ana M. Martinsa*

a
Centro de Química Estrutural, Instituto Superior Técnico, 1049-001 Lisboa, Portugal
email: ana.martins@ist.utl.pt
Nowadays, there are two main reasons which stimulate research in the field of the sulfoxidation
catalytic reactions: the synthesis of sulfoxides, an important class of compounds widely utilized
in the pharmaceutical industry and academia, and the removal of sulfur compounds from fuels
and industrial effluents, in order to satisfy the new environmental legislations.
A number of vanadium-dependent haloperoxidases mediate the oxidation of sulfides by
hydrogen peroxide.1 In an attempt to gain an insight into the biological roles of vanadium, many
recent studies have been focused in the design of model compounds that mimic the metal
coordination sphere in the active sites of these vanadium-dependent enzymes, as well as their
reactivity in the oxidation states +3, +4 and +5.2 It was previously observed that vanadium and
other early transition metal complexes of tetra-(N2O2)-dentate diamine-bisphenolate ligand
have proved to be highly active catalysts in olefin polymerization3 and in the Ring Opening
Polymerization of lactones.4 Moreover, Diamino-bisphenolate (N2O2 ligand =
t
[Me2N(CH2)2N{CH2−(2−OC6H2−Bu 2−3,5)2}]) complexes of molybdenum and tungsten revealed
to be very active catalysts in olefin epoxidation.5
In this work we present results on the synthesis and structural characterization of N2O2
complexes of V(III) and V(V) and the catalytic activity of VVO[N2O2]X (X = Cl, OiPr) in the
sulfoxidation of thioanisole. The highest conversion (93%) was obtained with VVO[N2O2]OiPr and
H2O2 almost without further reaction to the sulfone (5%). Preparation of a chiral version of this
complex is in course in order to test the enantioselectivity.
O
S S
H 2 O2
X
tBu O
t
O V O Bu
But N tBu
X = Cl, OiPr
Acknowledgements: We thank the FCT, Portugal, for financial support (SFRH/BD/28762/2006,

SFRH/BD/40279/2007, PPCDT/QUI/55744/2004 and PPCDT/QUI/55985/2004)
[1] I. Fernández, N. Khiar, Chem. Rev. 103 (2003) 3651–3705.

[2] D. C. Crans, J. J. Smee, E. Gaidamauskas, L. Yang, Chem. Rev. 104 (2004) 849.
[3] S. Gendler, S. Groysman, Z. Goldschmidt, M. Shuster, M. Kol, J. Polym. Sci. 44 (2006) 1136.
[4] A. J. Chmura, M. G. Davidson, M. D. Jones, D. Lunn, M. F. Mahon, A. F. Johnson, P. Khunkamchoo, S. L.
Roberts, S. S. F. Wong, Macromolecules, 39 (2006) 7250.
[5] C. Trindade, S. Barroso, S. Namorado, P. M. Reis, A. M. Martins, B. Royo, manuscript in preparation.

Polystyrene bound dioxovanadium(V) complex of histamine derived

ligand for the oxidation of methyl phenyl sulfide, diphenyl sulfide and
benzoin
Mannar R. Maurya* and Aarti Arya

Department of chemistry, Indian Institute of Technology Roorkee, Roorkee-247667, India,
e-mail: rkmanfcy@iitr.ernet.in
Ligand H2sal-his derived from salicylaldehyde and histamine has been covalently bonded to
chloromethylated polystyrene cross-linked with 5 % divinylbenzene. Upon treatment with
[VO(acac)2] in dimethylformamide (DMF), the polystyrene bound ligand (abbreviated as PS-
Hsal-his, I) gave the stable intermediate polystyrene bound oxovanadium(IV) complex, which
on oxidation yielded the dioxovanadium(V) PS-[VO2(sal-his)](1) complex. The corresponding
non-polymer bound complex, [VO2(sal-his)](2) and its peroxo analogue [VO(O2)(sal-his)](3)
have also been isolated. These complexes have been characterized by IR, electronic and 1H NMR
spectral studies, magnetic susceptibility measurements, and thermal as well as scanning
electron micrographs studies. Complex PS-[VO2(sal-his)](1) has been used as catalyst for the
oxidation of methyl phenyl sulfide, diphenyl sulfide and benzoin with 30% H2O2 as an oxidant.
Under the optimised reaction conditions, a maximum of 95.3% conversion of methyl phenyl
sulfide with 63.7% selectivity towards methyl phenyl sulfoxide and 36.3% towards methyl
phenyl sulfone has been achieved in 2 h of contact time. Under similar conditions, diphenyl
sulfide gave 83.4% conversion where selectivity of reaction products varied in the order:
diphenyl sulfoxide (71.8%) > diphenyl sulfone (28.2%). A maximum of 91.2% conversion of
benzoin has abeen achieved within 6 h of reaction time where selectivity of the obtained
reaction products varied in the order: methylbenzoate (45.3%) > benzyl (22.5%) >
dimethylacetal (20.9%) > benzoic acid (11.3%). The polymer-anchored heterogeneous catalyst
is free from leaching during catalytic action and is recyclable. Catalytic activities of the polymer
bound catalyst have also been compared with the corresponding non-polymer bound complex,
[VO2(sal-his)].
Acknowledgements: Prof. M. R. Maurya acknowledges Fundação Oriente for the financial support received
and Department of Science and Technology, New Delhi is also gratefully acknowledged for financial support
of the work

Dioxovanadium(V) Schiff base complexes of

R(-)-1,2-diaminopropane and o-hydroxycarbonyl compounds.
Synthesis, characterization, catalytic properties and structure
Grzegorz Romanowski,a Waldemar Nowicki,a Artur Sikorski,a Andrzej Wojtczak,b

a
Faculty of Chemistry, University of Gdansk, Sobieskiego 18/19, PL-80952 Gdansk, Poland
b
Faculty of Chemistry, N. Copernicus University, Gagarina 7, PL-87100 Torun, Poland
email: greg@chem.univ.gda.pl
Vanadium plays active roles in many biologically important reactions such as

halogenation of organic substrates, activation or fixation of nitrogen through an alternative
pathway1, potent inhibitor of phosphate-metabolizing enzymes2 and a cofactor in
haloperoxidases and nitrogenases3. Some of the vanadium compounds stimulate glucose uptake
and inhibit lipid breakdown in a manner remarkably reminiscent of insulin effects4,5 or exert
preventive effects against chemical carcinogenesis on animals6. Recently, it has been
established that vanadium(V) complexes with Schiff bases, which are excellent models for active
sites of vanadium haloperoxidases, are able to catalyze the oxidation of organic sulfides to the
corresponding sulfoxides7-9.
A series of dioxovanadium(V) complexes, obtained by monocondensation of R(-)-1,2-
diaminopropane and aromatic o-hydroxycarbonyl compounds, were prepared in high yields. The
complexes were characterized in the solid state (IR) and in solution (UV-Vis, CD, 1H and 51V
NMR). Single crystal X-ray analyses were performed with dimeric and monomeric form of the
complexes. The complexes comprising ligands derived from 3-methoxy and 5-
methoxysalicylaldehyde catalyze the oxidation of thioanisole to the corresponding sulfoxide by
cumene hydroperoxide.
Figure 1. The molecular structure of the one of the vanadium(V) complexes.
Acknowledgements: This scientific work has been supported from funds for science in years 2007-2009 as a
research project (N N204 0355 33, BW/8000-5-0399-8, DS/8210-4-0086-8).
[1] A. Butler, J.V. Walker, Chem. Rev. 93 (1993) 1937.

[2] D. Rehder, Angew. Chem. Int. Ed. Engl. 30 (1991) 148.
[3] J.S. Martinez, G.L. Carrol, R.A. Tschirret-Guth, G. Altenhoff, R.D. Little, A. Butler, J. Am. Chem. Soc.
123 (2001) 3289.
[4] K.H. Thompson, C. Orvig, Coord. Chem. Rev. 219–221 (2001) 1033.
[5] D.C. Crans, L. Yang, J.A. Alfano, L.-H. Chi, W. Jin, M. Mahroof-Tahir, K. Robbins, M.M. Toloue, L.K.
Chan, A.J. Plante, R.Z. Grayson, G.R. Willsky, Coord. Chem. Rev. 237 (2003) 13.
[6] A.M. Evangelou, Crit. Rev. Onco./Hematol. 42 (2002) 249.
[7] E. Kwiatkowski, G. Romanowski, W. Nowicki, M. Kwiatkowski, K. Suwinska, Polyhedron 22 (2003) 1009.
[8] E. Kwiatkowski, G. Romanowski, W. Nowicki, M. Kwiatkowski, K. Suwinska, Polyhedron 26 (2007) 2559.
[9] G. Romanowski, E. Kwiatkowski, W. Nowicki, M. Kwiatkowski, T. Lis, Polyhedron 27 (2008) 1601.

Chiral dioxovanadium(V) complexes of Schiff bases derived from 1,2-

diphenyl-1,2-diaminoethane and aromatic o-hydroxyaldehydes.
Synthesis, characterization, catalytic properties and structure
Grzegorz Romanowski,a Waldemar Nowicki,a Tadeusz Lis,b
a
Faculty of Chemistry, University of Gdansk, Sobieskiego 18/19, PL-80952 Gdansk, Poland
b
Faculty of Chemistry, University of Wroclaw, F. Joliot-Curie 14, PL-50283 Wroclaw, Poland
email: greg@chem.univ.gda.pl
The discovery of vanadium in active sites of biological systems of nitrogenase1 and

bromoperoxidase2 and recognition of its environment increased the interest in the vanadium
complexes with ligands bearing oxygen and nitrogen atoms for mimicking the biological activity
in natural systems. Structural models for the active site in haloperoxidases have already been
reported3-5. Recently, it has been established that vanadium(V) complexes with Schiff bases,
which are excellent models for active sites of vanadium containing haloperoxidases, are able to
catalyze the oxidation of organic sulfides to the corresponding sulfoxides6,7. Vanadium
haloperoxidases catalyze the oxidation of halides in the presence of hydrogen peroxide to highly
reactive intermediate, a hypohalous acid, which may react either with suitable nucleophilic
acceptor, if present, forming a halogenated compound or with hydrogen peroxide yielding 1O2.
A series of dioxovanadium(V) complexes, obtained by monocondensation of R,R(+)-1,2-
diphenyl-1,2-diaminoethane or S,S(-)-1,2-diphenyl-1,2-diaminoethane and aromatic o-
hydroxyaldehydes, were prepared in high yields. The complexes were characterized in the solid
state (IR) and in solution (UV-Vis, CD, 1H and 51V NMR). Single crystal X-ray analyses were
performed with two of such complexes and revealed different conformations of the five-
membered chelate rings. Complexes, which incorporate singly condensed products with 3- or 5-
methoxysalicylaldehyde act as catalyst to the oxidation of thioanisole by cumene
hydroxyperoxide.
Figure 1. The molecular structure of the one of the vanadium(V) complexes.
Acknowledgements: This scientific work has been supported from funds for science in years 2007-2009 as a
research project (N N204 0355 33, BW/8000-5-0399-8, DS/8210-4-0086-8).
[1] R.L. Robinson, R.R. Eady, T.H. Richardson, R.W. Miller, M. Hawkins, J.R. Postgate, Nature 322 (1986)
388. [2] H. Vilter, Phytochemistry 23 (1984) 1387 [3] M. Casny, D. Rehder, Chem. Commun. (2001) 921.
[4] C. Gruning, D. Rehder, J. Inorg. Biochem. 80 (2000) 185. [5] C. Kimblin, X. Bu, A. Butler, Inorg. Chem.
41 (2002) 161. [6] E. Kwiatkowski, G. Romanowski, W. Nowicki, M. Kwiatkowski, K. Suwinska, Polyhedron
22 (2003) 1009. [7] E. Kwiatkowski, G. Romanowski, W. Nowicki, M. Kwiatkowski, K. Suwinska, Polyhedron
26 (2007) 2559.

V-catalysed oxidations with H2O2
V.Contea, F. Fabbianesia, B. Florisa , P. Gallonia, D. Sordia, I. Arendsb, D. Rehderc

a
Dip. Scienze e Tecnologie Chim., Univ. Roma Tor Vergata, via Ricerca Scientifica, 00133, Roma IT
b
Lab. of Biocatalysis and Organic Chemistry, Delft University of Technology, Delft, NL.
c
Inst. Inorganic and Applied Chem., Hamburg University, Martin-Luther-King-Platz 6 D-20146 Hamburg, D
e-mail: valeria.conte@uniroma2.it
In the present V(V) Catalyst, oxidant

paper, the "Sub" "Sub-O"
Solvent, TOC
performance of
some vanadium
Catalysts
based catalysts will Substrates
O O
be presented.[1] O V
O
OMe H3C O
O V O
High TON’s and O O O V
N
selectivities were N
O N
N N N N
H H
obtained by using CH3OH
H3C
N
trifluoroethanol as a Cat.1 Cat.2 Cat.3 H
solvent, which is
known to activate S
CH3
O
H2O2.
The potential of the O
NH
V complexes shown O
V O O O N O N OH
in the scheme, in O
V O V
N O +
the oxidation of O O
N N
thioethers, alcohols, CF3SO3-
and alkenes with

both dioxygen and
Oxidants
H2O2 in a variety of Cat.4 Cat.5 VO(SALen)TfO
ILs, has been H2O2, O2

N + N
screened. V
Between the ILs O O O
studied, the EtSO4-

hydrophobic VO(SALen)EtSO4
bmim+PF6- gives in
general the best
Solvents
feats.
PF6- [(CF3SO2)2N]-
F
F N +
OH N N +
N
F
BMImPF6 BMImTf2N
TFE
NO3- NO3-
N + N + OH
N N
BMImNO3 HOPMImNO3
[1] D. Sordi : WG1COST-STSM-D40-1773 from Rome to Delft.

On the nature of V(V) species in hydrophilic ionic liquids: a

spectroscopic approach
István Bányai,a Valeria Conte,b Lage Pettersson,c Adriano Silvagnib

a
Dept. of Colloid and Environmental Chemistry, University of Debrecen, H-4010, Debrecen, Pf 31, Hungary
b
Dip. Scienze e Tecnologie Chim., Univ. Roma Tor Vergata, via Ricerca Scientifica, 00133, Roma, Italy
c
Department of Chemistry, Umeå University, SE-90187, Umeå, Sweden
email: valeria.conte@uniroma2.it
Aqueous solutions of V(V) peroxovanadates with high ionic concentrations have the potential to be
more effective oxidising agents than the corresponding simple aqueous solutions.1 However, they
have received little investigation. The present study uses mainly 51V NMR in order to understand the
effects of increasing ionic concentrations, using three different ionic compounds that also exist as
hydrophilic ionic liquids.
H2VO4- (-560 ppm)

[bmim][BF4] Decavanadates (-422, -503, -521 ppm)
V4O124- (-577 ppm)
V5O155- (-586 ppm) Vanadate-fluoride adducts?
(-465, -548, -612 ppm)
[bmim][BF4]
[VO(O2)2]- (-690 ppm) [VO(O2)2F]2- (-700 ppm)
51
V NMR and other experiments partially elucidated the nature of aqueous vanadates and
peroxovanadates to which the hydrophilic ionic liquids [bmim][BF4], [bmim][TfO] and [bdmim][BF4]
have been added.
N N N
+ + + BF4-
N BF4- N CF3SO3- N
[bmim][BF4] [bmim][TfO] [bdmim][BF4]
These ionic liquids alter the solution chemistry of aqueous vanadate by increasing aggregation (with
and without H2O2) and also increase the rate of peroxide consumption in reactions catalysed by
vanadium.
In ionic liquids containing BF4-, the formation of vanadate-fluoride and tetrafluoroborate adducts is
suggested, based on the appearance of new 51V NMR resonances at -465, -503, -612 ppm. The
results also include reactivity data for peroxovanadates in ionic liquids.
Acknowledgements: A. Silvagni COST-STSM-D29-02097 from Rome to Debrecen.
[1] V. Conte, B. Floris, A. Silvagni, Vanadium catalyzed oxidation in Ionic Liquids, in ACS Symposium Series
974: Vanadium: the Versatile Metal, K. Kustin, J. Costa Pessoa and D.C. Crans Eds. (2007) 28-37.

Characterization in the solid state of chiral salen and salan ligands and
their vanadium(V) compounds
Fernando Avecilla,a Pedro Adão,b Isabel Correiab and João Costa Pessoab
a
Departamento de Química Fundamental, Universidade da Coruña, Campus da Zapateira s/n, 15071,
A Coruña, Spain. email: avecil@udc.es
b
Centro de Química Estrutural, Instituto Superior Técnico, TU Lisbon, Av. Rovisco Pais,
1049-001 Lisboa, Portugal
We report the characterization in solid state of chiral salen and salan type ligands, which
are derived from salicylaldehyde and chiral diamines (cyclohexane and diphenyletylenediamine),
and some dinuclear vanadium(V) compounds with them. A variety of vanadium complexes have
been introduced as structural and/or functional models for biologically active vanadium
compounds.[1] The vanadium compounds reported can be studied as models in oxidation
catalysis.
In solution salen ligands have the disadvantage of the hydrolysis of the C=N bond,
particularly in water containing solvents, and we have worked with salan ligands where the
imine bonds have been reduced to amines. The salen reduced derivatives exhibit different
structural and chemical properties, increasing the stability of the complexes and their flexibility,
which are also more resistant to hydrolysis.
We prepared the complexes starting from VIVOCl2. The oxidation of VIV was probably due
to diffusion of air into the solution during the crystallization.[2] The resulting VO2L complexes
precipitated as dinuclear species containing tetradentate ligands with phenolate and amine
coordinated to the dioxovanadium(V) ion. X-ray structures of these compounds demonstrate
that they form dimers in the solid state with a OVV(μ-O)VVO unit (V2O3 core) with tetradentate
ligands and one μ-oxo bridge, which are relatively rare.[3] In fact, only two examples were found
in the literature of amine derivatives which act as tetradentate ligands and both of them are
mixed valence(IV/V) dimers.[4]
This work illustrates the high propensity of the vanadium centre to increase its
coordination number via dimerization of two pentacoordinate monomers if the steric control
exercised of the ligands allow it.
Acknowledgements: The authors thank FEDER, Fundação para a Ciência e a Tecnologia, POCI 2010
[1] D. Rehder, Coord. Chem. Rev. (1999), 182(1), 297-322.

[2] I. Correia, J. Costa Pessoa, M. T. Duarte, R. T. Henriques, M. F. M. Piedade, L. F. Veiros, T. Hakusch, T.
Kiss, A. Dörnyei, M. M. C. A. Castro, C. F. G. C. Geraldes and F. Avecilla, Chem. Eur. J. (2004), 10, 2301-
2317.
[3] I. Cavaco, J. Costa Pessoa, M. T. Duarte, R. T. Henriques, P. M. Matias and R. D. Gillard, J. Chem. Soc.,
Dalton Trans., (1996), 1989-1996.
[4] a) A. Kojima, K. Okazaki, S. Ooi and K. Saito, Inog. Chem., (1983), 22, 1168-1174; b) J-P. Launay, Y.
Jeannin and M. Daoudi, Inorg. Chem., (1985), 24, 1052-1059

Intramolecular electron transfer in the solid phase: presenting a

unique example of single-crystal-to-single-crystal transformation from
a binuclear vanadium(V)-a lcoholate to an oligomeric vanadium(IV)-
aldehydic compound
Pabitra Baran Chatterjee,a Muktimoy Chaudhury,*,a

a
Dept. of Inorganic Chemistry, Indian Association for the Cultivation of Science, Kolkata-700 032, India,
email: icmc@iacs.res.in
Single-crystal-to-single-crystal (SCSC) transformations in the solid state involve coordinated

movement of atoms in the matrices. Most of these transformations are reversible, triggered by
light with a few thermally induced incidences are also known. Majority of these studies involve
organic molecules since crystals of metallo-organic frameworks can hardly retain their single
crystallinity after the rearrangements that happen in the solid phase. However, several similar
transformations involving coordination compounds have been reported in recent years,
accompanied by many interesting changes in properties such as host-guest behavior,
magnetism and photochemical reactivity. In the present work, we report an unprecedented
coordination driven oligomerization of a red colored dinuclear oxovanadium(V) compound
[V2O2L2] 1 involving 2,6-bis(hydroxymethyl)-p-cresol (H3L) as a bridging ligand to an infinite 1D
chain of greenish brown oxovanadium(IV) entity [V2O2(L*)2]α 2 through a SCSC irreversible
transformation pathway. The solid-state constitutional rearrangement of 1 to 2 is probably the
first case where an intramolecular-redox process, triggered by the oxidation of a coordinated
alkoxy group to an aldehydic moiety, generating two equivalents of electron which are
consumed by one equivalent each of vanadium(V) and hydrogen ion followed by solid-state self-
assembly to generate the product in almost 100 % yield. Confirmations in favor of this novel
SCSC transformation have come from time interval IR spectroscopy, magnetic susceptibility and
epr spectrum for the oligomeric vanadium(IV) compound 2 and more precisely from single-
crystal X-ray diffraction analyses. Perhaps the most interesting structural feature behind this
serendipitous SCSC transformation is the generation of a new ligand viz. 2-formyl-6-
hydroxymethyl-p-cresol (H2L*) involving two types of C-O bonds attached as side arms to the
aromatic ring unlike its predecessor (H3L).
Oxidation
Curing
Reduction
1 2

Electron transfer reactions of an amavadin-like complex
Jeremy M. Lenhardt,a Michael D. Johnson,a Debbie C. Crans,b Bharat Baruahb

a
Department of Chemistry and Biochemistry, New Mexico State University, Las Cruces, NM 88003
b
Department of Chemistry, Colorado State University, Fort Collins, CO 80523
email : crans@lamar.colostate.edu
The kinetics of the electron self-exchange process of amavadin and an amavadin model have
been studied using the Marcus cross relationship and directly measured using 51-V NMR line
broadening techniques with good agreement between the two methods. Outer-sphere electron
transfer reaction pathways are ascribed to both complexes. Exchange rates approximately two
orders of magnitude larger than other vanadium (IV/V) couples are reported. The results are
compared to previous studies with the natural product amavadin [1] and little change is found.
The significance of these studies will be discussed.
We thank the Luso-American Development Foundation for partial travel funds. We also thank NSF for
funding this research.
[1] J. Lenhardt, B. Baruah, D. C. Crans and M. D. Johnson, Chem. Comm. (2006) 4641-4643.

Interaction of hydroquinonate ligands with VV and MoVI
Chryssoula Drouza,a Anastasios D. Keramidas,b
a
Department of Agriculture Production, Biotechnology and Food Science, Cyprus University of Technology,
3603, Limasol, Cyprus, email: Chryssoula.drouza@cut.ac.cy
b
Department of Chemistry, University of Cyprus,1678 Nicosia, Cyprus
Study of the interaction of hydroquinones with redox active metal ions is of great importance
because such combination represents model systems for the electron and proton transfer
reactions in biological systems. Hydroquinone Vanadium and molybdenum participate in redox
reactions in biological systems like those of oxygen transfer systems (xanthine oxidases,
sulphate oxidases, nitrate reductases etc).1-4 On the other hand modified hydroquinone can
serve as connecting bridge between two redox centres, such as metal ions, thus allowing the
investigation of electronic interactions throughout the bridge.5 Hydroquinone has very low
oxidation potential thus does not stabilize metals in high oxidation state. In order to stabilize
the coordination of VIV/V and MoVI with hydroquinone we have synthesized modified
hydroquinones, one is shown in scheme 1. These ligands chelate and stabilize VIV/V and MoVI
ions forming stable complexes characterized with X-ray single crystal analysis.
O OH
O
OH
N OH
O N
HO
OH OH
O
Scheme 1. Ligand used in this work.
1D and 2D 1H NMR spectroscopies were used to characterize all complexes and investigate the
lability in aqueous solution. 2D EXSY spectra show an intramolecular exchange in aqueous
solution, and the mechanism is investigated.
Acknowledgements: The authors would like to thank PRF of Cyprus (TEXNO/0506/19) for their financial
support.
[1] Hille, R. Chem. Rev. 96, 2757 (1996).

[2] Collison, D., Garner, C. D., Joule, J. A., Chem. Soc. Rev. 25 (1996).
[3] D. Rehder, Coordination Chemical Reviews 182(1999) 197.
[4] C. Drouza, V. Tolis, V. Gramlich, C. Raptopoulou, A. Terzis, M.P. Sigalas, T.A. Kabanos, A.D. Keramidas,
Chem. Commun. (2002) 2786.
[5] Drouza, C., Keramidas, A. D. J. Inorg. Biochem. 80, 75 (2000).

New insight into the lipo-hydrophilic characterisation of a series of

antidiabetic VO(IV) and Zn(II) complexes and their carrier ligands
Éva Anna Enyedy,a Tamás Kissa
a
Department of Inorganic and Analytical Chemistry, University of Szeged, H-6701 Szeged, Hungary,
email: enyedy@chem.u-szeged.hu
The main target of the design of novel antidiabetic vanadium(IV) and zinc(II) complexes is
obviously to achieve compounds with higher biological activity and reduced side effects.
Complexation of these metal ions with carrier ligands leads to the protection against the
hydrolytic processes and to the formation of neutral, bis complexes enhancing their lipophilic
character and the scale of absorption from the digestive tract. Since the insulin-enhancing
effects of these complexes are closely correlated many times to their octanol-water distribution
coefficients among other factors [1], in the development of new metal complexes the
determination of this basic physico-chemical property is an important issue. The octanol-water
distribution coefficient of the carrier ligands has also effect on the binding to serum proteins,
which may have significant role in the metabolism of the antidiabetic complexes.
The lipo-hydrophilicity of a series of vanadium(IV) and zinc(II) complexes and their carrier
ligands were reinvestigated in the present work. It has involved a wide pH range study to
determine the pH independent constants (log P) for the ligands and the bis complexes
considering the actual chemical speciations and the individual UV-visible spectra of all species
formed in the systems with classic shake-flask method by the means of ICP-AES and UV-visible
spectrophotometry.
Acknowledgements: The authors would like to thank to the Hungarian Science Research Fund (OTKA
PD050011, T49417) for financial support.
[1] H. Sakurai, A. Katoh, Y. Yoshikawa, Bull. Chem. Soc. Jpn. 79 (2006) 1645-1664.

Syntheses and characterisation of novel [VO(O2)2L](L=ligand) type

complexes
Takeshi Higuchi,a Masato Hashimoto,a Seichi Okeya,a Yutaka Yoshikawa,b

Hiromu Sakuraic
a
Department of Material Science and Chemistry, Faculty of Systems Engineering, Wakayama University
Skaedani 930, Wakayama 640-8510, Japa, email: mh1043@sys.wakayama-u.ac.jp
b
Department of Bioinorganic Chemistry, Kyoto Pharmaceutical University, 5 Nakauchi-cho, Misasagi,
Yamashina-ku, Kyoto 607-8414, Japan
c
Institute of Oriental Medicine,Suzuka University of Medical Science, 1001-1 Kishioka-cho, Suzuka, Mie
513-0816, Japan, email: sakuraih@suzuka-u.ac.jp
Some vanadyl and [VO(O2)2L] type peroxo complexes are known to show the insulin-mimetic
effects. We therefore aimed at syntheses and X-ray and NMR structural analyses of novel
[VO(O2)2L] type complexes as well as analyses of their behaviour in aqueous media by NMR
(51V, 13C, 1H, 15N). The ligands used were amino acids which are common organic matters in the
biological systems, having various compositions and donor sites.
glycinato ligand
Structure of M[VO(O2)2(OCOCH2NH2)]·4H2O (M=Sr, Ca)
Amino acids such as glycine, L-alanine, L(+)-arginine, L-glutaminic acid, L-histidine, and L-
cysteine as well as a nucleobase adenine, have been tested as organic ligands. Formation of
several V-containing peroxo complexes were detected by 51V NMR. Among these complexes we
have been so far successful to crystallise M[VO(O2)2(OCOCH2NH2)]·4H2O (M=Sr, Ca) having a
glycinato ligand, and structurally analysed by a single crystal X-ray diffraction technique (see
figure). Attempts to crystallise other complexes are still ongoing. The decrement of a 51V signal
at about -750 ppm in the reaction solution after the crystallisation suggests that the signal can
be assigned to this complex. This complex was further characterised by IR, TG-DTA, 1H NMR,
13
C NMR, and organic elemental analyses. The complex salts were not soluble in organic
solvents such as ethanol, methanol, acetone and acetonitrile but soluble in water. The
solubilities were enhanced by adding NaCl or KCl. The detailed behaviour concerning dissolution
of the complex salts are now in investigation. Phosphate buffer (pH 7.2), in contrast, forced
immediate decomposition of the complexes which were detectable by 51V NMR. This behaviour
encouraged us to make biological tests, which are going on at present. Furthermore, attempts
to incorporate Zn(II), which is also known to be effective as an insulin-mimetic material, into
the peroxovanadate complexes are in progress. The results of these ongoing investigations will
also be presented in the poster.
Acknowledgements: The authors would like to thank Prof. Lage Pettersson at Umeå University for his kind
discussion and suggestions.

Density functional theory study of structure and NMR chemical shifts

of oxoperoxo vanadium(V) complexes of L-lactic acid
Licínia L.G. Justino,a,b M. Luísa Ramos,a,b Fernando Nogueira,c Abilio J.F.N Sobral,a
Carlos F.G.C. Geraldes,d,b Martin Kaupp,e Hugh D. Burrows,a Carlos Fiolhaisc and
Victor M.S. Gila
a
Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade de Coimbra,
3004-535 Coimbra, Portugal, email: liciniaj@qui.uc.pt
b
Centro de Neurociências e Biologia Celular, Universidade de Coimbra, Portugal.
c
Departamento de Física e Centro de Física Computacional, Faculdade de Ciências e Tecnologia,
Universidade de Coimbra, 3004-516 Coimbra, Portugal
d
Departamento de Bioquímica, Faculdade de Ciências e Tecnologia, Universidade de Coimbra,
3001-401 Coimbra, Portugal.
e
Institut für Anorganische Chemie, Universität Würzburg, Am Hubland, D-97074 Würzburg, Germany
Vanadium occurs in nature as a trace element. It is essential for several organisms and,
in particular, is implicated in the synthesis of chlorophyll in green plants and in the normal
growth of some animals.1 It is, possibly, also essential for humans.2 In recent decades, in vivo
and in vitro studies of the biological effects of this metal have revealed other important effects.
These include the ability to inhibit certain enzymes, the possibility of mimicking the effects of
insulin, the capacity to reduce cholesterol biosynthesis,3 in addition to antitumorigenic
properties.4 Peroxo V(V) complexes show antitumorigenic activity and also enhanced
insulinomimetic2,5 activity compared with the anionic salts of the higher oxidation states of
vanadium. Additionally, these complexes have been studied as functional models6 for the
haloperoxidase enzymes,7 and they are efficient oxidants for a variety of substrates.8
Previously,9 we have reported a study of the system V(V)–L-lactic acid–H2O2 in aqueous solution
using multinuclear NMR spectroscopy and have proposed structures for the corresponding
peroxo V(V) complexes of this acid. The solid state structure of one of these complexes has
been presented,10 but detailed information is lacking on the structures of the other complexes
found in aqueous solution. In this study we have applied density functional theory (DFT)
methods to study the structures, and to simulate the solution NMR chemical shifts of the
complexes. Various combinations of density functionals and pseudopotentials with associated
valence basis-sets were compared for reproducing the known solid-state data. Gas-phase
optimizations at the B3LYP/SBKJC level have been found to provide the overall best results. This
method was subsequently applied to all the V(V)-lactate-peroxide complexes found in solution.
The NMR chemical shifts were computed in all-electron DFT-IGLO calculations (UDFT-IGLO-
PW91 level). This provides a way to evaluate how close the theoretical structures are from the
solution ones. The chosen methodology was, additionally, able to predict and analyze a number
of interesting structural features for V(V) oxoperoxocomplexes of α-hydroxycarboxylic acids,
such as the bridging of the V(V) atoms in the V2O2 core of dinuclear complexes in the solid state
by hydroxy bridges and the preference for 1:1 V(V):peroxide stoichiometry and the very low
stability of complexes with 1:2 V(V):acid stoichiometry in aqueous solution.
Acknowledgments: LLGJ thanks “Fundação para a Ciência e a Tecnologia” for the postdoctoral grant
SFRH/BPD/26415/2006 and the “Laboratório de Computação Avançada”, of the Department of Physics of
the University of Coimbra, for the computing facilities (Milipeia cluster).
[1] D. Rehder, Angew. Chem. Int. Ed. Engl. 30 (1991) 148-167 and references therein.
[2] D.C. Crans, J.J. Smee, E. Gaidamauskas, L. Yang, Chem. Rev. 104 (2004) 849-902.
[3] N.D. Chasteen, Struct. Bonding 53 (1983) 105-138.
[4] C. Djordjevic, Met. Ions Biol. Syst. 31 (1995) 595-616.
[5] K.H. Thompson, J.H. McNeill, C. Orvig, Chem. Rev. 99 (1999) 2561-2572.
[6] G.J. Colpas, B.J. Hamstra, J.W. Kampf, V.L. Pecoraro, J. Am. Chem. Soc. 116 (1994) 3627-3628.
[7] A. Butler, J.V. Walker, Chem. Rev. 93 (1993) 1937-1944.
[8] T. Hirao, Chem. Rev. 97 (1997) 2707-2724.
[9] L.L.G. Justino, M.L. Ramos, M.M. Caldeira, V.M.S. Gil, Eur. J. Inorg. Chem. (2000) 1617-1621.
[10] P. Schwendt,; P. Švančárek, I. Smatanová, J. Marek, J. Inorg. Biochem. 80 (2000) 59-64.

Density functional theory study of the oxoperoxo vanadium(V)

complexes of glycolic acid. structural correlations with
NMR chemical shifts
Licínia L.G. Justino,a,b M. Luísa Ramos,a,b Martin Kaupp,c Hugh D. Burrows,a Carlos
Fiolhaisd and Victor M.S. Gila
a
Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade de Coimbra,
3004-535 Coimbra, Portugal, email: liciniaj@qui.uc.pt
b
Centro de Neurociências e Biologia Celular, Universidade de Coimbra, Portugal.
c
Institut für Anorganische Chemie, Universität Würzburg, Am Hubland, D-97074 Würzburg, Germany
d
Departamento de Física e Centro de Física Computacional, Faculdade de Ciências e Tecnologia,
Universidade de Coimbra, 3004-516 Coimbra, Portugal
In view of the relevance of vanadium compounds for both their biological and industrial
applications, we have carried out a DFT study of the structures and structural correlations with
NMR chemical shifts of oxoperoxo and dioxo V(V) complexes of glycolic acid. Peroxovanadium
complexes with α-hydroxycarboxylic acids are of particular relevance in biochemistry, since the
anions of many of these exist in biological media and are involved in a number of fundamental
physiological processes. Previously,1 we have studied the system V(V)–glycolic acid–H2O2 in
aqueous solution using multinuclear NMR spectroscopy and proposed structures for the
oxoperoxo V(V) complexes of this acid present in solution. The solid state structure of one of
these complexes is known.2 In this work we have applied the DFT B3LYP/SBKJC method, which
we previously validated for related systems,3 to calculate the gas-phase optimized geometries of
the V(V)–glycolate–peroxide complexes. Subsequently, we have calculated the 51V, 17O, 1H and
13
C chemical shifts for the theoretical geometries in all-electron DFT calculations at the UDFT-
IGLO-PW91 level. The theoretical chemical shifts have been compared with the experimental
solution values to assess the quality of the theoretical structures. With the objective of
understanding the major structural features determining the metal and oxo oxygen chemical
shifts in the NMR spectra of α-hydroxycarboxylate V(V) complexes, we have carried out a study
of the effects of structural changes on the 51V and 17O NMR chemical shifts for several glycolate
V(V) complexes, using the referred computational methodologies. The coordination of a small
ligand to the metal, the replacement of a fragment of a ligand by a different fragment and
changing the geometry of the complex have been considered. This investigation has shown, for
example, that structural modifications far from the metal nucleus do not significantly affect the
metal chemical shift, explaining why it is possible to establish reference scales that correlate the
type of complex (type of metal centre associated with a certain type of ligand) with its typical
range of metal chemical shifts, such as that formulated by Rehder.4 These studies have been
extended to small molecules used in quantitative analysis.
Acknowledgments: LLGJ thanks “Fundação para a Ciência e a Tecnologia” for the postdoctoral grant
SFRH/BPD/26415/2006 and the “Laboratório de Computação Avançada”, of the Department of Physics of
the University of Coimbra, for the computing facilities (Milipeia cluster).
[1] L.L.G. Justino, M.L. Ramos, M.M. Caldeira, V.M.S. Gil, Inorg. Chim. Acta 311 (2000) 119-125.
[2] P. Švančárek, P. Schwendt, J. Tatiersky, I. Smatanová, J. Marek, Monatsh. Chemie 131 (2000) 145-154.
[3] See poster in this symposium.
[4] D. Rehder. C. Weidemmann, A. Duch, W. Priebsch, Inorg. Chem. 27 (1988) 584-587.

Protein-protein interactions among vanadium-binding proteins and

related proteins in a vanadium-rich ascidian
Tatsuya Ueki, Koki Shintaku, Masao Yoshihara, Hitoshi Michibata
Department of Biological Science, Graduate School of Science, Hiroshima University, 1-3-1 Kagamiyama,
Higashi-Hiroshima 739-8526, Japan, email: ueki@hiroshima-u.ac.jp
Several species of ascidians can accumulate extremely high levels of vanadium ions in their
blood cells. We have been trying to identify and isolate proteins involved in this process. So far
we obtained several vanadium-binding proteins (Vanabins [1-3], GSTs, and VBPs) and putative
membrane transporters for vanadium, sulfate and protons from several species of ascidians. By
using one of Vanabins, we isolated a Vanabin-interacting protein 1 (VIP1) from blood cells of
Ascidia sydneiensis samea [4]. VIP1 was localized in the cytoplasm of signet ring cells and giant
cells. Using a two-hybrid method, we revealed that VIP1 interacted with Vanabins 1, 2, 3, and 4
but not with VanabinP. Furthermore, we found that Vanabin1 interacted with all of the other
Vanabins. From the blood plasma, we isolated a novel vanadium-binding protein named VBP-
129, and revealed that VBP-129 interacted with VanabinP regardless of the presence or absence
of vanadium ions [5]. These results indicated that two protein-protein interaction system
functions in A. sydneiensis samea; Vanabins and VIP1 in cytoplasm of signet ring cells, and
VanabinP and VBP-129 in blood plasma.
Figure 1. Known and putative protein-protein interaction network in vanadocytes.
Acknowledgements: The authors thank Mr. T. Morita and the staff at the International Coastal Research
Center of the Ocean Research Institute, The University of Tokyo, Otsuchi, Iwate, Japan, for their help in
collecting adult ascidians. This work was supported in part by Grants-in-Aids from the Ministry of Education,
Culture, Sports, Science, and Technology of Japan (#17370026 and 17651048 to H.M. and #18570070 to
T.U.) and a grant from the Toray Science Foundation (03-4402 to T.U.).
[1] T. Ueki, T. Adachi, S. Kawano, M. Aoshima, N. Yamaguchi, K. Kanamori, H. Michibata, Biochim. Biophys.
Acta 1626 (2003) 43-50.
[2] K. Fukui, T. Ueki, H. Ohya, H. Michibata, J. Am. Chem. Soc. 125 (2003) 6352-6353.
[3] T. Hamada, M. Asanuma, T. Ueki, F. Hayashi, N. Kobayashi, S. Yokoyama, H. Michibata, H. Hirota, J.
Am. Chem. Soc. 127 (2005) 4216-4222.
[4] T. Ueki, K. Shintaku, Y. Yonekawa, N. Takatsu, H. Yamada, T. Hamada, H. Hirota, H. Michibata, Biochim.
Biophys. Acta 1770 (2007) 951-957.
[5] M. Yoshihara, T. Ueki, N. Yamaguchi, K. Kamino, H. Michibata, Biochim. Biophys. Acta 1780 (2007) 256-
263.

Synthesis of new oxo-vanadium(IV) coordination compounds and

evaluation of their insulin mimetic actvity
Jessica Nilsson,a Matti Haukka,b Eva Degerman,c Dieter Rehder,d Ebbe Nordlandera
a
Inorganic Chemistry Research Group, Chemical Physics, Center for Chemistry and Chemical Engineering,
Lund University, Getingevägen 6, SE-22100 Lund, Sweden
b
Department of Chemistry, University of Joensuu, Box 111, FI-80101 Joensuu, Finland
c
Department of Experimental Medical Science, Biomedical Center, Lund University,
SE-221 48 Lund, Sweden
d
Institut für Anorganische und Angewandte Chemie, Universität Hamburg, Martin-Luther-King-Platz 6, D-
20146 Hamburg, Germany, email: jessica.nilsson@chemphys.lu.se
With the intention of preparing new insulin mimetic compounds, two new V(IV) oxo complexes
of the tetradentate ligand N-(2-hydroxybenzyl)-N,N-bis(2-pyridylmethyl)amine, L, (Figure 1a)
have been prepared and characterized by NMR and IR spectroscopy, mass spectrometry,
elemental analysis and X-ray diffraction. In vitro effects on the insulin signaling pathways of
the new complexes [VIVO(HSO4)(L)] (Figure 1b) and [VIVO(Cl2)(L)].MeOH as well as of a related
V(IV) oxo complex of trispyridylmethylamine1 have been investigated. Neither of the complexes
did, however, show the insulin mimetic effect observed for VOSO4 or Na3VO4 salts. In fact this
type of tetradentate coordinating ligands seems to inhibit the inherent insulin mimetic effect of
vanadium. To investigate this further we are now in the process of developing complexes
containing derivates of the original ligand, altering the coordination mode as well as the
hydro/lipophilicity.
a) b)
N N
N
OH
Figure 1. a) The ligand, N-(2-hydroxybenzyl)-N,N-bis(2-pyridylmethyl)amine, used for synthesis of the new

complexes, one of which is b) [VIVO(HSO4)(L)].
Acknowledgements: The authors would like to thank The Research School in Pharmaceutical Science (FLÄK),
The Swedish Foundation for International Cooperation in Research and Higher education (STINT), The
European Cooperation in the Field of Scientific and Technical Research (COST Action D21) and The Royal
Physiographic Society in Lund for financial support.
[1] Y. Tajika, K. Tsuge and Y. Sasaki, Dalton Trans. (2005), 1438-1447

The analysis and determination of vanadium IV in wastes collected

from mining ores in Nigeria.
Gloria Omoruyi, Olakunlemi Akinsulire, Oluwaseun Alao
Department of Chemistry, Obafemi Awolowo University, Adeyemi Campus, P.M.B 520, Ondo, Ondo State,
Nigeria. omruyig@yahoo.com
1-(2-Hydroxy-4-methoxybenzophenone)-4-phenylthiosemicarbazone (HMBPT) was investigated

as a new reagent for the flotation of vanadium(IV). At pH 1.5, vanadium(IV) forms a 1:1 pale-
violet complex with HMBPT in aqueous solution. An intense clear violet layer was formed after
flotation, by adding an oleic acid (HOL) surfactant. The composition of the float was 1:1
[V(IV)]:[HMBPT]. A highly selective and sensitive spectrophotometric procedure was proposed
for the determination of microamounts of V(IV) as its floated complex. The molar absorptivities
of the V(IV)-HMBPT and V(IV)-HMBPT-HOL systems were 0.4 × 104 and 0.12 × 105 L mol-1 cm-1
at 560 nm, respectively. The formation constants of the species formed in the presence and
absence of HOL were 4.6 × 107 and 8.7 × 105 L mol-1, respectively. Beer's law was obeyed up
to 1 × 10-4 mol L-1 in the aqueous layer as well as in the oleic acid layer. The HMBPT-V(IV)
complexes formed in the aqueous solution and scum layer were characterized by elemental
analysis, infrared and UV spectrophotometric studies. The mode of chelation between V(IV) and
HMBPT is proposed to be due to a reaction between the protonated bidentate HMBPT ligand and
V(IV) through the S=C and N=C groups. Interferences from various foreign ions were avoided
by adding excess HMBPT and/or Na2S2O3 as a masking agent. The proposed flotation1 method
was successfully applied to the analysis of V(IV) in synthetic mixtures, wastes of power stations,
simulated samples and in real ores. The separation mechanism is discussed.
G . A. Whittlow, S. E. Lee, R. R. Mullir, R. A. Wenglar and T. P. Sherlock, J. Eng. For Power, (1988), 105,
88.
A. I. Vogel “A Text Book of Quantitative Inorganic Analysis”, (1994), Longman, London.
Koleso, A.O, Chemistry of Vanadium, (2000).

Vanadium induced cyclization of thiosemicarbazone: formation of

heptanuclear mixed valence V(IV)/V(V) complex
Mirta Rubčić,a Ivica Đilović,a Marina Cindrić,a Dubravka Matković-Čalogovića

a
Laboratory of General and Inorganic Chemistry, Department of Chemistry, Faculty of Science, University of
Zagreb, Horvatovac 102a, Zagreb, Croatia, e-mail: mirta@chem.pmf.hr
Thiosemicarbazones, a small organic molecules which belong to a family of thiourea

derivatives, are associated with various biological activities including antibacterial, antiviral and
antitumor.[1] As ligands, they can coordinate to metal ions in diverse manners due to the
number of mixed soft-hard donor atoms and conformational flexibility.[2] Furthermore, under
the influence of metal cations as oxidants they can easily undergo ring closure process affording
variety of heterocyclic rings.[3] Data in the literature reveal that various metal cations, such as
Ag(I), Zn(II), V(IV) etc., are capable of inducing cyclization reactions of thiosemicarbazone or
related dithiocarbazate systems.[4]
Recently, we have reported two new thiazoline compounds obtained by vanadium
induced cyclization of acetylacetone and thiosemicarbazone ligands.[5] As a continuation of the
previous research, we have investigated the reactions of oxovanadium(IV) acetylacetonate and
salicylaldehyde 4-phenylthiosemicarbazone (H2L) in the presence of different bases (imidazole,
4-picoline and pyridine) under inert atmosphere. When imidazole (im) or 4-picoline (4-pic) were
used mononuclear vanadium(IV) complexes, [VO(L)(im)] (Figure 1(a)) and [VO(L)(4-pic)] were
obtained. Interestingly, in the case of pyridine we isolated previously reported thiazoline
compound [5] and polinuclear mixed-valence V(IV)/V(V) complex, [V7O14(Lcycl)3(py)3] (Figure
1(b)). In the polinuclear complex with unprecented [V7O14]3- core, vanadium atoms are
coordinated by bridging ligands containing 1,2,4-thiadiazole ring, as a product of vanadium
induced oxidative cyclization, and pyridine as ancillary ligands.
(a) (b)
Figure 1. (a) [VO(L)(im)]; (b) [V7O14(Lcycl)3(py)3].
All isolated products were identified and characterised by means of chemical analysis (C
H, N, S), IR spectroscopy, thermogravimetric methods and when possible by single crystal X-ray
diffraction method.
[1] (a) W.-X. Hu, W. Zhou, C.-N. Xia, X. Wen, Bioorg. Med. Chem. Lett. 16 (2006) 2213–2218. (b) N.
Bharti, K. Husain, M. T. G. Garza, D. E.Cruz-Vega, J. Castro-Garza, B. D. Mata-Cardenas, F. Naqvi, A. Azam
Bioorg. Med. Chem. Lett. 12 (2002) 3475–3478. (c) D. F. Smee, R. W. Sidwell Antiviral Research 57 (2003)
41–52.
[2] J.S.Casas, M.S.Garcıa-Tasende, J. Sordo, Coord. Chem. Rev. 209 (2000) 197-261.
[3] P. Lo Meo, M.Gruttadauria, R. Noto Arkivoc i (2005) 114-129.
[4](a) A. Castineiras, I. Garcıa-Santos, S. Dehnen, P. Sevillano Polyhedron 25 (2006) 3653-3660. (b) J. S.
Casas, M. V. Castano, E. E. Castellano, J. Ellena, M. S. Garcıa-Tasende, A. Gato, A. Sanchez, L. M. Sanjuan,
J. Sordo Inorg. Chem. 41 (2002) 1550-1557. (c) S. K. Dutta, S. Samanta, D. Ghosh, R. J. Butcher, M.
Chaudhury Inorg. Chem. 41 (2002) 5555-5560.
[5]M. Cindrić, M. Rubčić, I. Đilović, G. Giester, B. Kamenar Croat. Chem. Acta 80 (2007) 583-590.

A new vanadium(V)-peroxo species in the presence of physiological

citrate. The missing link in the structural speciation of the V(V)-
peroxo-citrate system.
Athanasios Salifoglou, Catherine Gabriel
Department of Chemical Engineering, Aristotle University of Thessaloniki, 54124 Thessaloniki, Greece

email: salif@auth.gr
Vanadium is an essential element, which exists in all organisms at low concentration.

Vanadium participation in a plethora of biological systems and abiotic applications, has spawn
considerable research over its role in nature, its potential use in pharmaceutical therapeutics
and generally its biological action.1 The latter is supported by the fact that vanadium plays a
catalytic role in metalloenzyme systems such as nitrogenase and haloperoxidases.2 As an
inorganic cofactor, vanadium possesses and promotes bioactivities, ranging from
antitumorigenicity to mitogenicity, inhibition of metabolic enzymes such as
phosphoglucomutases2,3 and others.1 Outstanding in this regard is its influence in the
heterogeneous syndrome of Diabetes mellitus through its insulin mimetic action.4,5 In an effort
to understand the aqueous chemistry of insulin mimesis exhibited by vanadium in its biologically
relevant oxidation states V(IV,V), well-designed synthetic approaches were developed at the
binary and ternary level with physiological ligands. Among the various ligand-substrates
studied in the presence of vanadium were α-hydroxycarboxylate-containing organic ligands, the
most biologically relevant of which was citric acid. Citric acid exists in human plasma6,
promoting chemical interactions with metal ions and variably influencing key metabolic
functions. In view of the significance of the above mentioned (bio)chemistry, aqueous
vanadium-peroxo-citrate complexes were targeted.7 Consequently, the chemical reactivity of
V(V)-peroxo-citrate system was investigated under control of the molar stoichiometry and pH-
dependent conditions leading to a new ternary complex
[V2O2(O2)2(C6H5O7)2][quanidiniumH]4.6H2O (1).
The synthesized complex was fully characterized by numerous spectroscopic (FT-IR, UV-Visible,
and multinuclear NMR), electrochemical (cyclic voltammetric), and ultimately X-ray
crystallographic techniques. The structural nature of this species emphasizes the degree of
deprotonation of citric acid in formulating the coordination environment of V(V) in the presence
of H2O2. To this end, the existence of such a ternary species emerges in consonance with the
other existing analogous species and justifies its presence on the requisite speciation scheme as
a competent structural variant. Hence, species 1 is the missing link in the structural speciation
of the ternary V(V)-peroxo-citrate, completing the family of species bearing deprotonated forms
of citrate and exhibiting variable structural features as a result of their synthetic assembly and
isolation from solutions covering the physiological pH range. Collectively, the physicochemical
properties of 1 formulate the profile of ternary V(V)-peroxo-citrate species arising in aqueous
media and shed light onto the chemical reactivity of vanadium participating in insulin mimetic
activity.
Acknowledgements: This work was supported by and by a ‘‘PENED” grant co-financed by the E.U.-European
Social Fund (75%) and the Greek Ministry of Development-GSRT (25%).
[1] In Metal Ions in Biological System: Edited by Sigel, H., and Sigel, A.. Marcel Dekker, Inc., New York NY,
(1995), pp. 325-362, 407-425, 558-560.
[2] a) J. K. Klarlund, Cel, 41, (1985), 707-717. b) J. B. Smith, Proc. Natl. Acad. Sci. USA 80, (1983),
6162-6167.
[3] a) K. M. Walton, J. E. Dixon, Annu. Rev. Biochem. 62, (1993),101-120. b) K.-H. W. Lau, J. R. Farley, D.
J. Baylink, Biochem. J. 257, (1989), 23-36.
[4] H. Sakurai, Y. Kojima, Y. Yoshikawa. K. Kawabe, H. Yasui, Coord.Chem. Rev. 226, (2002), 187.
[5] D. L. Flynn, J. Med. Chem. 35, (1992), 1489-1491.
[6] H. A. Krebs, W. A. Johnson, Enzymologia 4, (1937), 148-156.
[7] a) M. Kaliva, C. P. Raptopoulou, A. Terzis, A.Salifoglou, J. Inorg. Biochem. 93, (2003), 161-173. b) M.
Kaliva, E. Kyriakakis, C. Gabriel, C.P. Raptopoulou, A. Terzis, J.-P. Tuchagues, A.Salifoglou, Inorganica Chimica
Acta 359, 14, (2006),4535-4548.

New C-functionalized tris(pyrazolyl)methanes and their vanadium

complexes
Telma F.S. Silva,a,c Riccardo Wanke,c Luísa M.D.R.S. Martins,b,c

Armando J.L. Pombeiroc
a
Área Científica de Física, ISEL, R. Conselheiro Emídio Navarro, 1959-007 Lisbon, Portugal,
b
Departamento de Engenharia Química, ISEL, R. Conselheiro Emídio Navarro, 1959-007 Lisbon, Portugal,
c
Centro de Química Estrutural, IST, TU, Av. Rovisco Pais, 1049-001 Lisbon, Portugal,
email: tsilva@dem.isel.ipl.pt
Recently, we have initiated the study of the coordination chemistry of hydrotris(1-

pyrazolyl)methane, HC(pz)3 (pz = pyrazolyl), and its derivatives bearing substituents on the
pyrazolyl rings (e.g., hydrotris(3,5-dimethyl-1-pyrazolyl)methane, HC(3,5-Me2pz)3) or the C-
methine carbon-substituted tris(1-pyrazolyl)methanesulfonate (as its lithium salt Li[SO3C(pz)3]),
towards V, Fe, Cu or Re centres.1-5 In addition, we have found that some of the synthesized
scorpionate complexes of those metals can act as selective catalysts in the single-pot oxidation
of ethane to acetic acid and in the peroxidative oxidation of cyclohexane to cyclohexanol and
cyclohexanone.
Herein we report the study of the reactivity of hydrotris(1-pyrazolyl)methane towards the

methine carbon functionalization and the coordination of the obtained C-functionalized
scorpionates to a V centre. Hence we have prepared C-functionalized tris(pyrazolyl)methane
derivatives RC(pz)3, R= CH2OH or new CH2OCH2(py) (py = pyridyl ring), and investigated their
behavior at vanadium(III) centres:
N N
HO C N N 3 or Cl N
O C N N 3
VCl3 Cl V C R
MeOH or THF, reflux N N
Cl
N N
R = HOCH2 or pyCH2OCH2
The synthesis and characterization of the new scorpionate and V-complexes are reported.
Acknowledgements: The work has been partially supported by the Fundação para a Ciência e Tecnologia
(FCT) and its POCI 2010 programme (FEDER funded).
[1] T.F.S. Silva, L.M.D.R.S. Martins, E.C.B.A. Alegria, A.J.L. Pombeiro, Adv. Synth. Catal. 350 (2008) 706.
[2] E.C.B. Alegria, M.V. Kirillova, L.M.D.R.S. Martins, A.J.L. Pombeiro, Appl. Catal. A: Gen. 317 (2007) 43.
[3] T.F.S. Silva, L.M.D.R.S. Martins, M.F.C.G. Silva, A.J.L. Pombeiro, Acta Cryst. E, 63 (2007) m1979.
[4] E.C.B. Alegria, L.M.D.R.S. Martins. M. Haukka, A. J.L. Pombeiro, Dalton Trans (2006) 1.
[5] E.C.B. Alegria, L.M.D.R.S. Martins, M.F.C.G. Silva, A.J.L. Pombeiro, J. Organomet. Chem. 690 (2005)
1947.

Synthesis, molecular and supramolecular structures of oxo compounds

formed by biologically active central atom, heteroligand/s and
counterions: vanadium(V), pyridine or pyrazine carboxylates and
amides
Michal Siváka, Peter Schwendta, Silvia Pacigováa and Gyepes Róbertb
a
Department of Inorganic Chemistry, Comenius University, Faculty of Natural Sciences, Mlynská dolina,
842 15 Bratislava, Slovak Republic, b Department of Inorganic Chemistry, Charles´ University, Faculty of
Natural Sciences, Prague, Albertov, 128 00 Prague, Czech Republic, e-mail: sivak@fns.uniba.sk
In the reaction systems V2O5 – H2O2 – L1 – L2 – H2O, the interaction of vanadium(V) with
organic compounds L1 and L2: dipicolinate (dipic), picolinate (pic), quinolinate (1-) (Hquin),
pyrazinate (pca), picolinamide (pa), nicotinamide (1-Hnica), isonicotinamide (inica) or
pyrazinamide (pcaa), which exhibit either as free substances or bonded in coordination
compounds different biological activities, resulted in formation of crystalline oxo, and oxo
peroxo compounds: (Hpa)[VO(O2)dipic(H2O)]•H2O (1), (Hnica)[VO(O2)dipic(H2O)] (2),
[VO(O2)(pic)(pa)]·H2O (3), [VO(O2)(Hquin)(pa)]·2H2O (4) (Figure 1, left) , [VO(O2)(pca)(pa)]
(5), (1-Hnica)6V10O28·2H2O (6) and (H-inica)4H2V10O28· inica (7). The coordination of two
bidentate ligands in pentagonal bipyramidal complexes 3 – 5 to the VO(O2)+ group with a triple
V≡O(oxo) bond1 too confirm our empirical stereochemical rules2.
Figure 1. Molecular structure of 4 (left) and anion- π interactions between pca ligands in 5 (right).
The supramolecular structures of 1-7 are constructed by hydrogen bonds („classical“ and C-
H•••O) and interactions between the π - electrons of aromatic rings: parallel/non-parallel
displaced π - π or the rare anion- π interactions in 3 and 5 (Figure 1, right), the latter also
confirmed by DFT calculations of electrostatic potential distributions and MOs for the solid state.
Acknowledgements: Authors would like to thank the Ministries of Eduction of: the Slovak Republic (grant
VEGA 1/4462/07) and Czech Republic (grant GA 203/99/M037 ), and Comenius University Bratislava (grant
UK 172/2007) for their financial support.
[1] S. Pacigová, R. Gyepes, J. Tatiersky, M. Sivák, , Dalton Trans. (2008), 121-130

[2] J. Tatiersky, P. Schwendt, M. Sivák, J. Marek, Dalton Trans. (2005), 1-7

Bi- and hexanuclear vanadium (IV) complexes of a p-hydroquinone-

based ligand: synthesis and structural characterization
Marios Stylianou and Anastasios D. Keramidas
Department of Chemistry, University of Cyprus, Nicosia 1678, Cyprus,

email: chpgms1@ucy.ac.cy
It is well established that the electron transfer reactions of p-quinones, along with their redox
products, p-semiquinones and p-hydroquinones play an important role in biological systems.1,2
Vanadium also participates in biological processes as a catalyst in the active sites of
metalloenzymes. Consequently, vanadium chemistry with hydroquinone-based ligands, may
have immediate implications on its role in its action as a biological agent and thus, may give
fundamental aspects of the electron transfer reactions between transition metal centres and p-
quinone cofactors.3 In an effort to comprehend the interaction and the aqueous chemistry of
vanadium (IV) and p-dioxolene ligands, reactions of vanadium (IV) salts and an electron-active
bis-substituted p-hydroquinonate ligand were pursued in water and led to isolation of V(IV)-p-
hydroquinonate complexes, the structure and properties of which depend strongly on the
solution pH. X-ray crystallography revealed the formation of bi- (1) and hexa-nuclear (2)
vanadium (IV) complexes where the metal atom in both molecules coordinated in an octahedral
geometry. In 1, three binuclear complexes formed an open triangular array where the average
distance between the neighboring metal centres is 8.6 Å while in 2, three binuclear complexes,
analog to 1, are connected to each other via VIV-O-VIV bridges forming the hexanuclear
structural motif illustrated in Figure 1. For both compounds, BVS calculations confirmed
vanadium's oxidation state as IV, and in conjuction with X-ray crystallography ligand’s oxidation
state was assigned as p-hydroquinone. FT-IR confirmed metal atom’s coordination and thus
ligand’s oxidation state in both complexes, while elemental analysis (CHN) confirmed their
purity. Magnetic susceptibility measurements in the solid state at room temperature for 1 and 2
supported their paramagnetism.
Figure 1. Molecular structure of the hexanuclear VIV-p-hydroquinonate complex 2.
Acknowledgements: The authors would like to thank the Research Promotion Foundation of Cyprus for the
financial support of this work with the proposal TEXNO/0506/19 (BYKH).
[1] M. R. A. Blomberg, P. E. M. Siegbahn, and G. T. Babcock, J. Am. Chem. Soc. 120 (1998) 8812-8824.
[2] M. S. Craige, M. L. Paddock, J. M. Bruce, G. Feher, and M. Y. Okamura, J. Am. Chem. Soc. 118 (1996)
9005-9016.
[3] C. Drouza, V. Tolis, V. Gramlich, C. Raptopoulou, M. P. Sigalas, T. A. Kabanos, and A. D. Keramidas,
Chem. Commun. (2002) 2786-2787.

The effect of ionic strength on the stability constant of vanadium(IV)

complex with methionine
Karim Zare,a,b Saied Abedini Khorrami,c Bahareh Khorramdinc

a
b
c
Chemistry Department, Islamic Azad University, North Tehran Branch, Tehran, Iran
email: kzare110@hotmail.com
The equilibrium of vanadium(IV) complex formed by methionine in acidic media has been
investigated by a combination of potentiometric and spectrophotometric techniques. The metal-
ligand equilibria were studied at 25 ± 0.1ºC in the ionic range of interest 0.1 < I < 1 mole dm-3
of sodium perchlorate. Oxyvanadium has been reported as VO2+ ion in the pH range of 1.3 < pH
< 2.5. Under these experimental conditions, hydrolysis of vanadium(IV) was negligible and the
1:1 complex has the formula VOHY, where Y- represents the fully dissociated amino carboxylate
anion. All of the stability constants have been determined at various wavelengths. Comparison
of the ionic strength effect on this complex formation reaction has been made using a Debye-
Huckel type equation. The method based on the relationship A=f(pH) was employed, on account
of the high stability of the complexes studied. Absorbance and pH was measured for solution
containing a large excess of the ligand.1-4

[2] P. Lagrange, M. Schneider, K. Zare, J. Lagrange, Polyhedron 13 (1994) 861-867.
[3] F. Gharib, K. Zare, S.A. Khorrami, J. Chem. Eng. Data 40 (1995) 186-189.
[4] K. Zare, P. Lagrange, J. Lagrange, J. Chem. Soc. Dalton Trans. (1979) 1372-1376.

Interaction of a pyrimidinone-V(IV) complex with human serum

transferrin
Gisela Gonçalves,a João Costa Pessoa,a Isabel Tomaz,a,b M.Margarida C.A. Castro,c
Carlos F.G.C. Geraldes,c Fernando Avecillad
a
Centro de Química Estrutural, Instituto Superior Técnico, Av. Rovísco Pais, TU Lisbon,
1049-001 Lisboa Portugal, email: gisela.goncalves@mail.ist.utl.pt
b
Centro de Ciências Moleculares e Materiais, Faculdade de Ciências da Universidade de Lisboa,
Campo Grande 1749-016 Lisboa - Portugal;
c
Dpto. de Bioquímica e Centro de RMN, Universidade de Coimbra, 3001-401 Coimbra, Portugal;
d
Dpto. de Química Fundamental, Universidade da Coruña, A Coruña 15071, Spain.
In the last years, research in vanadium chemistry has gained new impetus: in addition to the
potential benefits of vanadium compounds for the oral treatment of Diabetes, its anti-tumour
potential has also been recognized 1.
It has been proposed that in higher organisms the delivery of vanadium into cells can be
promoted by natural carriers such as plasma proteins, particularly by the human serum
transferrin 2.
The vanadium complexes of maltol and ethylmaltol are promising compounds for the oral
treatment of Diabetes, 1 and pyridinone complexes have also been considered. We prepared a
pyrimidinone ligand MHCPE (2-methyl-3H-5-hydroxy-6-carboxy-4-pyrimidinone ethyl ester),
and studied its complexation with VIVO2+ and VVO2+ by potentiometry, UV-Vis, EPR and NMR
spectroscopy. MHCPE is an an efficient ligand for both V(IV) and V(V). The complexes are quite
stable, complex formation starting at pH lower than two.
In this work we report and discuss some results regarding the interaction of vanadium, and
vanadium(IV)-MHCPE complexes with human serum transferrin (hTF) by circular dichroism (CD)
and EPR spectroscopy. By CD the 200-250 nm, 250-330 nm and 400-1000 nm were examined
separately, as give distinct information regarding the interaction of V-species with hTf. Namely,
the existence of CD signal in the 400-1000 nm is a clear indication of the binding of VIVO-
species to chiral hTf sites. It is concluded that the ternary system, VIVO-MHCPE-transferrin,
leads to a stronger binding than for the binary VIVO-transferrin species. Moreover, the order of
mixing the reagents (VIVO + MHCPE + hTF) appears to have influence upon the CD spectra
recorded.
We anticipate MHCPE can be an effective ligand to improve vanadium transport in blood
plasma if the MHCPE ligand is also absorbed in the gastro-intestinal tract.
O
O
OH
N
H3C N O
H
Figure 1. Structure of the ligand MHCPE (2-methyl-3H-5-hydroxy-6-carboxy-4-pyrimidinone ethyl ester)
Acknowledgements: The authors wish to thank to the Fundação para a Ciência e Tecnologia,
(SFRH/BD/32131/2006 and SFRH/BPD/34695/2007), FEDER POCI 2010 and PPCDT/QUI/56949/2004, the
Spanish-Portuguese Bilateral Programme (Acção Integrada E-56/05) and University of A Coruña for financial
support.
[1] K.H. Thompson and C. Orvig, J. Inorg. Biochem., 100 (2006) 1925-1953.
[2] T. Kiss, T. Jakusch, D. Hollender, A. Dörnyei, E. A. Enyedy, J. Costa Pessoa, H. Sakurai and A. Sanz-
Medel, Coord. Chem. Rev., Vol. 252 (2008) 1153-1162.

VIVO complexes with bis(pyridyl) derivatives
Daniele Sanna,a Giovanni Micera,b Luisa Pisano,b

Eugenio Garribba,b Dóra Kiss,c Katalin Várnagy,c
a
Istututo CNR di Chimica Biomolecolare, I-07040 Sassari, Italy, email: Daniele.Sanna@icb.cnr.it;
b
Dipartimento di Chimica, Università di Sassari, Via Vienna 2,I-07100 Sassari, Italy
c
Department of Inorganic and Analytical Chemistry, University of Debrecen, H-4010 Debrecen, Hungary
Oxovanadium(IV) complexes of bis(imidazolyl) derivatives of amino acids have been recently

examined by some of us.1 The bis(imidazolyl) moiety acts as an anchoring group and avoids
hydrolysis and precipitation of vanadium hydroxide allowing the deprotonation and coordination
of the amide nitrogen. Pyridine nitrogen is known as a good donor group in vanadium
coordination chemistry2 and bis(pyridyl) derivatives of amino acids could keep VO2+ ion in
solution in the acidic pH range and favour the binding of the amide nitrogen.
In this context we studied the coordinating properties of a series of bis(pyridyl) derivatives
through the combined application of potentiometric and spectroscopic methods. In particular we
examined 2,2’-dipyridylmethane and its derivatives, 2,2’dipyridylketone, 2,2’-dipyridylmethanol
and 2,2’-dipyridylamine and two amino acid derivatives of 2,2’-dipyridylmethylamine (DPMA),
namely N-glycyl-DPMA and N-histidyl-DPMA.
The results show that the simple bis(pyridyl) derivatives, having only Npyridine donor atoms, form
mono-chelated complexes, while the derivatives with a carbonyl or hydroxyl groups also
complexes with (Npyr, CO/O–) coordination. To assign the binding modes to the various species
bidentate ligands, 2-acetylpyridine and 2-pyridinemethanol, have been used as simple models.
The 51V hyperfine coupling constant (Az) of the complexes with 2x(N, O–) coordination shows an
anomalously low value. This anomalous reduction will be discussed and possible explanations
will be proposed. With the two amino acid derivatives, N-glycyl- and N-histidyl-DPMA, the metal
binding starts with the formation of complexes with bis(pyridyl) coordination and continues at
higher pH values with the coordination of the amino and deprotonated amide groups.
Figure 1. Calculated structure of the complex [VO(N-glycyl-pyridylmethylamine)(OH)].
DFT calculations were performed to obtain information on the structure of the species formed by
N-glycyl-DPMA and N-histidyl-DPMA. DFT methods were also used to predict the 51V hyperfine
coupling constant for vanadyl-pyridine complexes. The calculations on the model complex
[VO(pyridine)(H2O)4]2+, with an equatorially coordinated pyridine, show that Az value depends
on the orientation of the pyridine ring with respect to the V=O bond, analogously to what
experimentally and theoretically found for the species with imidazole.3, 4
[1] K. Várnagy, T. Csorba, D. Kiss, E. Garribba, G. Micera, D. Sanna, Eur. J. Inorg. Chem. (2007) 4884–
4896.
[2] T. Duma, R. Hancock, J. Coord. Chem. 32 (1994) 135-146.
[3] T. S. Smith II, C. A. Roof, J. W. Kampf, P. G. Rasmussen, V. L. Pecoraro, J. Am. Chem. Soc. 122 (2000)
767-775.
[4] A. C. Saladino, S. C. Larsen, J. Phys. Chem. A 106 (2002), 10444-10451.

Interaction of insulin-enhancing vanadium compounds with transferrin

and low molecular mass bioligands
Daniele Sanna,a Giovanni Micera,b Eugenio Garribba,b

a
Istututo CNR di Chimica Biomolecolare, I-07040 Sassari, Italy, email: Daniele.Sanna@icb.cnr.it;
b
Dipartimento di Chimica, Università di Sassari, I-07100 Sassari, Italy
The interaction of human serum transferrin (hTf) with VO(IV) and a series of insulin-enhancing
vanadium compounds, namely cis-[VO(picolinato)2(H2O)], [VO(6-methylpicolinato)2],
[VO(acetylacetonato)2], and [VO(maltolato)2]) has been examined in aqueous solutions using
frozen solution electron paramagnetic resonance (EPR) spectroscopy.
Moreover the interaction of insulin-enhancing vanadium compounds with transferrin and low
molecular weight ligands of the blood serum (lactic and citric acids) has been considered. For
comparison the system hTf-VO(IV) has been reexamined.
The results show that in the binary system VO(IV)-hTf, as previously reported,1 the metal ion
can occupy three different binding sites, A, B1 and B2, identified with the two N- and C-terminal
coordination sites of hTf for Fe(III). The synergic anion bicarbonate is necessary for the metal
binding analogously as reported in the case of iron; this ligand, however, can be replaced by
different anions like citrate or lactate.
When considering the interaction of the insulin-enhancing compounds with hTf, the prevalent
vanadium complexes present in solution depend on the stability of the binary VO(IV)-carrier
species. With strong carriers the main species present in solution can be identified as a ternary
complex with hTf and a carrier molecule; with intermediate carriers mixed complexes VO(IV)-
hTf-carrier and VO(IV)-hTf-lactate (or citrate) are formed, while with weak carriers the
vanadium is present in solution mainly as (VO)2hTf, the binary complex with hTf.
Besides hTf, human serum albumin (HSA), can be involved in the transport of the insulin
mimetic vanadium compounds in the blood serum.2 Since the relative stabilities of the vanadium
complexes with hTf and HSA are unknown we examined the ternary system VO(IV)-hTf-HSA at
different ratios and concentrations.
EPR results show that human serum transferrin seems to be the preferred ligand for the
oxovanadium(IV) ion. However, as it will be explained in detail, the vanadium binding to human
serum albumin cannot be completely excluded and this means that both these high molecular
mass ligands of the blood serum (i.e. hTf and HSA) contribute to the transport of the insulin-
enhancing vanadium compounds to the target organs, with hTf being the preferred one.
Figure 1. Anisotropic EPR spectra of the systems VO(IV)-hTf, VO(IV)-hTf-lactate and VO(IV)-lactate.
[1] N. D. Chasteen, in Biological Magnetic Resonance; Plenum Press: 1981, vol. 3, pp. 53-119 and
references therein.
[2] B. D. Liboiron, K. H. Thompson, G. R. Hanson, E. Lam, N. Aebischer, C. Orvig, J. Am. Chem. Soc. 127
(2005) 5104-5115.

The effects of the trigonal bipyramidal distortion on the spectroscopic

and electrochemical properties of VIVO bis-chelated species
Eugenio Garribba,a Giovanni Micera,a Daniele Sanna,b Elzbieta Lodyga-Chruscinska,c

a
Dipartimento di Chimica, Università di Sassari, Via Vienna 2, 07100 Sassari, Italy, email: garribba@uniss.it;
b
Istituto C.N.R. di Chimica Biomolecolare, Trav. La Crucca 3, 07040 Li Punti, Sassari, Italy
c
Institute of General Food Chemistry, Technical University of Lodz, ul. Stefanowskiego, 90924 Lodz, Poland
Among the five-coordinated VIVO complexes, those with square-pyramidal geometry are the
most common. Only few examples of a geometry close to the trigonal bipyramid were described
in the literature.1
In this work the behaviour of the bis-chelated VIVO complexes formed by simple (glycolic, 2-
hydroxyisobutiric, 2-ethyl-2-hydroxybutiric and benzilic) and complex (citric and D-, L-, DL-
tartaric) α-hydroxycarboxylic acids was studied. The structure of the VOL2H−2 species in aqueous
solution was simulated by DFT methods with Gaussian 03 software, which provide a valid tool
for the optimization of the structures of complexes in absence of X-ray single crystal analysis.
EPR spectra of trigonal bipyramidal distorted species are rhombic with three g (gx ≠ gy ≠ gz)
and three A values (Ax ≠ Ay ≠ Az), whereas electronic absorption spectra are characterized by
four transitions between 400 and 850 nm: this is due to the loss of degeneracy of the dxz and
dyz atomic orbitals.2 It was found that in aqueous solution the distortion follows the steric
hindrance of the substituents on the α-carbon atom and the hydrophobicity of the ligands. The
trigonal bipyramidal distortion, expressed by the structural index of trigonality τ,3 can be
correlated with the values of: i) |Ax – Ay|, where Ax and Ay are the 51V hyperfine coupling
constants along the x and y axes in the anisotropic EPR spectrum; ii) Δλ = λ2 – λ3, where λ2 and
λ3 are the central bands in the electronic absorption spectrum; and iii) the half-wave potential
E1/2 for the oxidation of [VIVO(LH−1)2]x− to the corresponding VVO2 species [VVO2(LH−1)2](x−1)− in
the cyclic voltammogram. The results are confirmed by DFT calculations which show that the
trigonal bipyramidal distortion results in a four-band electronic spectrum.
Figure 1. Effect of the trigonal bipyramidal distortion τ of VIVO complexes of α-hydroxycarboxylates on Δλ.
We think that the results are of general validity and can be applied to every penta-coordinated
VIVO complex formed by bidentate ligands to determine its trigonal bipyramidal distortion.
[1] C. R. Cornman, K. M. Geisre-Bush, S. R. Rowley, P. D. Boyle, Inorg. Chem. 36 (1997) 6401-6408.

[2] E. Garribba, G. Micera, A. Panzanelli, D. Sanna, Inorg. Chem. 42 (2003) 3981-3987.
[3] A. W. Addison, T. N. Rao, J. Reedijk, J. van Rijn, G. C. Verschoor, Dalton Trans. (1984) 1349-1356.

VO(oda): a vanadyl(IV) complex with an OOO-donor group.

Bioactivity on human colon adenocarcinoma Caco-2 cell line.
Josefina Rivadeneiraa,b,Cecilia I. Mugliaa, Enrique J. Barana,b, Liliana Bruzzonea,

Susana B. Etcheverrya,b
a
Facultad de Ciencias Exactas, UNLP. 47 y 115 (1900) La Plata, Argentina etcheverry@biol.unlp.edu.a
b
CEQUINOR (CONICET-UNLP), Facultad de Ciencias Exactas, UNLP, La Plata, Argentina
Vanadium is a trace element widespread distributed in nature. Vanadium compounds have

attracted scientific attention due to their potential therapeutic applications. The pharmacological
effects of vanadium include insulin mimetic actions, osteogenic and antitumoral effects. In
particular, the antitumoral actions of vanadium can be evaluated by the determination of different
parameters such as cell proliferation, morphology and disruption of cellular architecture. Vanadium
compounds exert their antineoplastic actions by different mechanisms (inhibition of key protein
tyrosine phosphatases, changes in cell cytoskeleton proteins, and disturbance of redox equilibria in
the cells that causes an increment in the oxidative stress and alterations in the ratio GSH/ GSSG).
Altogether, these effects may lead to the induction of apoptosis and/or necrosis, and finally to cell
death.
On the other hand, strong chelating ligands are very important in aqueous media because they
offer the opportunity of trapping different metal species. This process becomes particularly
significant in living systems, where different metals are acquired, transported and stored mostly by
low-molecular-weight compounds involving multidentate oxygen donors. Among the family of
multidentate oxygen donor species, oda= oxodiacetate, O(CH2COO-)2, stands as a versatile
complexing agent. It holds an OOO donor group and can complex metal ions by forming chelate
rings. The synthesis of the complex VO2+-oda has been previously reported. The aim of the present
study is to extend our previous observations on the bioactivity of VO2+-oda on tumoral cells,
focusing the attention on its cytotoxicity effects on the human colon adenocarcinoma cell line Caco-
2, trying to understand its mechanisms of action.
The complex caused an inhibitory effect on cell proliferation in a dose response manner in the range
of 10-100 µM (p<0.001) (Crystal violet assay). Nevertheless, this inhibitory effect was lower than
the inhibition in other tumoral cell line (UMR106 rat osteosarcoma) studied in our laboratory. IC50
for the complex in Caco-2 cell line was >> 100 µM. This inhibition of Caco-2 proliferation was
reversed by scavengers of free radicals as a mixture of vitamin C and E (50 µM). The reversion was
complete in the range of low doses of the complex (10-25 µM) and only partial at higher
concentrations (50-100 µM). Morphological studies were carried out using Giemsa staining and light
microscopy. In basal conditions, the cells displayed polygonal shape and big nuclei with numerous
nucleoles. Cells present also numerous connections between each other. Upon incubation with the
complex, the nuclei showed different alterations in their form and some membrane blebs could be
seen. Besides, the cytoplasm of the cells also showed important transformations such as numerous
irregular vacuoles and lost of neighbouring connections. These changes increased with the doses
and correlated with a decrease in number of cells per field. Moreover, the investigation of the
effects of VO2+-oda on the actin filaments, indicated a disassembly of the network as a function of
complex concentration. Thus, the morphological alterations were in parallel with the results of
proliferation study. In order to get a deeper insight into the mechanisms underlying the cytotoxicity
of VO2+-oda, we determined its effect on the oxidative stress using two parameters: the oxidation
of dihydrorhodamine 123 to rhodamine (measured by spectrofluorometry) and the changes in the
ratio of reduced glutathione (GSH) to oxidized glutathione (GSSG). The complex produced a great
increment in the levels of rhodamine in the range of 50-100 µM while a decrease in the GSH/GSSG
ratio could be observed. Besides, the mixture of vitamins C and E, scavenger of free radicals,
caused a partial reversion of the VO2+-oda effect in the range of complex concentration 50-100 µM.
Altogether these results suggest that VO2+-oda exerts its cytotoxicity effects on human colon
adenocarcinoma (Caco-2) cells through, at least in part, an increment in the oxidative stress and
the alterations of actin cellular network.
Acknowledgements: S. B. Etcheverry thanks the Reitoria da Universidade Técnica de Lisboa, Portugal, the
financial support for travelling.

Modifying antiprotozoa activity of organic compounds through

complexation with vanadium
Dinorah Gambino,a Julio Benítez,a Marisol Vieites,a Lucía Guggeri,b Pablo Smircich,b
Beatriz Garat,b Miriam Rolón,c Celeste Vega,c Antonieta Rojas de Arias,c Daniel
Figueroa,d Tanof Celmar Costa França,d Edgar Marchán,e Zulay Simonie
a
Cátedra de Química Inorgánica, Facultad de Química, UDELAR, Gral. Flores 2124, 11800 Montevideo,
Uruguay; bLaboratorio de Interacciones Moleculares, Facultad de Ciencias, UDELAR, Igua 4225, 11400
Montevideo, Uruguay; cCEDIC, Fundación M. Bertoni/Laboratorios Díaz Gill, Asunción, Paraguay;
d
Departamento de Quimica, IME, 22290-270, Rio de Janeiro, Brazil; eInstituto de Investigaciones en
Biomedicina y Ciencias Aplicadas, Universidad de Oriente, Venezuela;
email: dgambino@fq.edu.uy
According to the World Health Organization infectious and parasitic diseases are major causes of
human disease worldwide. Chagas´s disease and Leishmaniasis, diseases caused by
kinetoplastid parasites of the genus Trypanosoma and Leishmania respectively, are large
burdens in the American continent. Chagas´ disease affects nearly 20 million people in Latin
America. Leishmaniasis threatens 88 countries around the world, 72 of which are developing
ones. Currently, Leishmania and HIV co-infection is a serious world problem. Chemotherapy is
unsatisfactory, available treatments suffering from limited efficacy and/or undesirable side
effects and/or development of resistance.
Searching for new therapeutic tools against Chagas' disease, we have been working on the
development of metal-based drugs by including in a single molecule an organic bioactive ligand
and a metal with pharmacological potentiality. This approach could lead to a metal-drug
synergism, produce an additive effect or improve bioavailability of the organic drug. By means
of this strategy we developed different bioactive metal complexes and studied their mechanism
of action. Among them a family of vanadyl complexes of bioactive 3-aminoquinoxaline-2-
carbonitrile-N1,N4-dioxide derivatives, VO(L)2, showed improved anti-trypanosomal activity
when compared with the free ligands. We were able to explain this behaviour on the basis of
lipophilicity and electronic characteristics of the quinoxaline substituents. Taking into account
these results, more recently, we have been working with another aromatic amine N-oxide
bearing in vitro anti-trypanosomal and anti-Leishmania activities, namely pyridine-2-thiol-N-
oxide (mpo), and its vanadium, platinum, palladium and gold complexes. It has been previously
demostrated that mpo blocks Trypanosoma cruzi´s growth in culture and in infected mammalian
myoblasts, affecting all stages of its life cycle and showing low IC50 values. Although it may
have other intracellular targets, it inhibits the parasite specific enzyme NADH-fumarate
reductase, enzyme responsible of the conversion of fumarate to succinate which is required by
the parasite for energy production. We evaluated the antiprotozoa activity of its vanadyl
complex VO(mpo)2. It showed a threefold increase of activity against T. cruzi epimastigotes (CL-
B5 strain) when compared with mpo sodium salt, showing an IC50 value in the micromolar range
and higher activity than the anti-trypanosomal drugs Nifurtimox and Benznidazol. It also
showed high in vitro leishmanicidal activity against Leishmania(L.) mexicana (NR strain) and
Leishmania(V.) braziliensis (M2903 strain). In addition, it demonstrated highly selective anti-
parasite activity since no unspecific citotoxicity on mammalian cells (J774 macrophages and
NCTC clone 929 fibroblasts) was observed at the doses where it showed activity. Trying to
provide insight into its mechanism of action NADH-fumarate reductase was evaluated as
potential parasite target. In addition, the enzyme was theoretically modelled and preliminary
docking studies with VO(mpo)2 are being performed. All data strongly suggest that the potent
antiprotozoa action of VO(mpo)2 could mainly rely on the inhibition of the enzyme, although
other secondary targets cannot be discarded. VO(mpo)2 could constitute a new antiprotozoa
chemotherapeutic alternative to be further evaluated in experimental models.
Acknowledgements: The authors would like to thank RIDIMEDCHAG CYTED network and Grants of Fonacit
G-2005000827. DG would like to thank Technical University of Lisbon for financial support.

Diabetes and vanadium: levels of vanadium in blood samples
Maria João Pereiraa; Cláudia Pedroa; Filipa Rodriguesa; Hélio Martinsb; Hercília
Martinsc; Mª João Faíscac; Mª João Melod; Eugénia Carvalhoe and Manuel Aurelianoa
(a) CCMAR, University of Algarve, Campus das Gambelas, 8005-139 Faro, Portugal
(b) FCT, University of Algarve, Campus das Gambelas, 8005-139 Faro, Portugal
(c) SPC, Faro Hospital, 8005 Faro, Portugal
(d) SIH, Faro Hospital, 8005 Faro, Portugal
(e) Center for Neuroscience and Cell Biology, University of Coimbra, 3000 Coimbra
A promising application for vanadium in human’s health arises from recent studies that
evaluated vanadium to have benefits affects in the treatment and prevention of diabetes.
Vanadium is an essential element well known as a metabolic regulator, a mitogenic activator, an
insulin-mimetic agent and by reversing drug resistance. Since it displays insulin-like activity
through correction of metabolic disorders associated with insulin deficiency, vanadium can be
used in diabetes treatment. However, the pharmacological and toxicological effects of vanadium
are far from a clear identification.
Type 2 diabetes mellitus (T2DM) is associated with a clinical phenotype known as the metabolic
syndrome. The metabolic syndrome is characterized by visceral obesity, pathogenic
dyslipidemia, glucose intolerance, insulin resistance and markers of cardiovascular disease.
T2DM is considered a modern disease once it is highly related with modern style of life favouring
sedentary and obese people.
In the present study, realised in the University of Algarve collaboration with the Immune
Therapy Service and the Pathology Service of the Hospital of Faro (HDF), it was analysed and
correlated several parameters associated with type 2 diabetes such as age, fasting serum
concentration of glucose, insulin, glycated haemoglobin (HbA1c), triglycerides (TGs), total
cholesterol (TC), low density lipoprotein- and high density lipoprotein – cholesterol (LDL-C and
HDL-C), markers of insulin resistance (HOMA-IR and QUICKI) in individuals with normal glucose
tolerance (NGT, n=66) and T2DM (n=625). In addition, we also studied the vanadium content
in blood samples (NGT=34 and T2DM=41), by furnace atomic absorption spectroscopy.
We demonstrate that TC, LDL-C, TG, did not differ among NGT and T2DM, although individuals
with T2DM present mean HDL concentrations of 47.35 ± 9.5 mg/dL, lower than the NGT with
53.27 ± 10.5 mg/dL (p<0.05). The NGT present mean HbA1c of 4.7 ± 0.4 %; while T2DM with
8.21 ± 1.1 % (p<0.001). The calculated values of insulin sensitivity (QUICKI) differ from 0.37
± 0.03 to 0.30 ± 0.03 (p<0.05) between the NGT and the T2DM population; and the index of
insulin resistance (HOMA) differ from 1.71 ± 1.1 to 7.93 ± 8.7 (p<0.05) between the NGT and
the T2DM population. Individuals with NGT present mean vanadium concentrations of 77.63 ±
19.9 ng/mL, higher than the T2DM with 59.35 ± 17.7 ng/mL (p<0.001). These results show
that NGT individuals present means vanadium concentrations 1.3 higher than T2DM.
Putting it all together, although preliminary, the obtained results may contribute to a better
understanding of vanadium metabolism and its relationship with biochemical parameters
associated with diabetes.
Acknowledgements: The authors would like to thank FCT – The Portuguese Foundation for Science and
Technology (SFRH/BD/41044/2007) and project POCI/SAU-MMO/57598/2004 for their help and financial
support.

Oxovanadium(IV) macrocycles: potential antivirals against HIV
Allison Ross,1 Neil Robertson,1 Simon Parsons1 and Peter J. Sadler1,2

1
School of Chemistry, University of Edinburgh, West Mains Road, Edinburgh, EH9 3JJ, UK and 2Department
of Chemistry, University of Warwick, Gibbet Hill Road, Coventry CV4 7AL, UK
Email: p.j.sadler@warwick.ac.uk
Some macrocycles, including cyclam derivatives, show promise as stem cell mobilizers and
antivirals, including activity against HIV and AIDS. The specific configurations adopted by metal
cyclam complexes may be important for receptor recognition and biological activity1. Natural
macrocyclic compounds with complexed metal ions play a role in many biological processes.
Cyclic polyamines in particular bind to a wide range of metals and in many cases show
configurational changes during binding2. In this work, novel vanadium complexes have
Figure 1: Oxovanadium(IV) cyclam chloride
been characterized and oxovanadium(IV) bicyclam complexes show high antiviral activity
against HIV. In particular, an oxovanadium(IV) bicyclam chloride species has shown antiviral
activity comparable with AMD3100, an effective entry inhibitor against HIV (and now a
successful stem-cell-mobilizing drug). Intriguingly, oxovanadium(IV) cyclam complexes were
completely inactive, and each crystallised in the thermodynamically stable trans-III
configuration with a 6th ligand trans to the oxygen of the characteristic V=O group.
Magnetic susceptibility measurements and FTIR spectroscopy confirmed the presence of

V(IV). The complexes have been studied by EPR, which revealed differences in behaviour
between the bicyclams and cyclams in aqueous solution. Protein recognition is being
investigated since the CXCR4 coreceptor is involved in HIV entry into cells and stem cell
anchoring.
Acknowledgements: We thank the BBSRC (studentship for A Ross) and RCUK (Rasor) for support, Drs.
Abraha Habtemariam and Ana Pizarro for assistance and advice.
[1] Liang X, Parkinson J A, Weishaupl M, Gould R O, Paisey S J, Park H, Hunter T M, Blindauer C A, Parsons
S, Sadler P J (2002) J Am Chem Soc 124: 9105-9112
[2] Hunter T M, McNae I W, Liang X, Bella J, Parsons S, Walkinshaw M D, Sadler P J (2005) Proc Natl Acad
Sci USA 102: 2288-2292.

Vanadocene complexes of α-amino acids: synthesis, structure and

cytostatic activity
Jaromír Vinklárek,a Hana Paláčková,a Jana Holubová,a Jan Honzíček,b Lenka

Zárybnická,c Zuzana Šinkorovác
a
The Department of General and Inorganic Chemistry, Faculty of chemical-technology, University of
Pardubice, nám.Čs. Legií 565, 532 10 Pardubice, Czech Republic, email:jaromir.vinklarek@upce.cz
b
Instituto de Tecnologia Química e Biológica da Universidade Nova de Lisboa, Av. da República, EAN, 2780-
157, Oeiras Portugal.
c
The Department of Radiobiology, Faculty of Military Health Sciences, University of Defence, Třebešská
1575, 500 01 Hradec Králové, Czech Republic.
Bent metallocenes Cp2MCl2 (Cp = η5-C5H5, M = Ti, V, Nb, Mo) are representatives of recently
developed non-platinum-group metal antineoplastic agents exhibiting pronounced in vivo and in
vitro activity against various tumor cell lines and markedly inhibiting the growth of several
human carcinomas heterotransplanted into athymic mice.[1-2] Mechanism of antitumor action of
metallocene compounds at the molecular level is still not sufficiently solved. However,
biological, cytological and chemical studies show that active metallocene species inhibits DNA
replication through interaction with DNA molecule or with DNA processing enzymes.[3]
The interaction between vanadocene dichloride (Cp2VCl2) and proteins was studied using model
system metallocene - amino acid. The first vanadocene(IV) complexes of α-amino acids were
prepared using reaction of vanadocene dichloride and α-amino acids in aqueous solution of
neutral pH.[4] All prepared complexes have been characterized by analytical and spectroscopic
methods. Molecular structures of fourteen compounds
were determined by X-ray diffraction analysis (Figure
1.). EPR spectroscopy was used for investigation of
their behaviour in solutions. It was found that majority
of α-amino acids without further function group is
coordinated to vanadocene fragment through oxygen
atom of carboxylic group and nitrogen of amino group
giving chelate complexes [Cp2V(N,O-aa)]Cl. Only L-
proline forms monodentate complex [Cp2V(O-pro)2]Cl2
with two amino acids bonded through oxygen atoms of
carboxylic groups. Reaction of Cp2VCl2 with L-cystein
gives other structural types. Chelate complexes
[Cp2V(N,S-cys)] and [Cp2V(O,S-cys)]Cl with amino acid Figure 1. Structure of [Cp2V(ile)][PF6]
bonded though sulphur are formed.
The considerable attention was also paid to antitumor properties of these amino acid complexes.
The cytostatic activity towards human leukaemia cell line HL-60 was comparable with starting
vanadocene dichloride and even better then in case titanocene dichloride (Cp2TiCl2) that was
clinically tested structural analogue of vanadocene dichloride.
Acknowledgements: The authors would like to thank Ministry of Education of the Czech Republic Research
Project MSM0021627501 for help and financial support.
[1] P. Köpf-Maier, H. Köpf, Chem. Rev. 87 (1987) 1137-1152.

[2] K. Mross, P. Robben-Bathe, L. Edler, J. Baumgart, W. E. Berdel, H. Fiebig, C. Unger Onkologie 23 (2000)
576-579.
[3] Waern, J. B.; Harding, M. M. J. Organomet. Chem. 2004, 689, 4655-4668.
[4] J. Vinklárek, H. Paláčková, J. Honzíček, J. Holubová, M. Holčapek, I. Císařova Inorg. Chem. 45 (2006)
2156-2162.

Biological variability in the anti-apoptotic effects of vanadium
Gail R. Willsky a, Barbara A. Bistram a, Rebecca Z. Grayson a, Lai-Har Chi a,

Martha Clark a, Debbie C. Crans b
a
University at Buffalo (SUNY), Buffalo, NY 14214. USA. b Department of Chemistry, Colorado State
University, Ft. Collins CO 80523 USA, email: gwillsky@buffalo.edu
The biological effects of vanadium (V) vary greatly in different biological systems1. This
fact explains, in part, why differring biological endpoints are reported by different research
groups with slightly different cells and V compounds. In these studies, the effects of changes of
the biological system were observed using the simple salt vanadate, V(V) in two cell culture
systems. Induction of apoptosis by V treatment was explored using caspase inhibitors in growth
experiments and monitoring of apoptotic cells using DNA labeling (TUNEL assay) with flow
cytometry. We have previously reported the inhibitory effects of V(V) on muscle cell growth2.
Here V inhibited cell growth in both muscle myoblasts (L6) and rat hepatoma cells (H4IIE) cells.
In both cell lines V affected cell adhesion before killing the cells as expected since V is known to
affect cytoskeleton elements such as actin. Caspase inhibitors protected muscle cells from cell
death, but not liver cells. Since Caspases are activated by apoptosis, the protection of cells from
growth inhibition by caspase inhibitors is indicative of the induction of apoptosis.
A. B.
Figure 1 TUNEL assay for apoptosis in cell culture

Cells were grown to approximately 40% confluence and treated with different concentrations of vanadate
from 0 to 500 uM for 12 hours. A. H4IIE liver cells, B. L6 myoblasts.
Vanadate treatment induced apopoptosis in muscle cells (Figure 1B); but not in liver cells
(Figure 1A) in the TUNEL assay. Induction of apoptosis results in the shift of the cell population
to the right, indicative of increasing amounts of fluorescent dye being incorporated in the cells at
the site of apoptosis-induced breaks in the DNA.
These studies imply that V growth inhibition is mediated via the apoptotic pathway in
muscle but not in liver. The differential results observed could be due to the induction of
different vanadium-sensitive components in the two cell lines, differential uptake of vanadium in
the two cell types or other factors. Liver and muscle cells frequently have different metabolic
pathways activated, or different levels of activation are seen in response to a stimuli. For
example, glucose transport in muscle is strongly stimulated (4- 20 fold) by insulin, while glucose
transport in liver only shows a 2 fold stimulation after insulin treatment. Both tissues are
differently affected by the onset of diabetes. The results reported here show the benefits for
directing vanadium therapies to specific tissues, and thus presents new directions of research
for this class of compound.
Acknowledgements: We thank the NIH and Luso-American Development Foundation for financial support.
[1] A.Tracey, G. Willsky, E.Takeuchi, (2007) Vanadium: Chemistry, Biochemistry, Pharmacology and
Technical Applications, CRC Press , Boca Raton FL. 250 pp.
[2]G. Willsky, M. Godzalla III, P. Kostyniak, L.-H. Chi , R. Gupta,V. Yuen, J. McNeill, M. Mahroof-Tahir, J.
Smee, L. Yan, A. Lobernick, S. Watson, and D. Crans, ACS Symposium Series 974 (2007) 93-109.

Fenton chemistry revisited: vanadate’s role in

the study of antioxidants
Wu Lisha,a Leif A. Eriksson b, Åke Stridb, Simon Dunne a, Sarah Angus-Dunnea

a
Institution for Biology and Chemical Engineering, Mälardalens University, Eskilstuna (Sweden)
b
Department of Natural Sciences and Örebro Life Science Centre, Örebro University (Sweden)
Fenton chemistry is generally known as the reaction of Fe(II) or Fe(III) salts with peroxide to
create hydroxyl free radicals1. Several other metals including vanadium(IV) and (V) are known
to create a similar effect2. The generation of free radicals is generally an unwanted effect, which
most biological systems have effective defenses against. We will report how both the
Fe/peroxide and the V/peroxide systems along with NMR spectroscopy can be employed to
probe the effectiveness of various natural compounds as antioxidants.
[1] Stadtman, E.R., Berlett, B.S., J. Biol. Chem., (1991), 266 (26): 17201 -17211.
[2] Valko, M., Morris, H., Cronin, M. T.D. Current Medicinal Chemistry, (2005), 12(10), pp. 1161-1208(48);
Natarajan S. Venkataramanan, Gopi Kuppuraj and Seenivasan Rajagopal, Coord. Chem. Reviews, (2005),
249, (11-12), 1249-1268.

Hydroxylamino-vanadate derivatives as protein tyrosine

phosphatase inhibitors
Xu Zhou,a Leif A. Eriksson b, Simon Dunne a, Sarah Angus-Dunnea

a b
Institution for Biology and Chemical Engineering, Mälardalens University, Eskilstuna (Sweden) Department
of Natural Sciences and Örebro Life Science Centre, Örebro University (Sweden)
Protein tyrosine phosphatases (PTPs), are known targets for the treatment of diabetes as they
regulate phosphorylation in the insulin signaling pathway. Vanadate acts as an inhibitor of PTPs
and leads to amplified insulin receptor signaling. Vanadate itself is active only in doses which
are unsuitable for long-term therapeutic treatment of diabetes, due to deposition of vanadium in
bones leading to osteoporosis. Hydroxylamino-vanadium derivatives are potential PTPs
inhibitors in smaller amounts and thus have possible use as oral pharmaceuticals for the
treatment of diabetes.
The compounds which show strong affinity for the active site on PTP1B through molecular
modeling have been synthesized and their speciation under physiological conditions as
51
determined by using V NMR spectroscopy techniques will be reported.
S
N
OH
1

Vanadium interactions with the calcium pump ATPase: an overview
Rosa F. Brissos,a,b Fábio L. Fontes,a,b Hélio Martins,a Gil Fraqueza,a,b Teresa Tiago,a,b
Jorge Martins,a,c Rui O. Duarte,d José J.G. Moura,d Manuel Aurelianoa,b
a b
Dept. Chemistry Biochemistry and Pharmacy, FCT, University of Algarve, Faro, Portugal; Centre for Marine
c
Sciences (CCMAR), University of Algarve, Faro, Portugal; CBME, University of Algarve, Faro, Portugal;
d
Dept. Chemistry, FCT, New University of Lisbon, Monte da Caparica, Portugal
It is well known that vanadium inhibits the calcium pump ATPase1. Back then, only the
monomeric vanadate species (V1) was recognized as the active specie having biological roles,
disregarding the possible contribution of other vanadate oligomers. Among them, decameric
vanadate species (V10) was later recognized also to interact with Ca2+-ATPase inducing protein
dimmers2 besides inhibiting the Ca2+ translocation coupled to ATP hydrolysis3. Whereas V1 was
described as interacting with aspartate binding site, blocking the enzyme in the E2 conformation
V10 was also found to interact with several protein conformations1,3 through binding to the
nucleotide binding site4. The ability of vanadate to act either as a phosphate analog or as a
transition state analog with enzymes catalysis phosphoryl group transfer suggests that
vanadium coordination compounds may reveal mechanistic preferences in these classes of
enzymes. Recent studies from our group, proposed that different vanadium compounds such as
pyridine-2,6-dicarboxylatedioxovanadium(V) (PDC-V(V)), and two vanadium(IV) compounds,
bis(maltolato)oxovanadium(IV) (BMOV) and an analog of amavadine, bis(N-
hydroxylamidoiminodiacetato)vanadium(IV) (HAIDA-V(IV)) affect differently the SR Ca2+-
ATPase being the relative order of inhibition: PDC-V(V) > BMOV > vanadate > HAIDA-V(IV),
with IC50 values of 25, 40, 80 and 325 µM, respectively5 lower than the one observed for
vanadate-citrate complexes (0.5 mM)6. Once that the Ca2+-ATPase can adopt several
conformations, the specific nature of the interactions of each of the vanadium compounds with
the sarcoplasmic reticulum Ca2+-ATPase is an important scope of investigation.
LUMEN
CYTOPLASM
In the present work, we study the interaction between monomeric (V1) and decameric
(V10) vanadate species with the Ca2+-ATPase at several conformations, by using atomic
absorption spectroscopy and UV/Vis spectrophotometry. The preliminary results suggest that
although being more negatively charged the V10 stoichiometry of interaction with the
sarcoplasmic reticulum (SR) Ca2+-ATPase is apparently not different from V1. Further studies,
will confirm if the interaction of the different vanadium oligomers is, at least in part, dependent
on the different protein conformations that occurs during the mechanism of calcium
translocation. It is expected that these studies will allow an extended and improved
understanding of vanadium mode of interaction and its effects in calcium homeostasis and
muscle contraction regulation through the SR Ca2+-ATPase.
Acknowledgements: T. Tiago thanks to the fellowship (SFRH/BPD/20777/2004) from (FCT).
[1] Y. Dupont, and N. Bennett, FEBS Lett. 139 (1982) 237-240. [2] L. Dux, and A. Martonosi, J. Biol. Chem.
258 (1983) 2599-2603; [3] M Aureliano, V.M.C. Madeira, Biochim. Biophys. Acta 1221 (1994) 259-271; [4]
S. Hua, G. Inesi, and C. Toyoshima, J. Biol. Chem. 275 (2000) 30546.; [5] M. Aureliano, F. Henao, T. Tiago,
R.O. Duarte, J.J.G. Moura, B. Baruah, and D.C. Crans, Inorganic Chemistry. (2008) in press.; [6] M,
Aureliano, T. Tiago, R. M Gândara, A. Sousa, A. Moderno, M Kaliva, A. Salifoglou, R. O Duarte, J. J. G Moura,
Inorg. Biochem, 99 (2005) 2355-2361.

Decavanadate effect on rat synaptic plasma membrane

Na+/K+-ATPase activity
Mirjana Colovic,a Nada Bosnjakovic-Pavlovic,b Anne Spasojevic-de Bire,c Vesna Vasic,a

a
Vinča Institute of Nuclear Sciences, P.O.Box 522, 11001 Belgrade, Serbia, e-mail: colovicm@vin.bg.ac.yu
b
c
Decameric vanadate species interact, in vitro, with high-affinity with many proteins such as
myosin and SR calcium pump and also inhibit these biochemical systems involved in energy
transduction1. The purpose of this study was the investigation of the in vitro effect of
(NH4)6V10O28.5H2O on rat synaptic plasma membrane (SPM) sodium pump activity.
The method of Chinea et al2 was used for synthesis of ammonium decavanadate crystals. SPM
were isolated from the whole rat brain. The Na+/K+_ATPase activity was assayed in the absence
(control) and presence of decavanadate (within the range 1x10-10 to 1x10-1) in standard
medium containing 50 mM Tris-HCl (pH 7.4), 100 mM NaCl, 20 mM KCl, 5 mM MgCl2, 2 mM ATP
and 25 μg enzyme in a final volume of 200 μl. Incubation mixtures were preincubated for 10
min at 37oC in the presence of investigated compound or distilled water (control). The inorganic
orthophosphate (Pi) liberated from the hidrolysis of ATP, was measured using modified
spectrophotometric procedure3. The increasing concentrations of decavanadate induced
inhibition of enzymatic activity in a concentration-dependent manner (Fig 1). The dependence of
enzyme activity, expressed as a percentage of the control value (obtained without inhibitor) on
inhibitor concentration fit a sigmoidal function. The obtained half-maximum inhibitory
concentration (IC50) of decavanadate for sodium pump, determined by sigmoidal fitting, was
(4.7 ± 0.1) x 10-7 mol/L.
100
80
activity (% of control)
60
40
20
1E-11 1E-10 1E-9 1E-8 1E-7 1E-6 1E-5 1E-4 1E-3 0,01
decavanadate (M)
Figure 1. The concentration dependent inhibition of SPM sodium pump induced by ammonium
decavanadate. The values are expressed as mean ± S.E.M.
[1] M. Aureliano, R. Gandara, J. Inorg. Biochem. 99 (5) (2005) 979-985.

[2] B. Chinea, D. Dakternieks, A. Duthie, C.A. Ghilardi, P. Gili, A. Mederos, S. Midollini, A. Orlandini,
Inorg. Chim. Acta 298 (2000) 172-177.
[3] V. Vasić, D. Jovanović, D. Krstić, G. Nikezić, Lj. Vujisić, N. Nedeljković,Toxicol. Let. 110 (1-2) (1999) 95-
104.

Differential interaction of Sarcoplasmic Reticulum Calcium ATPase

with Mo, V and W Oxometalates
Gil Fraquezaa,b, Emilie Ritob,c, Rosa Brissosb,c, Teresa Tiagob,c, Jorge Martinsb,d, Rui O.
Duartee, José J.G. Mourae and Manuel Aurelianob,c
a
Escola Superior de Tecnologia, Universidade do Algarve, 8005-139 Faro, Portugal;
b
Departamento de Química, Bioquímica e Farmácia, FCT, Universidade do Algarve, Faro, Portugal;
c
CCMar, Universidade do Algarve, Faro, Portugal;
d
IBB-CBME, Universidade do Algarve, Faro, Portugal; e REQUIMTE, Departamento de Química, FCT,
Universidade Nova de Lisboa, Monte da Caparica, Portugal.
Vanadium (V), tungsten (W) and molybdenum (Mo) oxometalates are widely applied as
analytical reagents for the determination of numerous pharmacologically active substances and
different biochemical parameters1. It has been shown that these compounds act on some
cellular enzymatic systems leading to the normalization of blood pressure, blood glucose and
serum lipid levels1. The insulin mimetic effects of these compounds have been associated to the
specific regulation of protein kinase receptors, including the insulin receptor. We have recently
reported that organic vanadium compounds, some of them with insulin mimetic properties,
inhibit the activity of sarcoplasmic reticulum calcium ATPase (SR-Ca2+-ATPase), and may
therefore also regulate the muscle contraction process through this ATPase2.
In the present study we aim to clarify the interaction between V, W and Mo, with the calcium
pump, by combining spectroscopic with kinetic studies. We found that the hydrolytic activity of
SR-Ca2+-ATPase was inhibited by all four oxometalates, however the decameric specie of
vanadate exhibit the lower value of IC50. The relative order of inhibition was V10 > V1> W > Mo
whit IC50 values of 0.015 mM, 0.05 mM, 0.4 mM and 45 mM, respectively.
Upon incubation of SR-Ca2+-ATPase with V1, V10, W and Mo at 25ºC, the results show an
increase in the hydrolytic activity, after 15 minutes for all four oxometalates. After 60 minutes
of incubation, the relative order of decrease in the SR-Ca2+-ATPase activity was V10 ≈ W > Mo.
V1 oxometalate appears to increase the hydrolytic activity of SR-Ca2+-ATPase.
In order to clarify the type of the inhibition effects caused by V10, this phenomenon can be
reverted by adding DTT to the incubation preparation.
It is suggested that clearing up the interaction between SR-Ca2+-ATPase with V, W and Mo
oxometalates can help to further understand the modulation of some cellular enzymatic
systems, such as the SR-Ca2+-ATPase, by different oxometalate compounds.
Acknowledgements: T. Tiago is the recipient of a post-doctoral fellowship (SFRH/BPD/20777/2004) from the

Portuguese Foundation for Science and Technology (FCT).
[1] Stankov,M.J.;Markovic, S.U.; Antunovic,I.H.; Todorovic,M. and Djurdevic,P. Journal of Trace Elements in
Medicine and Biology (2007), 21, 8-16.
[2] Aureliano,M.; Henao,F.; Tiago,T.; Duarte, R.O.; Moura, J.J.G.; Baruah, B. and Crans, D.C. Inorganic
Chemistry. (2008) in press.

Vanabin2 extracted from ascidian vanadocyte is

a novel vanadium reductase
Norifumi Kawakami,a Tatsuya Ueki,a Yusuke Amata,b Kan Kanamori,b Koichi Matsuo,c
Kunihiko Gekko,c and Hitoshi Michibataa
a c
Department of Biological Science and Department of Mathematical and Life Sciences, Graduate School of
Science, Hiroshima University, 1-3-1 Kagamiyama, Higashi-Hiroshima 739-8526, Japan, and bDepartment of
Chemistry, Graduate School of Science and Engineering, University of Toyama, Gofuku 3190, Toyama 930-
8555, Japan, email: kawakami@hiroshima-u.ac.jp
The unusual phenomenon found in the ascidians with exceptional ability to accumulate
vanadium ions at concentrations up to 350 mM, a107-fold increase over its concentration in
seawater (35 nM), has been attracting the interdisciplinary attention of chemists, physiologists,
and biologists. Accumulated vanadium ions (VV) are first reduced to VIV in ascidian vanadocytes
and stored in their vacuoles where they are finally reduced to VIII and seem to exist as free
ions[1]. Reducing agents must, therefore, participate in the reduction of vanadium[2]. A family of
vanadium-binding proteins, Vanabins, were found in a vanadium-rich ascidian[3-5]. Among them,
Vanabin2 analyzed its solution structure has been revealed to be a rare protein with 9 disulfide
bonds per a molecule[6]. The disulfide bonds were cleaved by GSH, which resulted in the
reduction of VV to VIV. In fact, 10 μM Vanabin2 evoked a strong EPR signal intensity due to VIV
species when it was added to the reaction mixture containing 2 mM VV and 2 mM GSH at room
temperature. Thus, Vanabin2 can act as a VV reductase in vandocytes.
S
GSH Vanabin2 V(IV)
S 9
SH
GSSG Vanabin2 V(V)
SH n
261 286 311 336 361 386 411

[mT]
Scheme1 (left). Possible VV reduction cascade in vanadocytes.

Figure 1 (right). EPR signal obtained from Scheme 1 assay system. Dashed line, immediately after the
addition of 10 μM Vanabin2 to the reaction mixture of 2 mM VV and 2 mM GSH; Solid line, 24 hr after the
addition of 10μM Vanabin2 to the reaction mixture of 2 mM VV and 2 mM GSH.
Acknowledgements: The authors thank Mr. T. Morita and the staff at the International Coastal Research
Center of the Ocean Research Institute, The University of Tokyo, Otsuchi, Iwate, Japan, for their help in
collecting adult ascidians. This work was supported by Research Fellowships of the Japan Society for the
Promotion of Science for Young Scientists.
[1] J. Hirata H. Michibata, J. Exp. Zool. 257 (1991) 160-165.

[2] K. Kanamori, M. Sakurai, T. Kinoshita, T. Uyama, T. Ueki, H. Michibata, J. Inorg. Biochem. 77 (1999)
157-161.
[3] T. Ueki, T. Adachi, S. Kawano, M. Aoshima, N. Yamaguchi, K. Kanamori, H. Michibata, Biochim. Biophys.
Acta 1626 (2003) 43-50.
[4] K. Fukui, T. Ueki, H. Ohya, H. Michibata, J. Am. Chem. Soc. 125 (2003) 6352-6353.
[5] M. Yoshihara, T. Ueki, T. Watanabe, N. Yamaguchi, K. Kamino, H. Michibata, Biochim. Biophys. Acta
1730 (2005) 206-214.
[6] T. Hamada, M. Asanuma, T. Ueki, F. Hayashi, N. Kobayashi, S. Yokoyama, H. Michibata, H. Hirota, J.
Am. Chem. Soc. 127 (2005) 4216-4222.

Inhibition of rat synaptic plasma membrane

Ca2+-ATPase activity by decavanadate
Danijela Krstica, Nada Bosnjakovic-Pavlovicb, Anne Spasojevic-de Birec, Vesna Vasicd

a
Institute of Chemistry, School of Medicine, University of Belgrade, Serbia, e-mail: krsticdana@yahoo.com
b
c
d
Vinča Institute of Nuclear Sciences, P.O.Box 522, 11001 Belgrade, Serbia
Decavanadate has a strong inhibitory effect on some nucleotide binding enzymes such as
sarcoplasmic reticulum calcium pump which belongs to the P-type ATPase family1. The aim of
this work was the investigation of the in vitro effect of ammonium decavanadate,
(NH4)6V10O28.5H2O on rat synaptic plasma membrane Ca2+-ATPase (PMCA) activity, which also
belongs to the P-type ATPase family. Orange crystals of (NH4)6V10O28.5H2O were prepared
according to the method of Chinea et al2. The SPM were isolated from the whole rat (albino,
vistar) brain according to the standard method3. The rat synaptic PMCA activity was assayed in
the absence (control) and presence of decavanadate (within the range 1x10-10 to 1x10-1) in
standard medium containing 50 mM Tris-HCl (pH 7.4), 0.5 mM EGTA, 0.5 mM CaCl2, 5 mM
MgCl2, 2 mM ATP and 25 μg enzyme in a final volume of 200 μl. Incubation mixtures were
preincubated for 10 min at 37oC in the presence of investigated compound or distilled water
(control). The inorganic orthophosphate (Pi) liberated from the hidrolysis of ATP, was measured
spectrophotometricly at 690 nm. The obtained results show (Figure 1) that decameric vanadate
species inhibited rat synaptic calcium pump in a concentration-dependent manner. Dependence
of the AChE activity, expressed as the percent of control value (obtained without inhibitor) on
the inhibitor concentration has a sigmoidal shape. The concentrations that reduce the response
by 50% (half-maximum inhibitory concentration-IC50) obtained by Hill analyse (Figure 1, inset)
of inhibition curve was (3.1 ± 0.1) x 10-8 mol/L.
log (% activity/(100 - % activity))
100 1
80
activity (% of control)
0
-8 -7
log C (of decavanadate)
-6
60
-1
40
20
1E-11 1E-10 1E-9 1E-8 1E-7 1E-6 1E-5 1E-4 1E-3 0,01
decavanadate (M)
Figure 1. The concentration dependent inhibition of SPM Ca2+-ATPase induced by ammonium decavanadate.
Hill plot of inhibition curve (inset) The values are expressed as mean ± S.E.M.
[1] M. Aureliano, R. Gandara, J. Inorg. Biochem. 99 (5) (2005) 979-985.

[2] B. Chinea, D. Dakternieks, A. Duthie, C.A. Ghilardi, P. Gili, A. Mederos, S. Midollini, A. Orlandini,
Inorg. Chim. Acta 298 (2000) 172-177
[3] RS. Kohen, F.Blomberg, K. Berzins, P. Siekevits J. Cell Biol. 74 (1977) 181-203

Modeling supramolecular interactions of vanadium species
Ines Lippold and Winfried Plass
Institut für Anorganische und Analytische Chemie, Friedrich-Schiller-Universität Jena,

Carl-Zeiss-Promenade 10, 07745 Jena, Germany, email: sekr.plass@uni-jena.de
Supramolecular interactions are a prominent feature in biological systems. A specific example is

given by the vanadium haloperoxidases (V-HPOs) for which a hydrogen bonding network is observed
that governs their reactivity.1 Therefore, models are desired to contain suitable donors that generate
a polar protic surrounding, capable of generating an appropriate hydrogen bonding environment.
Cyclodextrins (CDs) are hosts that provide hydrophobic cavities with hydrophilic outer walls. They
form inclusion compounds with various apolar groups that partially or completely included in the
cavity. Parts of the guest protruding out of the CD-cavity could take part in the hydrogen bonding
system.2 Herein we present new cis-dioxovanadium(V) complexes with appropriate side chains that
fit in CD cavities (Figure 1).
Figure 1. Syntheses of the inclusion compounds K[VO2(aldhyguest)@xCD].
Hydrazone ligands H2aldhyguest are synthesized via Schiff-base condensation of aromatic ortho-
hydroxy-aldehyds (ald) and different apolar acid-hydrazides (hyguest). The reaction of potassium
vanadate with H2aldhyguest in the presence of 1 or 2 equivalents of α− or β-CD in water yield the
chiral 1:1 or 1:2 inclusion compounds K[VO2(aldhyguest)@xCD].3 For selected examples their solid
state and solution structures will be discussed.
[1] R. Wever, W. Hemrika in Handbook of Metalloproteins, Vol. 2 (Eds.: A. Messerschmidt, R. Huber, T.

Poulos, K. Wieghardt), John Wiley and Sons Ltd., Chichester, 2001, pp. 1417–1428.
[2] J. Szejtli, Chem. Rev. 98 (1998) 1743–1753.
[3] I. Lippold, H. Görls, W. Plass, Eur. J. Inorg. Chem. (2007) 1487–1491.

Vanadium imidazolylcarboxylate complexes: synthesis,

characterization, and phosphatase inhibition
Craig C. McLauchlan, Bradley A. Greiner, Nicole A. Dorner, Emily A. Backhus, and

Jamie E. Meyer
Department of Chemistry, Illinois State University, Normal, IL 61790-4160 USA, email: ccmclau@ilstu.edu
In the course of our investigations of vanadium-containing compounds for use as insulin

enhancing agents, we have generated a series of novel vanadium coordination complexes with
bidentate ligands. Specifically we have focused on two ligands meant to mimic naturally
occuring ligands, namely imidizole-4-carboxylate (imc, shown) and anthranilate. For each
ligand, we have generated a series of complexes containing the V(III), V(IV), and V(V)
oxidation states. Each complex is being investigated using alkaline phosphatse inhibition
studies as prima facia evidence for potential use as an insulin enhancing agent. Under our
experimental conditions, for instance, V(imc)3 appears to be as potent an inhibitor of alkaline
phosphatase as vanadyl sulfate. Here we report the syntheses, characterization, reactivity, and
phosphatase inhibition activity of our newly formed complexes, focusing on complexes
analogous to the known picolinate complexes.
O O
-
O NH O NH O
HN HN
N N O O N N O
V V V
O O O N O O O O
N HN N
O O
NH NH
V(imc)3 VO(imc)2 [VO2(imc)2]-
Figure 1. A series of V/imc complexes
Acknowledgements: The authors would like to thank the National Science Foundation (U.S., CHE-0645081)
for financial support.

Functional and structural interactions of three vanadium coordination

complexes with the Sarcoplasmic Reticulum Calcium Pump
Ana M.Pereiraa,b, Teresa Tiagoa,b,c, Fernando Henaoc, Carlos Gutiérrez-Merinoc, Bharat

Baruahd, Debbie C.Cransd and Manuel Aurelianoa,b
a
Dept de Química, Bioquímica e Farmácia, FCT, Universidade do Algarve, 8005-139 Faro, Portugal, email:
maalves@ualg.pt; bCCMar, Universidade do Algarve, Faro, Portugal; cDept Bioquímica y Biologia Molecular,
Faculdad de Ciências, Universidad de Extremadura, Badajoz, Spain; dDept of Chemistry, Colorado State
University, Fort Collins, Colorado 80523-1872,USA
Sarcoplasmic Reticulum Ca2+-ATPase (SERCA) is a complex transmembrane and energy

transducting system that is extensively studied and well understood. Recently, we have
demonstrated that three different classes of vanadium coordination complexes including
pyridinedicarboxylate vanadium (V) (PDC-V(V)), oxovanadium(IV)-bis(maltolato) (BMOV) and
an analogue of amavadine, bis(N-hydroxylamidoiminodiacetato)vanadium(IV) (HAIDA-V(IV))
(Figure 1) inhibit the hydrolytical activity of this pump1. While the first two are known to induce
insulin enhancing effects, the third one is a well-known analogue of a vanadium-containing
natural product. A relative inhibition order of PDC-V(V) > BMOV > vanadate > Amavadine (with
IC50 values of 25, 40, 80 and 325 µM, respectively) has been established. To this end, intrinsic
and extrinsic fluorescence studies as well as kinetic measurements on the 45Ca transport and
binding to the ATPase were performed to evaluate the effects of these three vanadium
complexes on the ATPase bioenergetic and structural function.
Figure 1. Molecular structures of PDC-V(V), BMOV, [VO2(ma)2]- and HAIDA-(IV).
Both BMOV and PDC were able to stimulate SR 45Ca binding in a similar way to metavanadate
solutions. Nevertheless, BMOV and PDC levels around the IC50 values for inhibition of hydrolysis
did not significantly inhibit the 45Ca uptake, irrelevant of incubation time. Such inhibition was
only observed at higher vanadium levels. Fluorescence studies with FITC labelled SERCA have
shown that BMOV and PDC shift the calcium pump to the E2 (like decavanadate and
monovanadate solutions) and E1 (like metavanadate solutions) conformations, respectively.
Together, these observations are consistent with an adduct formation between protein and V
compounds and with their complexation to the catalytic site of Ca2+-ATPase, as previously
suggested1. Although amavadine favoured the E1 conformation (a high Ca2+ affinity state), it
significantly inhibited 45Ca binding, suggesting that amavadine may interact with calcium
binding sites of the pump. Collectively, these results indicate that the three coordination
compounds could promote a response in the calcium homeostasis and muscle contraction
systems through the SERCA pump.
Acknowledgments: Work supported by Joint Spanish-Portuguese Project CRUP-E-106/05 and by the POCTI
program financed through FEDER: project 38191/QUI/2001 (to M.A.). Dr. T. Tiago is the recipient of a post-
doctoral fellowship (SFRH/BPD/20777/2004) from the Portuguese Foundation for Science and Technology
(FCT).
[1] M. Aureliano, F. Henao, T. Tiago, R.O. Duarte, J.J.G. Moura, B. Baruah, D.C. Crans. Inorganic Chemistry
in press.

Binding of vanadium (IV) and (V) to actin:effects on function

and structure
Susana Ramosa,b, Teresa Tiagob,c, Rui Duartea, José J. G. Mouraa, Manuel Aurelianob
a
REQUIMTE/CQFB, Dpto. Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa,
2829-516 Caparica, PORTUGAL;
b
CCMar, Dpto. Química e Bioquímica, Faculdade de Ciências e Tecnologia, Universidade do Algarve,
8000-139 Faro, PORTUGAL;
c
Dpto. De Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad de Extremadura,
Av. Elvas s/n, 06071 Badajoz, SPAIN
email: s.ramos@dq.fct.unl.pt
The chemistry of vanadium is characterized by multiple oxidation states (+2 to +5), being
largely found in the +4 and +5 oxidation states, both of which are readly accessible under
physiological conditions [1]. In aqueous solutions, the chemistry of tetravalent vanadium is
centered on VO2+ ion. This ion forms complexes with a diversity of ligands and is known to bind
to numerous proteins [2]. In vanadium (+5) solutions different oligoanions can occur
simultaneously in equilibrium such as monomeric (V1), dimeric (V2), tetrameric (V4) and
decameric (V10) species.
Actin is one of the major components in the microfilament system of the eukaryotic cells, being
involved in many cellular processes, such as the maintenance of cell shape, cytoplasmic
streaming and cell division. The ability of actin monomers (G-actin) to polymerize into
filamentous form (F-actin) is crucial in structural and motile functions of the cells. A major role
of actin lies in the generation of force by striated and smooth muscle cells [3].
Previous results from our group demonstrated that decameric species inhibit G-actin
polymerization and enhance F-actin depolymerization, disturbing the G-actin/F-actin
equilibrium. Besides V10, tetrameric vanadate species may also contribute to the inhibition of
actin polymerization [4]. We now show that incubation of F-actin with decavanadate inhibits 70
% the myosin-S1-ATPase activity stimulated by F-actin (IC50 = 0,80 ± 0,15 μM), while
metavanadate and vanadyl ion have a much lower effect (only 25 % inhibition for the maximum
vanadium concentrations used, 50 μM). The cysteine oxidation observed upon G- and F-actin
incubation with decavanadate may play a key role to the functional alterations described above.
To gain a deeper knowledge about the interactions of vanadyl ions with actin, EPR studies are
being developed. Preliminary results indicate binding of 8 VO2+ ions/actin molecule, probably in
amino acid residues containing the group – NH2, such as asparagine (Asn), glutamine (Gln) and
lysine (Lys).
Susana Ramos and Teresa Tiago are supported by a PhD grant (SFRH/BD/29712/2006) and a post-doctoral
grant (SFRH/BPD/20777/2004) from the Portuguese Foundation for Science and Technology (FCT),
respectively.
[1] Chasteen, N. D., Structure and Bonding, Springer-Verlag Berlin Heidelberg, 1983;
[2] Chasteen, N. D., Biological Magnetic Ressonance, Vol. 3 (eds.) Berliner, L. Reuben, J., p 53, New York,
Plenum Press, 1981;
[3] Lorinczy, D. et al., Thermochimica Acta, (1988) 322, 95;
[4] Ramos, S. et al., J Inorg Biochem, (2006) 100, 1734.

List of
Participants

Oral lectures

List of Participants LP1
ARGENTINA CROATIA
Baran, Enrique Cindrić, Marina

Centro de Quimica Inorgânica - CEQUINOR Chemistry Department, University of Zagreb,
Universidad Nacional de La Plata Faculty of Science
Calle 47 esquina 115 Horvatovac 102a
1900 La Plata 10000 Zagreb
baran@quimica.unlp.edu.ar marina@chem.pmf.hr
Etcheverry, Susana Rubčić, Mirta

Facultad de Ciencias Exactas Chemistry Department, University of Zagreb,
Universidad Nacional de La Plata Faculty of Science
Calle 47 esquina 115 Horvatovac 102a
1900 La Plata 10000 Zagreb
etcheverry@biol.unlp.edu.ar mirta@chem.pmf.hr
BRAZIL CYPRUS
Antunes, Octávio Drouza, Chryssoula

Departmento de Química Inorgânica, UFRJ Department of Agricultural Production and Food
Centro de Tecnologia Science, Cyprus University of Technology
Bloco A, Lab 641 3036 Lemesos
Cidade Universitária chrysd@ucy.ac.cy
21.941-590 Rio de Janeiro
octavio@iq.ufrj.br Keramidas, Anastasios
Department of Chemistry, University of Cyprus
1678 Nicosia
CANADA akeramid@ucy.ac.cy
Orvig, Chris Stylianou, Marios

Department of Chemistry Department of Chemistry, University of Cyprus
University of British Columbia 1678 Nicosia
2036 Main Mall chpgms1@ucy.ac.cy
Vancouver, BC
V6T1Z1 Vancouver
orvig@chem.ubc.ca CZECH REPUBLIC
Thompson, Katherine Vinklárek, Jaromír

Department of Chemistry Department of General and Inorganic Chemistry,
University of British Columbia University of Pardubice
2036 Main Mall nám. Čs. legií 565
V6T 1Z1 Vancouver 532 10 Pardubice
kthompso@chem.ubc.ca jaromir.vinklarek@upce.cz
CHINA FRANCE
Ding, Wenjun Carn, Florent

College of Life Sciences Chimie de la Matière Condensée de Paris UPMC
Graduate University of Chinese Academy of Colège de France
Sciences 4 place Jussieu
No. 19A Yu Quan Road T.54-55 - Case 174
100049 Beijing 75252 PARIS
dingwj@gucas.ac.cn florent.carn@upmc.fr

LP2 List of Participants
Ghermani, Nour Eddine Rehder, Dieter

U.F.R. Pharmacie, Université Paris-Sud 11 Chemistry Department, University of Hamburg
Laboratoire Physico-Chimie - Pharmacotechnie - Martin-Luther-King-Platz 6
Biopharmacie 20146 Hamburg
UMR CNRS 8612 rehder@chemie.uni-hamburg.de
5 rue J.B. Clément
92296 Châtenay-Malabry Rosenthal, Esther
noureddine.ghermani@u-psud.fr Technische Universität Berlin
Secr. C2
Lorber, Christian Strasse des 17. Juni 135
Laboratoire de Chimie de Coordination 10623 Berlin
Centre National de la Recherche Scientifique –CNRS esther.rosenthal@tu-berlin.de
205 route de Narbonne
31077 Toulouse
lorber@lcc-toulouse.fr GREECE
Spasojevic, Anne Kabanos, Themistoklis

SPMS, Ecole Centrale Paris Section of Inorganic and Analytical Chemistry,
UMR 8580 CNRS Department of Chemistry
Grande voie des Vignes University of Ioannina
92295 Chatenay-Malabry 45110 Ioannina
anne.spasojevic@ecp.fr tkampano@cc.uoi.gr
Salifoglou, Athanasios
GERMANY Laboratory of Inorganic Chemistry
Department of Chemical Engineering
Geibig, Daniel Aristotle University of Thessaloniki
Institut für Anorganische und Analytische Chemie University Box 462
Friedrich-Schiller-Universität Jena 54124 Thessaloniki
Carl-Zeiss-Promenade 10 salif@auth.gr
07745 Jena
daniel.geibig@uni-jena.de
HUNGARY
Hartung, Jens
Technische Universität Kaiserslautern Enyedy, Éva
Fachbereich Chemie Department of Inorganic and Analytical Chemistry
Organische Chemie University of Szeged
Erwin-Schrödinger-Strasse 54 Dóm tér 7.
D-67663 Kaiserslautern PO Box 440
hartung@chemie.uni-kl.de 6701 Szeged
enyedy@chem.u-szeged.hu
Lippold, Ines
Institut für Anorganische und Analytische Chemie Jakusch, Tamas
Friedrich-Schiller-Universität Jena Department of Inorganic and Analytical Chemistry
Carl-Zeiss-Promenade 10 University of Szeged
07745 Jena Dóm tér 7.
ines.lippold@uni-jena.de PO Box 440
H-6721 Szeged
Plass, Winfried jakusch@chem.u-szeged.hu
Institut für Anorganische und Analytische Chemie
Friedrich-Schiller-Universität Kiss, Tamás
Lehrstuhl für Anorganische Chemie II Department of Inorganic and Analytical Chemistry
Carl-Zeiss-Promenade 10 University of Szeged
07745 Jena Dóm tér 7.
sekr.plass@uni-jena.de P.O.Box 440
H-6701 Szeged
tkiss@chem-u-szeged.hu

INDIA Garribba, Eugenio

University of Sassari
Chatterjee, Pabitra Via Vienna, 2
Department of Inorganic Chemistry I-07100 Sassari
Indian Association for the Cultivation of Science garribba@uniss.it
2A, 2B Raja S. C. Mallik Road
Jadavpur, Kolkata Lovat, Silvia
700032 West Bengal Department of Chemical Sciences
icpbc@iacs.res.in University of Padova
via Marzolo 1
Maurya, Mannar 35131 Padova
Department of Chemistry silvia.lovat@unipd.it
Indian Institute of Technolog Roorkee
Uttrakhand Sanna, Daniele
247 667 Roorkee C.N.R. Istituto di Chimica Biomolecolare
rkmanfcy@iitr.ernet.in Traversa La Crucca, 3
Baldinca-Li Punti
I-07040 Sassari
IRAN, ISLAMIC REPUBLIC OF Daniele.Sanna@icb.cnr.it
Majlesi, Kavosh Zonta, Cristiano

Chemistry Department Department of Chemical Sciences
Islamic Azad University University of Padova
Science & Research Campus via Marzolo 1
Hesarak 35131 Padova
1477893855 Tehran cristiano.zonta@unipd.it
kavoshmajlesi@gmail.com
Rezaienejad, Saghar JAPAN

Chemistry Department
Islamic Azad University Hashimoto, Masato
Science & Research Campus Fac. Syst. Eng., Dept. Mater. Sci. Chem.
Hesarak Wakayama University
1477893855 Tehran Sakaedani 930
saghar.rezaeinejad@gmail.com 640 8510 Wakayama
mh1043@sys.wakayama-u.ac.jp
Zare, Karim
Chemistry Department, Islamic Azad University, Hayashi, Yoshihito
Science & Research Campus Chemistry Department, Kanazawa University
Hesarak Kakuma
1477893855 Tehran 920-1192 Kanazawa
kzare110@hotmail.com hayashi@kenroku.kanazawa-u.ac.jp
Higuchi, Takeshi
ITALY Fac. Syst. Eng., Dept. Mater. Sci. Chem.
Wakayama University
Conte, Valeria Sakaedani 930
Chemical Sciences and Technology 640 8510 Wakayama
Università di Roma Tor Vergata dg7gl9@yahoo.co.jp
Via Ricerca Scientifica
00133 Roma Hirao, Toshikazu
valeria.conte@uniroma2.it Department of Applied Chemistry, Graduate School
of Engineering, Osaka University Yamada-oka
565-0871 Suita
hirao@chem.eng.osaka-u.ac.jp

Kanamori, Kan Yamamoto, Tomohiro

Department of Chemistry, Faculty of Science, Research & Development headquarters
University of Toyama Asahi soft drinks co., ltd.
Gofuku 3190 1-1-21, Midori
930-8555 Toyama 302-0106 Moriya-shi
kanamori@sci.u-toyama.ac.jp tomohiro.yamamoto@asahiinryo.co.jp
Kamiya, Shogo
Chemistry Department, Kanazawa University NETHERLANDS
Kakuma
920-1192 Kanazawa Wever, Ron
kamiyashogo@muki1.s.kanazawa-u.ac.jp University of Amsterdam
Katoh, Akira Nieuwe Achtergracht 129
Department of Materials and Life Science 1018 WS Amsterdam
Seikei University wever@science.uva.nl
3-3-1 Kichijoji-kitamachi, Musashino-shi
180-8633 Tokyo
katoh@st.seikei.ac.jp NIGERIA
Kawakami, Norifumi Omoruyi, Gloria

Biological Science, Hiroshima University Chemistry, Obafemi Awolowo University
Kagamiyama1-3-1, Adeyemi Campus
Higashi-hiroshima p.m.b 520
739-8526 Hiroshima Ondo state
kawakami@hiroshima-u.ac.jp 23434 Ondo
omoruyig@yahoo.com
Michibata, Hitoshi
Department of Biological Science
Hiroshima University, Graduate School of Science POLAND
Kagamiyama 1-3-1
739-8526 Higashi-Hiroshima Romanowski, Grzegorz
hmichi@hiroshima-u.ac.jp Faculty of Chemistry, University of Gdańsk
Sobieskiego 18/19
Sasai, Hiroaki PL-80952 Gdańsk
Inst. of Scientific and Industrial Research greg@chem.univ.gda.pl
Osaka University
8-1 Mihogaoka, Ibaraki-shi
567-0047 Osaka PORTUGAL
sasai@sanken.osaka-u.ac.jp
Adão, Pedro
Sakurai, Hiromu Centro de Química Estrutural
Department of Pharmaceutical Sciences Instituto Superior Técnico
Suzuka University of Medical Science Av. Rovisco Pais, 1
3500-3 Minami-tamagaki-chou, Mie 1049-001 Lisboa
513-0816 Suzuka pedro.m.adao@ist.utl.pt
sakuraih@suzuka-u.ac.jp
Almeida, Maria Marise
Ueki, Tatsuya UICOB- Laboratório de Biomateriais
Department of Biological Science Faculdade de Medicina Dentária de Lisboa
Hiroshima University Cidade Universitária
Graduate School of Science 1649-003 Lisboa
1-3-1 Kagamiyama PORTUGAL
739-8526 Higashi-Hiroshima marise.almeida@fmd.ul.pt
ueki@hiroshima-u.ac.jp

Aureliano, Manuel Gama, Sofia

Departamento de Química, Bioquímica e Farmácia, Química Inorgânica e Radiofarmacêutica
Faculdade de Ciências e Tecnologia Instituto Tecnológico e Nuclear
Universidade do Algarve Estrada Nacional 10
Campus de Gambelas 2686-953 Sacavém
8005-139 Faro sofiagama@gmail.com
maalves@ualg.pt
Geraldes, Carlos
Brissos, Rosa Departamento de Bioquímica
Departamento de Química, Bioquímica e Farmácia, Faculdade de Ciências e Tecnologia
Faculdade de Ciências e Tecnologia Universidade de Coimbra
Universidade do Algarve POBox 3126
Casa Brissos Vale Formoso 3001-401 Coimbra
8100-267 Loulé geraldes@ci.uc.pt
rosinha.brissos@gmail.com
Gonçalves ,Gisela
Butenko, Nataliya Centro de Química Estrutural
Departamento de Química, Bioquímica e Farmácia, Instituto Superior Técnico
Faculdade de Ciências e Tecnologia Av. Rovisco Pais, 1
Universidade do Algarve 1049-001 Lisboa
Campus de Gambelas gisela.goncalves@mail.ist.utl.pt
8005-139 Faro
Honzicek, Jan
n_butenko@hotmail.com
Instituto de Tecnologia Química e Biológica
Av. da República
2780-157 Oeiras
Castro, Maria Margarida
hohonza@post.cz
Departamento de Bioquímica
Faculdade de Ciências e Tecnologia
Humanes, Madalena
Universidade de Coimbra
Faculdade de Ciências da Universidade de Lisboa
P.O.Box 3126
Campo Grande
3001-401 Coimbra
1749-016 Lisboa
gcastro@ci.uc.pt
mmhumanes@fc.ul.pt
Cavaco, Isabel
Justino, Licínia
Departamento de Química, Bioquímica e Farmácia,
Departamento de Química
Universidade de Coimbra
Universidade do Algarve
Rua Larga
Campus de Gambelas
3004 – 535 Coimbra
8005-139 Faro
liciniaj@ci.uc.pt
icavaco@ualg.pt
Pereira, Ana
Fontes, Fábio
Campus de Gambelas
Rua das Oliveiras, n.º 23
8005-139 Faro
8500-601 Portimão
anamargaridapereira@gmail.com
fabiolevifontes@gmail.com
Pereira, Maria João

Fraqueza, Gil
Centro de Ciências do Mar
Escola Superior de Tecnologia
Urbanização Forte Novo Bloco C - r/c H
Campus da Penha
8125-214 Quarteira
8000 Faro
mjrpereiraster@gmail.com
gfraque@ualg.pt

Pessoa, João da Costa SLOVAKIA

Centro de Química Estrutural
Instituto Superior Técnico Schwendt, Peter
Av. Rovisco Pais, 1 Department of Inorganic Chemistry
1049-001 Lisboa Comenius University
joao.pessoa@ist.utl.pt Mlynska dolina
842 15 Bratislava
Pombeiro, Armando schwendt@fns.uniba.sk
Instituto Superior Técnico Sivak, Michal
Av. Rovisco Pais, 1 Department of Inorganic Chemistry
1049-001 Lisboa Comenius University
pombeiro@ist.utl.pt Mlynska dolina CH2
842 15 Bratislava
Ramos, Susana sivak@fns.uniba.sk
REQUIMTE/CQFB, Departamento de Química,
Universidade Nova de Lisboa SPAIN
2829-516 Caparica
s.ramos@dq.fct.unl.pt Porto Avecilla, Fernando
Departamiento de Quimica Fundamental,
Rangel, Maria Universidade da Coruña
Chemistry, Instituto de Ciências Biomédicas de Zapateira s/n
Abel Salazar 15071 A Coruña
Largo Abel Salazar, 2 avecil@udc.es
4099-003 PORTO
mcrangel@fc.up.pt Zorzano, António
Head, Molecular Medicine Programme
Silva, Telma Institute for Research in Biomedicine - IRB
Instituto Superior de Engenharia de Lisboa Baldiri Reixac, 10
Rua Conselheiro Emídio Navarro 08028 Barcelona
1950-062 Lisboa antonio.zorzano@irbbarcelona.org
tsilva@dem.isel.ipl.pt
Tomaz, Isabel SWEDEN

Centro de Ciências Moleculares e Materiais
Faculdade de Ciências da Universidade de Lisboa Angus-Dunne, Sarah
Campo Grande Chemical Engineering, Mälardalens University
1749-016 Lisboa HST Box 325
isabel.tomaz@ist.utl.pt 63105 Eskilstuna
sarah.angus-dunne@mdh.se
Nilsson, Jessica
Tyagi, Amit
Department of Chemistry, Lund University
Kemisk Fysik
Instituto Superior Técnico
Kemicentrum
Av. Rovisco Pais, 1
Getingevägen 60
1049-001 Lisboa
22241 Lund
amittyagig71@gmail.com
jessica.nilsson@chemphys.lu.se
Pettersson, Lage
Department of Chemistry, Umeå University
SE-901 87 Umeå
lage.pettersson@chem.umu.se

TAIWAN Makinen, Marvin

Biochemistry & Molecular Biology Department,
Chen, Chien-Tien University of Chicago
Department of Chemistry, Center for Integrative Science
National Taiwan Normal University 929 East 57th Street
#88, Sec. 4, Ding-jou Road 60637 Chicago, Illinois
11650 Taipei makinen@uchicago.edu
chefv043@ntnu.edu.tw
McLauchlan, Craig
Chemistry Department, Illinois State University
UNITED KINGDOM
CB 4160
61790-4160 Normal, IL
Correia, Maria
ccmclau@ilstu.edu
Chemistry Department, Imperial College
South Kensington
Pecoraro, Vincent
SW7 2AZ London
Chemistry Department, University of Michigan
m.rodrigues-correia@imperial.ac.uk
930 N. University Avenue
48109-1055 Ann Arbor
Littlechild, Jennifer
vlpec@umich.edu
Henry Wellcome Building for Biocatalysis
School of Biosciences, University of Exeter
Willsky, Gail
Stocker Road
Biochemistry Department, University at Buffalo
EX4 4QD Exeter
School of Medicine and Biomedical Sciences
J.A.Littlechild@exeter.ac.uk
140 Farber Hall
Ross, Allison 14214 Buffalo
Chemistry Departement, University of Edinburgh gwillsky@buffalo.edu
Office 96, Joseph Black Building, Kings Buildings,
West Mains Road
URUGUAY
EH9 3JJ Edinburgh
s0564788@sms.ed.ac.uk
Gambino, Dinorah
Inorganic Chemistry Department
UNITED STATES Faculty of Chemistry
Gral Flores 2124
Butler, Alison 11800 Montevideo
Department of Chemistry & Biochemistry, dgambino@aduanas.gub.uy
University of California
93196-9510 Santa Barbara
butler@chem.ucsb.edu YUGOSLAVIA
Cohen, Mitchell Colovic, Mirjana

Environmental Medicine Department of Physical Chemistry
New York University School of Medicine Institute of Nuclear Sciences
7 Old Forge Road Mike Petrovica 12-14
10987 Tuxedo Vinca, P.O.Box 522
mitchell.cohen@nyumc.org 11001 Belgrade
colovicm@vin.bg.ac.yu
Crans, Debbie C.
Chemistry Department, Colorado State University Krstić, Danijela
1301 Center Av , CO 80523 Biochemistry Department
80523 Fort Collins Institute of Medicinal Chemistry, School of Medicine
crans@lamar.colostate.edu University of Belgrade
Višegradska 26
Krzystek, Jurek 11000 Belgrade
National High Magnetic Field Laboratory krsticdana@yahoo.com
1800 E. Dirac Dr.
32310 Tallahassee
krzystek@magnet.fsu.edu

Author
Index

Author Index

Author Index AI1
A Coradin, T. – O56
Adão, P. – O3, O44, P5, P9, P15 Correia, I. – O3,
O3 O44, P5, P15
Alegria, E. C. B. A. – O50 Costa Pessoa, J. – O3, O8, O13, O15, O19, O37,
Almeida, M – O39 O44, O46, P5, P6, P9, P15, P32
Amata, Y. – P47 Crans, D. C.- O20,
O20 O22, P17, P41, P51
Amorim, M. J. – O9 Creagh, A. L. – O23
Andersson, I. – O11
Andrade, M. – O9 D
Angus-Dunne, S. – P42, P43 Degerman, E. – P24
Antunes, O. – O47 De Gioia, L. – O10
Arends, I. – O1, P13 Ding, W - O26
Arias, A. R. – P37 Dilović, I. – P26
Arrambide, G. – O15, O32 Djobourov, M. – O56
Arya, A. – P10 Dorner, N. A. – P50
Aubry, J.-M. – O40 Drouza, C. – O54, P18
Aureliano, M. - O34,
O34 P3, P38, P44, P46, P51, P52 Duarte, R. O. – P3, P44, P46, P52
Avecilla, F. – O3, O8, O13, O19, O44,
O44 O46, P5, P15, Dunne, S. – P42, P43
P32 Durupthy, O. – O56
B E
Backhus, E. A. – P50 Enyedy, E. A. – O14, P19
Bányai, I. – P14 Escribano, E. – O37
Baran, E. J. – O51,
O51 P36 Etcheverry, S.B. – O32,
O32 P36
Barrio, D. A. – O32 Eriksson, L. A. – P42, P43
Barroso, S. – P9 Evgeniou, E. – O48
Barta, C. A. – O23
Baruah, B. – P17, P51 F
Benítez, J. – O15, P37 Fabbianesi, F. – O1, P13
Berardi, S. – O1 Faísca, M. J. – P38
Biré, A. S. – O43, O46, P45, P48 Faneca, H. – O19
Bisht, M. – O8 Fayolle, B. – O56
Bistram, B. A. – O22, P41 Fernandez, T. L. – O47
Bordbar, K. – O23 Figueroa, D. – P37
Bonchio, M. – O1 Fiolhais, C. – P21, P22
Bosnjakovic-Pavlovic, N. – O43, O46, P45, P48 Floris, B. – O1, P13
Bouhmaida, N. – O46 Fontes, F. L. – P44
Brissos, R. F. – P44, P46 Fraqueza, G. – P44, P46
Bruzzone, L. – O32, P36 Fraústro da Silva, J. J. – O50
Burrows, H. D. – P21, P22 França, T. C. C. – P37
Fujinami, K. – O16
C
Carn, F. - O56 G
Carvalho, E. – P38 Gabriel, C. – O17, P27
Castro, M. M. C. A. – O13, O19,
O19 P32 Gáliková, J. – O18
Cavaco, I. - O37 Galloni, P. – O1, P13
Clark, M. – O22, P41 Gama, S. - O37
Chatterjee, P. B. – P16 Gambino, D. – O15,
O15 O32, P37
Chaudhury, M. – P16 Gameiro, P. – O9
Chen, C.T. - O2,
O2 O28 Garat, B. – O15, P37
Chi, L.-H. – O22, P41 Garribba, E. – O30,
O30 P33, P34, P35
Choukroun, R. – P7 Geibig, D. – P1
Cindrić, M. – P26 Gekko, K. – P47
Colovic, M. – P45 Geraldes, C.F.G.C. – O13, O19, P21, P32
Cohen, M. D. – O36 Ghermani, N.E. – O43, O46
Conte, V. – O1, P13, P14 Ghio, A. J. - O36
Conzen, S. D. – O28 Gil, V. M. S. – P21, P22

AI2 Author Index
Godzala III, M. – O22 Kumar, M. – P6

Gonçalves, G. - O13, O19, O39, P32 Kustin, K. – O16
Gorzsás, A. – O11 Kuznetsov, M. – O50
Grayson, R. Z. – O22, P41 Kuzvetsov, M. – O3
Greiner, B. A. – P50
Guedes da Silva, M. F. C. – O50 L
Guggeri, L. – O15, P37 Leite, A. – O9
Gutiérrez-Merino, C. – P3, P51 Lenhardt, J. M. – P17
Li, M. – O26
H Lichter, J. B. – O24
Hach, D. – O7 Licini, G. – O29, P8
Hartung, J. – O7 Lima, M. C. P. – O19
Hasan, Z. – O40 Lin, Y.-H. – O2
Hashimoto, M. - O12,
O12 P20 Lippold, I. – P49
Haukka, M. – P24 Lis, T. – P12
Hayashi, Y. - O45,
O45 P4 Lisha, W. – P42
Haynes, C. A. – O23 Littlechild, J. - O41
Henao, F. – P51 Livage, J. – O56
Higuchi, T. – O12, P20 Lodyga-Chruscinska, E. – P35
Hirao, T. - O52 Lorber, C. – O6
Hiromura, M. – O21 Lovat, S. – O29, P8
Hober, D. – O40 Lorber, C. – P7
Holubová, J. – P40
Honziček, J. - O49,
O49 P40 M
Humanes, H. – O39 Machado II, A. J. – O28
Maestro, M. – O19
I Majlesi, K. – O33A
33A, O33B
Isobe, K. – O45, P4 Makinen, M. W. - O28
Marchán, E. – P37
J Martins, A. M. – P9
Jakusch, T. – O14, O48, P2 Martins, H. – P38, P44
Johnson, M. D. – P17 Martins, H. – P38
Justino, L. L. G. – P21, P22 Martins, J. – P44, P46
Martins, L. M. D. R. S. – O50, P28
K Matković-Čalogović, D. – P26
Kabanos, T. A. - O48 Matsugo, S. – O16
Kanamori, K. - O16, P47 Matsumura, Y. - O25
Kamiya, S. – P4 Matsuo, K. – P47
Kao, C.-M. – O28 Maurya, M. R. – O3, O8,
O8 P6, P10
Katayama, T. – O5 Mba, M. – O29, P8
Katoh Akira – O25 McLauchlan, C. C. - O55,
O55 P50
Kaupp, M. – P21, P22 McNeill, J. H. – O24
Kawakami, N. – O35, P47 Meyer, J. E. – P50
Keramidas, A. D. – O48, O54,
O54 P18, P30 Melman, A. – O48
Kikushima, K. – O52 Melo, M. J. – P38
Kirillov, A. M. – O50 Michibata, H. - O35,
O35 P23, P47
Kirillova, M. V. – O50 Micera, G. – O30, P33, P34, P35
Kiss, D. – P33 Mioc, U. – O46
Kiss, T. – O14,
14 O48, P2, P19 Mishra, G. S. – O50
Khorrami, S. A. – P31 Moreno, V. – O37
Khorramdin, B. – P31 Moriuchi, T. – O52
Kostyniak, P. J. – O22 Moura, J. J. G. – P3, P44, P46, P52
Krstic, D. – P48 Muglia, C. I. – P36
Krzystek, J. - O53
Kubo, K. – O16
Kumar, A. – O8, P6

Author Index AI3
N S
Natálio, F. – O39 Sadler, P. J. – P39
Nicolai, M. – O39 Sakai, Y. – O16
Nikolakis, V. A. – O48 Sakurai, H. – O21,
O21 O25, P20
Nilsson, J. – P24 Salas, P. F. - O24
Nogueira, F. – P21 Salifoglou, A. - O17,
O17 P27
Nordlander, E. – P24 Sanna, D. – O30, P33, P34, P35
Nouri, O. – O37 Sasai, H. - O5
Nowicki, W. – P11, P12 Scaife, M. S. – O24
Nunes, A. – O9 Scarpellini, M. – O47
Schneider, C. J. – O10
O Schulz, H. – O7
Okeya, S. – O12, P20 Schwendt, P. – O18,
O18 P29
Olakunlemi, A. – P25 Shen, S. – O28
Oluwaseun, A. – P25 Shintaku, K. – P23
Omoruyi, G. – P25 Sigalas, M. P. – O48
Orvig, C – O23,
O23 O24 Sikorski, A. – P11
Silva, A. – O9
P Silva, C. – O9
Pacigová, S. – P29 Silva, J. A. L. – O50
Palacio, L. – O19 Silva, T. F. S. – O50, P28
Paláčková, H. – P40 Silvagni, A. – P14
Palavra, A. – O50 Simoni, Z. – P37
Parsons, S. – P39 Šinkorová, Z. – P40
Pecoraro, V. L. - O10 Sivák, M. – O18, P29
Pedro, C. – P38 Smee, J. J. – O22
Pereira, A. M. – P51 Smircich, P. – P37
Pereira, M. J. – P38 Soares, S. S. – P3
Pettersson, L. - O11,
O11 P14 Sobral, A. J. F. N. – P21
Pierlot, C. – O40 Stylianou, M. – O48
Pisano, L. – P33 Sordi, D. – O1, P13
Plass, W. - O38,
O38 P1, P49 Spasojević, Anne – O43,
O43 O46
Pombeiro, A. J. L. - O50,
O50 P28 Steunou, N – O56
Pontini, M. – O29, P8 Strid, A. – P42
Stylianou, M. – O54, P30
R
Ramos, M. L. – P21, P22 T
Ramos, S. – P52 Takizawa, S. – O5
Rangel, M. C. - O9 Tatiersky, J. – O18
Rehder, D. – O1, O31,
O31 P13, P24 Thompson, K. H. – O23, O24
Renirie, R. – O40 Tiago, T. – P44, P46, P51, P52
Rezaienejad, S. – O33A, O33B
33B Tomaz, I. – O13,
13 O15, O19, O37, O46, P32
Ribeiro, E. – O37 Tsalavoutis, J. T. – O48
Ribot, F. - O56
Rito, E. – P46 U
Rivadeneira, J. – O32, P36 Ueki, T. – O35, P47, P23
Róbert, G. – P29
Robertson, N. – P39 V
Rodrigues, F. – P38 Várnagy, K. – P33
Rolón, M. – P37 Vasic, V. – P45, P48
Romão, C. C. – O49 Vega, C. – P37
Romanowski, G. – P11, P12 Vieites, M. – P37
Rosenthal, E. C. E. - O4 Vinklárek, J. – O49, P40
Ross, A. – P39 Vinsetin, L. C. – O47
Rubčić, M. – P26

AI4 Author Index
W
Wada, N. – O16
Wanke, R. – P28
Weberski, M. P. – O55
Wei, D. - O26
Wever, R. - O40
Wilde, A. – O40
Willsky, G. R. - O22,
O22 P41
Wojtczak, A. – P11
X
Xie, Q. G. – O28
Y
Yang, J. – O26
Yoshikawa, Y. – P20, O25
Yoshihara, M. – P23
Yun, D. – O28
Z
Žák, Z. – O18
Zampella, G. – O10
Zare, K. – O33A, O33B, P31
Zárybnická, L. – P40
Zhou, X. – P43
Zonta, C. – O29,
O29 P8
Zorzano, A. - O27

V6 Symposium: The 6th International Vanadium Symposium" July 17 To 19th, 2008 Lisbon, Portugal

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V6 Symposium: The 6th International Vanadium Symposium" July 17 To 19th, 2008 Lisbon, Portugal

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6 th

The Chemistry and Biological

João Costa Pessoa (Chair), IST-TU Lisbon, Portugal

National Organizing Committee

João Costa Pessoa, IST-TU Lisbon, Portugal

International Advisory Board

Valeria Conte, Rome, Italy

V6 Symposium ∷ Lisbon 2008

V6 Symposium ∷ Lisbon 2008

The Calouste Gulbenkian Foundation gardens

V6 Symposium ∷ Lisbon 2008

The V6 Symposium Venue at Calouste Gulbenkian Foundation

V6 Symposium ∷ Lisbon 2008

V6 Symposium ∷ Lisbon 2008

Scientific Program – Oral Sessions

9:10 - Introductory Remarks

11:40 - O6 - Lorber, C. France) – “[ONNO]-type Amine Bis(phenolate)-Based Vanadium Catalysts

14.30 - O10 -Pecoraro, V. (USA) – “Computationally Assisted Design of Asymmetric Sulfoxidation

16:50 Poster Session / Coffee Break

17:10 Poster Session

17:50 - O15 - Gambino, D. (Uruguay) – “Vanadium complexes with polipyridyl ligands as

V6 Symposium ∷ Lisbon 2008

Friday, 18th July

9:10 - O19 - Castro, M. (Portugal) – “Chemical and Biochemical Studies of a 5-hydroxy-

11:40 - O25 - Katoh, A. (Japan) – ”Evaluation of Insulin-Mimetic Activities of Vanadyl Complexes

16:50 Poster Session / Coffee Break

17:10 Poster Session

17:50 - O34 - Aureliano, M. (Portugal) – “Recent advances in decameric vanadate biochemistry”

20.30 Symposium dinner

V6 Symposium ∷ Lisbon 2008

Saturday, 19th July

9:10 - O38 - Plass, W. (Germany) – “Vanadium haloperoxidases as versatile biological matrix:

14.30 - O48 - Kabanos, T. (Greece) – “Oxovanadium(V) compounds with bis(hydroxyamino)-

17:10 - O53 - Krzystek, J. (USA) –” Electron Paramagnetic Resonance of Vanadium(III)

V6 Symposium ∷ Lisbon 2008

Scientific Program – Poster Titles

P1 - Daniel Geibig DFT Model Studies of Vanadium Chloroperoxidase: Dissociative or Associative

P2 - Tamás Jakusch – “Anion “complexes” of diperoxo-vanadate Model compounds for

P3 - Manuel Aureliano – “Decameric vanadate reduction by physiological concentrations of

P4 - Shogo Kamiya – “Template synthesis of a spherical polyoxovanadate(V) by oxidative coupling

P5 - Pedro Adão – “Asymmetric oxidation of thioanisole catalysed by reduced Schiff base

P6 - Amit Kumar – “Oxidation of p-chlorotoluene and cyclohexene catalysed by polymer-

P7 - Christian Lorber – “Organometallic chemistry of vanadium with B(C6F5)3”

P8 - Silvia Lovat – “Vanadium(V) complexes as oxidation catalysts”

P9 - Ana M. Martins – “Vanadium diamine bisphenolate complexes: Synthesis, structures and

P10 - Mannar R. Maurya – “Polystyrene bound dioxovanadium(V) complex of histamine derived

P11 - Grzegorz Romanowski – “Dioxovanadium(V) Schiff base complexes of R(-)-1,2-

P13 - Valeria Conte – “V-catalysed oxidations with H2O2”

P17 - Debbie C. Crans – “Electron transfer reactions of an amavadin-like complex”

P18 - Chryssoula Drouza – “Interaction of Hydroquinonate ligands with VV and MoVI”

P20 - Takeshi Higuchi –“ Syntheses and characterisation of novel [VO(O2)2L](L=ligand) type

V6 Symposium ∷ Lisbon 2008

P24 - Jessica Nilsson – “Synthesis of new oxo-vanadium(IV) coordination compounds and

P26 - Mirta Rubčić – “Vanadium induced cyclization of thiosemicarbazone: formation of

P27 - Athanasios Salifoglou – “A new vanadium(V)-peroxo species in the presence of physiological

P32 - Gisela Gonçalves – “Interaction of a pyrimidinone-V(IV) complex with human serum

P33 - Daniele Sanna – “VIVO complexes with bis(pyridyl) derivatives”

P37 - Dinorah Gambino – “Modifying antiprotozoa activity of organic compounds through

P39 - Allison Ross – “Oxovanadium(IV) macrocycles: potential antivirals against HIV”

P41 - Gail R. Willsky – “Biological variability in the anti-apoptotic effects of vanadium”

V6 Symposium ∷ Lisbon 2008

P43 - Sarah Angus-Dunne – “Hydroxylamino-vanadate derivatives as protein tyrosine phosphatase

P49 - Ines Lippold – “Modeling supramolecular interactions of vanadium species”