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Why distal histidine cannot be replaced by glutamic acid in a hemoglobin, how this affects molecule?

Why distal histidine cannot be replaced by glutamic acid in a hemoglobin, how this affects molecule?

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Answer #1

The distal histidine stabilises the oxygen ligand in oxy-Hb through formation of a hydrogen bond from the imidazole ring.

The distal histidine also acts as a gate for the ligand entry in alpha and beta subunits of hemoglobin.

It positions the oxygen atom between the nitrogen atom and the iron atom of the same imidazole ring , hence stabilizing it.

Hestidine which is responsible for stabilization of oxygen in E7 (seventh residue of E helix) is far from heme iron so named as distal.

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