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  Haemoglobin

Haemoglobin:

Haemoglobin in the red blood cells takes oxygen from the lungs to the tissues. It distributes the oxygen molecule to myoglobin in the tissues. Whenever the oxygen has been liberated for cell respiration, haemoglobin drops its bright red color and becomes purple. It then joins with the waste carbon dioxide generated by the cells and deposits in the lungs and hence the gas can be exhaled.

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Nature of haemoglobin and myoglobin:

Both are having similar structure apart from the fact that myoglobin is a monomer and haemoglobin is a tetramer. Both are iron-porphyrin complex.

These are bio-coordination complexes formed among porphyrin and iron in its +2 oxidation state (Fe2+). The iron-porphyrin complex is termed as the heme group that is a part of haemoglobin. Each haemoglobin molecule comprises of four subunits, every unit is being a folded chain.

The working portion of haemoglobin is a heme group having a Fe2+ cation coordinated to four nitrogen atoms of porphyrin group and one nitrogen atom of histidine group. The sixth octahedral site is obtainable to bind oxygen molecule.

 

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