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HAEMOGLOBIN

S No
1

Introduction

Structure of Molecule
- A terameric conjugated chromoprotein having
heterogeneous quaternary structure

- Consist of Haem (4) and Globin (4) molecules

A respiratory pigment of animal blood; meant for transporting O2 (oxyhaemoglobin) and CO2 (carbomaenohaemoglobin) as
respective loose complexes; forms irreversible permanent complex (carboxyhaemoglobin) with CO, effecting its O2
transportation capacity
Its empirical formula is C3032H9816O872N780S8Fe4
Its molecular structure was given by Kendrew & Perutz(), based on X-ray diffraction studies
Size 64 X 55 X 50

Haem Molecules
-

4 in number
Non-protein prosthetic groups
Each consists of 4 Pyrolle rings
with 1 central Iron atom
Each Haem can attach to 1
molecule of O2; therefore, all
together can transport 4O2
molecules

Pyrolle Rings
-

Iron Atoms
-

Globin Molecules
-

Functions

4 in number; which are folded


upon one another
There are 2 & 2 Polypeptide
chains
A few contact points between 2
and 2 chains
There are several contact points
between and chains to
comprise pairs 11 & 22
Attach to CO2 for its transport

4 in number (I - IV)
Empirical formula is C20H14N4
N containing heterocyclic rings with specific side chains
CH3 (at positions 1,3,5 & 8)
CHCH2(at positions 2 & 4)
(CH2)2COOH ((at positions 6 & 7)
Pyrolle rings linked by methine(-CH=; methylene) bridges (at positions , , & )
2+

One atom in Ferrous (Fe ) state at center surrounded by 4 Pyrolle rings


Attached to N atoms of 4 Pyrolle rings by 2 covalent & 2 coordinate bonds
Attached to histidine residues of polypeptide chains
Each can attach to 1 molecule of O2

Polypeptide Chains
-

2 in number
Each consists of 141 Amino acids with valine at N-terminus and arginine at Cterminus
th
Haem pocket formed by histidine at 87 position
th
Binding site for Fe of Haem at 58 position histidine

Polypeptide Chains
-

2 in number
Each consists of 146 Amino acids with valine at N-terminus and histidine at Cterminus
nd
- Haem pocket formed by histidine at 92 position
rd
- Binding site for Fe of Haem at 63 position histidine
Transport O2 from respiratory surface to various tissues as a loose complex oxyhaemoglobin (Hb 4O8; Hb (O2)4); In mammals,
97% of O2 is transported in this form; O2 is attached to Haem part of Hb
Transport of CO2 from tissues to respiratory surface as a loose complex carbomaenohaemoglobin (HbNHCOOH). In
mammals, accounts for 23% of CO2 transported in the blood. CO2 is attached to Globin part of Hb.
+
Serves as an Acid-base buffer, as the constituent amino acids of the Globin either due to negative charge (which binds to H
+
ions) or ionization (e.g., Histidine produce H ions to neutralize alkalinity)