BIOLOGIC OXIDATION

ENERGI
(ATP)
Source of ATP :
1. Glycolysis.
2. Krebs Cycle.
3. Oxidative Phosphorylation.

Ox-red reactions
O2 accept single electron
 Oxidation-reduction potential

Oxidation : the removal of electrons

Reduction : the gain of electrons
Redox potential (E0) : the free energy change
is proportionate to the tendency of reactants
to donate or accept electrons
Redox potential of a system (Eo) is compared
with the potential of the hidrogen electrode
Biologic systems E0 expressed at PH 7
and electrode potential of H : 0,42 volts
 System EO volts
H+/H2 -0.42
NAD+/ NADH -0.32
Lipoate; ox / red -0.29
Acetoacetate/ 3 -0.27
hydroxybutyrate -0.19
Pyruvate/ lactate -0.17
Oxaloacetate/ malate +0.03
Fumarate/ succcinate +0.08
Cytochrome b; Fe3+/Fe2+ +0.10
Ubiquinone; ox/red +0.22
Cytocrome c1; Fe3+/Fe2+ +0.29
Cytocrome a; Fe3+/Fe2+ +0.82
Oxygen/ water
 Enzymes in ox-red
Called oxidoreductases
classified into 4 groups:
- oxidases
- dehydrogenases
- hydroperoxidases
- oxygenases
 Oxidases
Catalyzing the removal hydrogen and using
oxygen as a acceptor form water (H2O) or
hydrogen peroxide(H2O2)
Some oxidases contain copper and others
are flavoproteins
Cytochrome oxidase ( cyt.a.a3 ) :
heme protein contain Cu
terminal component of respiratory chain
contain two molecules of heme as
prosthetic group and Cu
 Oxidases

Flavoprotein enzyms contain FMN or FAD as

prosthetic groups
FMN and FAD are formed in body from riboflavin
They are tightly bound to their apoenzymes
but not covalently
Exampels: L-amino acid oxidase (in kidney),
xanthine oxidase (in intestinal, kidney, liver),
aldehyde oxidase (in liver) and glucose
oxidase (in fungus)
AH2 / 2 O2
1 AH2 O2
(Red)

OXIDASE OXIDASE

A H2O A H2O2
(Ox)
A B

Oxidation of a metabolite catalyzed by an oxidase (A)

forming H2O, (B) forming H2O2
 Dehydrogenases
Can not use oxygen as a hydrogen acceptor
Performing two main functions:
1. transfer hydrogen in a coupled oxidation
reduction reaction
specific for their substrates, but utilize
common coenzymes
useful in enabling oxidative process to
occur in the absence of oxygen
2. components in respiratory chain
transfer electron from substrate to
oxygen
Dehydrogenases link NAD
Using NAD+ or NADP+ as a coenzyme
These coenzyme are formed in body from
niacin
- freely and reversibly dissociate from their
apoenzymes
- NAD linked D-ase: oxidative pathways of
metabolism (glycolysis, krebs cycle,
respiratory chain)
- NADP linked D-ase: characteristically in
reductive synthesis (fatty acid synthesis,
steroid synthesis and PMP-shunt)
Dehydrogenases link riboflavin
Using FMN and FAD as a coenzyme
- more tightly bound to their apoenzymes
- most of them are concerned with electron
transport in / to resp chain
- NADH D-ase carrier of electrons
between NADH and components of higher
redox potential
- succinate D-ase, acyl Co-A D-ase, glycerol
3 P D-ase transfer electrons directly from
substrate to resp. chain
 Cytochromes as dehydrogenase

Classified as dehydrogenases, except for

cytochrome oxidase
- as carriers of electrons from flavoproteins to
cytochrome oxidase in the resp chain
- exampels: cyt b, c1, c, a, a3 (resp chain) and
cyt P 450, b5 (endoplasmic reticulum)
AH2 Carrier BH2
(Red) (Ox) (Red)

A Carrier-H2 B
(Ox) (Red) (Ox)
DEHYDROGENASE DEHYDROGENASE
SPECIFIC FOR A SPECIFIC FOR B

Oxidation of a metabolite catalyzed by coupled

dehydrogenases
 Hydroperoxidases

Using hydrogen peroxide or an organic

peroxide as substrate
Two type : - peroxidase
- catalase
Protecting against harmful peroxides
Peroxides generate free radicals
disrupt membranes and cause cancer and
atherosclerosis
 Peroxidases
Reducing peroxides using various electron
acceptors (ascorbate, quinones, cyt c):
H2O2 + AH2 2H2O + A
Founding in milk, leukocytes, platelets,
erythrocytes and other tissues involved in
eicosanoid metabolism
Glutathione peroxidase, containing selenium
destruction of H2O2 and lipid
hydroperoxidases protecting membrane
lipids and Hb
 Catalase
Using hydrogen peroxide as electron donor and
electron acceptor:
2 H2O2 2H2O + O2
In addition to possessing peroxidase activity, it
is able to use one of H2O2 as a substrate
(electron donor) and another of H2O2 as an
oxidant (electron acceptor)
Founding in blood, bone marrow, mucous
membranes, kidney and liver
 AH2 A

AH2
A

O2 H2O2 CATALASE 2H2O

OXIDASE

H2O2 O2

Role of catalase in the destruction of hydrogen peroxie

 Oxygenases
Catalyzing the direct transfer and
incorporation of oxygen into a substrate
Divided into two subgroups:
1. Dioxygenases / oxygen transferase
Incorporating both atoms of oxygen into
substrate: A + O2 AO2
2. Monooxygenases
Mixed function oxidases and
hydroxylases incorporate only 1 atom
of oxygen into substrate, the other oxygen
is reduced to water
 MONOOXYGENASES

Need an additional electron donor /

cosubstrate ( Z ):
A-H + O2 + ZH2 A-OH + H2O + Z
Cytochromes P450 are monooxygenases (as
cosubstrate ) important for
detoxification of many drugs and for
hydroxylation of steroids
NADH and NADPH donate reducing
equivalents for the reduction of cyt P450
 Cytochrome P 450
Mitochondrial cyt P450 systems in
steroidogenic tissues biosynthesis of
steroid hormones from cholesterol
Mitochondrial cyt P450 systems in kidney
metabolism of vitamin D
Mitochondrial cyt P450 systems in liver
biosynthesis of bile acid
 Superoxide free radicals (O2-)
Generated from transfer of a single
electron to O2
It is formed reduced flavin, are
reoxidized univalently by molecular oxygen
Superoxide dismutase in aerobic
organisms removal O2- , the reaction:
O2- + O2- + 2H+ H2O2 + O2
Superoxide can reduce oxidized cyt c:
O2- + cyt c (Fe3+) O2 + cyt c (Fe2+)
Exposure to an atmosphere of 100%
oxygen causes an adaptive increase in
superoxide dismutase