CHAPTER 11 NATURALLY-OCCURRING CO-ORDINATION

COMPLEXES

OBJECTIVES. In this Chapter we consider some

naturally-occurring Complexes Co-ordination Complexes.

The importance of many Co-ordination Complexes in

Biological systems cannot be stressed enough . For example,
without photosynthesis, which we know takes place in
presence of chlorophyll, it is actually very hard to imagine
what life would be like. The process of taking up oxygen
from the air and transporting it to the tissues is facilitated by
the heme complexes in hemoglobin. Once the blood is in the
tissues, the oxygen is handed over to myoglobin which stores
it until it is required for respiration . Again, it is difficult to
imagine life without the hemes in both myoglobin and
hemoglobin.
An understanding of co-ordination chemistry is thus, not just
an academic subject ...it actually helps us understand some
very important biologicalprocesses.

Macrocylic Ligands Occurring In Biological Complexes.

A macrocylic Ligand is one with all donor atoms occurring in an
enclosed ring system. By a
“ ring”, we do not mean something cyclic with a constant radius but
rather that ,the atoms are joined in such a way that one can go through
a cycle without breaking the ring. Examples of such ligands are shown
in Figures 11.1,11.2 and 11.3 . The ligand shown in Figure 11.1 forms
the skeleton of hemes(ie ligands with iron(II) as the central atom.
Figure 11.2 is the skeleton of chlorophylls, and Figure 11.3 is a
skeleton of vitamin B12 .
 NH N NH N N N

N HN N HN NH
N

Figure 11.1 Porphyrin Ring System

Figure 11.2 Chlorin Ring System Figure 11.3 corrin ring system

When we say that a ligand has donor atoms in a ring, we do not mean
that these are in a smooth circular ring. Rather, it means that the
donor atoms are connected with a chain that completes a ring .
A Heme. When a ferrous ion is put at the centre of the porphyrin ring
such as the one in Figure shown in Figure 11.4, we get a heme. The
heme may contain various side groups. The particular one in Figure
11.4 is as found in myoglobin.
Specific Examples of Naturally-occurring Co-ordination
Complexes.

Figure 11.4. A Heme of

Figure 11.5. Myoglobin

X
myoglobin
(X is either O2 or H2O
CH2 CH3
CH2 CH3 H3C
H3C
NFeN CH2 NFeN CH2

NN H3C
NN CH3
H3C CH3

HOOC CHOOH
HOOC CHOOH

Attachment of the globin at the 5th co-ordination

Site of the Heme

The Globin: This is a peptide chain with XXX amino acids depending
on source. The amine acid co-ordinated ti iron at the fifth co-
ordination site of the iron-porphyrin complex is histidine. It is notable
that the amine is co-ordinated to the central metal ion using the imine
nitrogen on the imidazole ring of histidine See Figure 11.6.
 Figure 11.6 - Stucture of Histidine

Imine Nitrogen on Imidazole ring of histidine

NH2
N
H2
C CH
HN
C O

OH

Chlorophylls . The green colouring matter in vegetation contains

many chromophores( substances which can absorb colour). One of
these is chlorophylla.( Figure 11.7)

Figure 11.7 Chlorophylla.

CH2
CH3
H3C
N N CH3
Mg
N N
H3C CH3
O
CO
OCH3
O=C
O
CH2 chlorophylla
CH
CCH3
CH2 The 16 -carbon phytyl Chain
CH2
CH2
3

H-C-CH3
CH3
Chlorophyll contains magnesium as the central atom co-ordinated to a
porphine macrocycle.
The degree of unsaturation, the side groups and the phytyl chain are
all notable. Chlorophylla, together with many other light-harvesting
molecules( we call them chromophores) collect sunlight and convert it
to electrical energy, more-less the way solar cells function. The
electrons , reduce
CO2 to simple sugars :

n CO2 + nH2O
h (CH2O) n + O2 H=470kJ/Mole
Respiration

These simple sugars are converted to other sugars, starch and even
cellulose. As can be readily seen, without chlorophyll, photosynthesis
would not take place and , in all probability, life would not be possible
as we know it.

(a) The prosthetic group of a cytochrome

CH3 CH3 NH
CH3
C S CH2 Peptide chain
HOOCCH2CH2
C
O
N N
Fe H
N N
CH2
HOOCCH2CH2
H
CH3 C
H3C S NH
CH2
CH
C
O
 A sketch of VitaminB12
CONH2

H3C
H2NOC CH3 CONH2

H3C
X

CONH2
N N
H 3C
Co

N N

CH3
CH3
H2NOC
H3C
CH3

O
NH

CONH2

H3C
O
O P O
N CH3

O HO N CH3

HOH2 C

VitaminB12 (X=CN)
 1.(b) Chlorophylla

Functions of Chlorophyll.Chlorophyll is one of the pigments

in green vegetation. It traps sunlight and converts it to
electrical energy(compare the functioning of a solar cell).
The photosynthesis equation is as follows:-
n CO2 + nH2O
h (CH2O) n + O2 H=470kJ/Mole
Respiration

Note that the same amount of energy absorbed in the process

of reducing a Molecule of carbon dioxide, is actually
released when the sugar is oxidized during the process of
respiration.

2(b) Difference Betweeen Myoglobin and Hemoglobin.and

their Biological Roles.

The Prosthetic group shown in the diagram plus the

globin, which is peptide chain with 160-163 amino acids is
what constitutes myglobin.
Four myglobin units, when wrapped together by protein
molecules constitute Hemeglobin, ie Hemoglobin is a
tetramer.
When the blood is within the lungs, Hemoglobin
combines with oxygen, holding an oxygen molecule at the
position marked X , and transports it to the tissues. Within
the tissues, the oxygen is released and co-ordinated by
myoglobin. The oxygen is held in this position until it is
required , eg for respiration. Both water and oxygen are held
at the position labeled X, reversibly.

2(c). Poisoning by both CO and mercury. Carbon

monoxide is also co-ordinated by the heme group of
myoglobin and Hemoglobin. Unlike the case with water and
oxygen, a CO molecule is co-ordinated irreversibly. This
implies that once a CO molecule has been
co-rdinated by hemoglobin, no more oxygen can be
transported to the tissues. If the site in myoglobin is co-
ordinated, the molecule cannot store oxygen. This is the
poisoning mechanism. Mercury form large cations , Hg2+and
[Hg2]+. Either of these is a soft acid
which readily combines with sulphur in essential amino acids
such as methionine and cysteine , thus denaturing them.
Mercury also readily denatures vitamin B12 and combining
with methyl groups to form methyl mercury species,
[HgCH3]+

2(b) Difference Betweeen Myoglobin and Hemoglobin.and

their Biological Roles.

The Prosthetic group shown in the diagram plus the

globin, which is peptide chain with 160-163 amino acids is
what constitutes myglobin.
Four myglobin units, when wrapped together by protein
molecules constitute Hemeglobin, ie Hemoglobin is a
tetramer.
When the blood is within the lungs, Hemoglobin
combines with oxygen, holding an oxygen molecule at the
position marked X , and transports it to the tissues. Within
the tissues, the oxygen is released and co-ordinated by
myoglobin. The oxygen is held in this position until it is
required , eg for respiration. Both water and oxygen are held
at the position labeled X, reversibly.

2(c). Poisoning by both CO and mercury. Carbon

monoxide is also co-ordinated by the heme group of
myoglobin and Hemoglobin. Unlike the case with water and
oxygen, a CO molecule is co-ordinated irreversibly. This
implies that once a CO molecule has been
co-rdinated by hemoglobin, no more oxygen can be
transported to the tissues. If the site in myoglobin is co-
ordinated, the molecule cannot store oxygen. This is the
poisoning mechanism. Mercury form large cations , Hg2+and
[Hg2]+. Either of these is a soft acid
which readily combines with sulphur in essential amino acids
such as methionine and cysteine , thus denaturing them.
Mercury also readily denatures vitamin B12 and combining
with methyl groups to form methyl mercury species,
[HgCH3]+

EXERCISE

1. Draw the structure of a naturally-occurring co-

ordination complex explaining clearly its known
biolgical Role .
2. Why , in your view, is a study of co-ordination
chemistry relevant to biolological systems?