Metalloporphyrins

Metalloporphyrins: The complexes between metal ions and porphyrin ligands are known as
metalloporphyrins. e.g. Haemoglobin (Hb) & Myoglobin (Mb)
NH HN
Fig 01 Structure of porphyrin ligand
Structure of Hemoglobin consists of Heme & Globin (polypeptide chain)

1) Heme is active sites of the both Hb & Mb.
2) In heme, Fe is in ferrous state i.e. +2 state (MCQ) and present in the center of the heme
structure.
3) Fe+2 binds equally to all four nitrogen atoms of porphyrin ring (i.e.heterocyclic ring)
4) Fe+2 & all four nitrogen atoms of porphyrin ring lie in one plane.
5) The fifth co-ordination site is occupied by ‘N’ atom of histidine linked to polypeptide chain
(called as globin)
6) O2 binds to this Fe(II) at the sixth coordination (vacant) position as shown
in fig.5.3
Fig. 02 Structure of heme group

2) Globin (polypeptide chain) :
The polypeptide chain (globin) in both Hb & Mb plays an important role in transport and store of
oxygen (O2) respectively. In the absence of the polypeptide chain, Fe (II) in heme group is
oxidized to Fe (III) irreversibly by O2 and thus it cannot function as oxygen carrier. Fe (II)-
Heme + O2 Fe (III)-Heme (Hematin). Thus, the polypeptide chain (globin) in both Hb & Mb
plays an important role in transport and store of oxygen (O2) respectively
STRUCTURE OF HEMOGLOBIN & MYOGLOBIN
Structural Similarities between Hb & Mb: Both contains Heme, polypeptide chain & Fe(II)
Fig. 03 Structure
of HbO2
 Hb is
tetrameric
heme
protein
with four
heme
units linked with four protein chains.
 Two protein chains are labeled as α made up of 141 amino acids.
 Two protein chains are labeled as β made up of 143 amino acids.
 Molecular weight of Hb is 64,500 daltons
 Mb is monomeric with single heme unit linked with single protein chain consisting of
153 amino acids.
 Molecular weight of Mb is 17,000.
Fig. 04 Structure of MbO2
Function of Hb and Mb in biological systems
1) Haemoglobin (Hb) binds and transports oxygen from the lungs to Myoglobin in tissues.
Explanation:
Hb 4O2 Hb (O2)4
Hb (O2)4 4Mb 4Mb (O2)

a) When Hb reaches the tissue, it becomes more tensed i.e. in T-form which is low-oxygen-
affinity form so O2 will be released.
b) While in lungs, Hb will be in relaxed form i.e. in R-form which is highoxygen- affinity
form so O2 will be able to be bound.
2) Transport of CO2: Hb transport CO2 to lungs as follow;
Hb (O2)4 2CO2 2H2O H2Hb+2 2HCO3- 4O2
Further this H2Hb2+ on oxygenation releases two protons (H+) whichreact with HCO3
dissolved in blood to set free CO2 in lungs.
H2Hb+2 4O2 Hb (O2)4 2H+
HCO3- H+ H2CO3 H2O CO2

3) Hb acts as a buffer: Hb constitutes one of the important buffer of the blood and helps to
maintain its acid –base balance.
Functions of Myoglobin (Mb):

1) Myoglobin is oxygen storage protein
2) Mb facilitates & enhances oxygen diffusion within the cell
3) The rate of O2 diffusion from capillaries to tissue is slow because of low the solubility of
oxygen.
4) Myoglobin increases the solubility of oxygen because Mb bind with O2 strongly than Hb
5) It binds O2 reversibly: O2 + Mb ⇋ MbO2 myoglobin oxymyoglobin
Structural changes taking place during oxygenation:
When an oxygen molecule is bound in the position opposite to this histidine,
the Fe(II) goes into a low spin state, eg orbitals are then empty and the radius of
the iron decreases (by 0.17A0) so much that it now fits in to the plane of the
porphyrin system as shown in fig
Cooperativity :
1) Cooperativity was proposed by M.F. Perutz
2) Definition of Cooperativity : Deoxy-hemoglobin (deoxy-Hb) has a relatively
low affinity for oxygen, but when one molecule binds to a single heme, the oxygen
affinity increases, allowing the second molecule to bind more easily, and the third
and fourth even more easily. This phenomenon of increasing oxygen affinity at
second, third and fourth sites in Hb is known as Cooperativity
3) Effect of Oxygen Binding by Oxygen Dissociation curve:
From % saturation Vs pO2 curve (called as oxygen dissociation
curve), it is clear thata)
Nature of curve: Curve for Hb is sigmoidal (S-shaped) whereas that of Mb is
hyperbolic.
b) Effect of binding with Hb: Hb binds O2 only at high partial pressure of oxygen
because it has less affinity towards oxygen.
Hb + O2 ⇋ HbO2 (At high partial pressure of oxygen)
c) Effect of binding with Mb: Mb binds O2 even at low partial pressure of
oxygen because it has more affinity towards oxygen.
Mb +O2 ⇋ MbO2 (At low partial pressure of oxygen)
d) Effect of binding in muscles & lungs:
i) When Hb reaches the cellular tissue (muscles), it becomes more tensed
i.e. in T-form which is low-oxygen-affinity form so O2 will be released.
ii) While in lungs, Hb will be in relaxed form i.e. in R-form which is highoxygen-
affinity form so O2 will be able to be bound.
e) Effect of binding w.r.t. pH: (called as Bohr effect)
i) The binding affinity of Hb with O2 decreases with decrease in the pH of
blood as shown in fig.
ii) In cellular tissue (muscles), oxygen is released to Mb more efficiently at

lower pH where CO2 concentration is high.
H2O + CO2 ⇋ H2CO3 ⇋ H+ + HCO3
-
iii) In lungs, pH is high (Alkaline), thus the affinity O2 binding with Hb is
high
f) Thus, phenomenon of Cooperativity promotes transfer of O2 from Hb
to Mb.
Fig. 05 Oxygen binding curves of Hb and Mb

Metalloporphyrins

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Metalloporphyrins: The complexes between metal ions and porphyrin ligands are known as

metalloporphyrins. e.g. Haemoglobin (Hb) & Myoglobin (Mb)

Fig 01 Structure of porphyrin ligand

Structure of Hemoglobin consists of Heme & Globin (polypeptide chain)

Fig. 02 Structure of heme group

STRUCTURE OF HEMOGLOBIN & MYOGLOBIN

Function of Hb and Mb in biological systems

Hb (O2)4 4Mb 4Mb (O2)

HCO3- H+ H2CO3 H2O CO2

Functions of Myoglobin (Mb):

ii) In cellular tissue (muscles), oxygen is released to Mb more efficiently at

Fig. 05 Oxygen binding curves of Hb and Mb

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