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Why would the myoglobin have to use covalently bound heme and ferrous ion in order for...

Why would the myoglobin have to use covalently bound heme and ferrous ion in order for the oxygen storage? What would happen if free ferrous ion meets with oxygen? What would happen if free heme (bound to ferrous ion) meets with oxygen?

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Answer #1

Ans . A heme group is bound in a hydrophobic cleft in the protein, and is key to function of myoglobin : it is to the heme that oxygen binds. The heme itself consists of an organic ring known as protoporphyrin that surrounds an iron atom.

When the iron achieves an oxidation state of +2 (ferrous state) ,' Fe ' can bind to an oxygen molecule and forms an oxymyoglobin.

Myoglobin is a single-chain globular protein with the heme prosthetic group in the center. Myoglobin binds oxygen with its heme group like hemoglobin.

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