LIGAND FIELD THEORY

BC-101

Ligand field theory (LFT)

It describes the bonding, and orbital arrangement
of coordination complexes.
A transition metal ion has nine valence atomic
orbitals - consisting of five (n)d, one (n+1)s, and three
(n+1)p orbitals. These orbitals are of appropriate
energy to form bonding interaction with ligands.

The LFT analysis is highly dependent on the geometry

of the complex, but most explanations begin by
describing octahedral complexes, where six ligands
coordinate to the metal.

ASSUMPTIONS

The bonding of orbitals leads to the formation are of

two states: Bonding and Antibonding
Bonding orbital is the lower energy state while
Antibonding orbital is the higher energy state.

Explanation:

The six bonding molecular orbitals that are formed

are "filled" with the electrons from the ligands, and
electrons from the d-orbitals of the metal ion occupy the
non-bonding and anti-bonding MOs.
The energy difference between the latter two types of
MOs is called O (O stands for octahedral) and is
determined by the nature of the -interaction between the
ligand orbitals with the d-orbitals on the central atom. As
described above, -donor ligands lead to a small O and
are called weak- or low-field ligands, which form high
spin complexes whereas -acceptor ligands lead to a large
value of O and are called strong- or high-field ligands
leading to low spin complexes.

The formation constant (K):

The formation constant (K1) is a measure of the stability
of a complex (ML) formed by a metal ion (M) with a
ligand (L) in aqueous solution, and refers to the
equilibrium:
M

ML

The constant is expressed as:

K1

[ ML ]
[M][L]

K values are usually rather large, and so are usually

given as log K values.

Formation constants (K1) of metal ions with

hydroxide:
In the given example, the hydroxide ion is a ligand. So when,
[Fe(H2O)5(OH)]2+ is formed, we can regard this as replacement
of a coordinated water by hydroxide, rather than as loss of a
proton. The two equations are related as follows:

[Fe(H2O)6]3+
[Fe(H2O)6]3+

[Fe(H2O)5(OH)]2+ + H+ pKa = 2.2

+ OH- [Fe(H2O)5(OH)]2+ + H2O
log K1 = pKw pKa
= 14.0 2.2
= 11.8

The hydrolysis of metal ions in

aqueous solution.

Metal aqua ions:

Metal ions in aqueous solution exist as aqua ions, where
water molecules act as ligands, and coordinate to the
metal ion via the oxygen donor atoms as shown for the
[Al(H2O)6]3+ hexaaqua ion below:
Figure 1. The aluminum(III) hexaaqua
ion, present in aqueous solution and
in many salts such as [Al(H2O)6]Cl3,
often written as AlCl3.6H2O.

Ligand Substitution in complexes:

A ligand substitution reaction is one in which a ligand in
a complex ion is replaced by another ligand. In many
ligand substitution reactions, water molecules in an
aqueous solution of a complex ion are replaced by
another ligand.

Cytochromes
All cytochromes contain iron, and the iron atom in all
cytochromes is coordinated by a planar array of four
nitrogen atoms provided by a cyclic tetradentate ligand
called a porphyrin. The ironporphyrin unit is called
a heme group. The structures of a typical porphyrin
(protoporphyrin IX) and its iron complex (protoheme)
are shown here. In addition to the four nitrogen atoms
of the porphyrin, the iron in a cytochrome is usually
bonded to two additional ligands provided by the
protein,

Cytochromes
In a cytochrome c, the heme
iron is coordinated to the
nitrogen atom of a histidine
imidazole and the sulfur atom
of a methionine thioether, in
addition to the four nitrogen
atoms provided by the
porphyrin.

Fe2+ is d6and can be either high spin (with four unpaired

electrons) or low spin (with no unpaired). Similarly, Fe3+ is d5 and
can also be high spin (with five unpaired electrons) or low spin
(with one unpaired electron). In low-spin heme complexes, both the
Fe2+ and the Fe3+ ions are small enough to fit into the hole in the
center of the porphyrin; hence the iron atom lies almost exactly in
the plane of the four porphyrin nitrogen atoms in both cases.
Because cytochromes b and c are low spin in both their oxidized
and reduced forms, the structures of the oxidized and reduced
cytochromes are essentially identical.
Hence minimal structural changes occur after oxidation or
reduction, which makes electron transfer to or from the heme very
rapid.

Haemoglobin and ligand substitution

Red blood cells carry oxygen efficiently because they contain
haemoglobin, a complex protein composed of four polypeptide chains. Each
protein chain contains four non-protein components called haem groups. Each
haem group has an Fe2+ ion at its centre oxygen can bind to the Fe2+ ion.
This allows haemoglobin to carry out its function of transporting oxygen
around the body.
When the Fe2+ ion in each haem group is bound to oxygen, the haem group is
red in colour. As blood passes through the lungs, the haemoglobin picks up
oxygen and carries it to the cells, where it can be released. Red blood cells
can also pick up carbon dioxide as a waste product to be transported back to
the lungs, where it is released.
Figure 3 shows the coordinate bonds formed around the Fe2+ ions in a haem
group.
There are four coordinate bonds between the Fe2+ ion and the nitrogen
atoms in the haem structure.
A further coordinate bond is formed to the protein globin.
A final coordinate bond can form to an oxygen molecule, which is then
transported.

Along with oxygen, small molecules such as CO and NO bind to

deoxymyoglobin even more tightly than does O2. The interaction of
the heme iron with oxygen and other diatomic molecules involves
the transfer of electron density from the filled t2gorbitals of the lowspin d6 Fe2+ ion to the empty * orbitals of the ligand. In the case of
the Fe2+O2interaction, the transfer of electron density is so great
that the FeO2 unit can be described as containing low-spin
Fe3+ (d5) and O2. We can therefore represent the binding of O2 to
deoxyhemoglobin and its release as a reversible redox reaction:
Fe2+ + O2 Fe3+O2
.

Although CO has a much greater affinity for a ferrous heme than does
O2 (by a factor of about 25,000), the affinity of CO for
deoxyhemoglobin is only about 200 times greater than that of O2,
which suggests that something in the protein is decreasing its affinity
for CO by a factor of about 100. Both CO and NO bind to ferrous
hemes in a linear fashion, with an FeC(N)O angle of about 180, and
the difference in the preferred geometry of O2 and CO provides a
plausible explanation for the difference in affinities.

the imidazole group of the distal histidine is located precisely where

the oxygen atom of bound CO would be if the FeCO unit were linear.
Consequently, CO cannot bind to the heme in a linear fashion; instead,
it is forced to bind in a bent mode that is similar to the preferred
structure for the FeO2 unit. This results in a significant decrease in
the affinity of the heme for CO, while leaving the O2 affinity
unchanged, which is important because carbon monoxide is produced
continuously in the body by degradation of the porphyrin ligand (even
in nonsmokers).