Why is Fe3+ unable to carry oxygen in methemoglobinanemia?

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SUMMARY

Methemoglobinanemia occurs when the iron atom in the heme group of hemoglobin is oxidized to the +3 state, rendering it incapable of carrying oxygen. The ferric ion (Fe3+) cannot bind to O2 due to its electronic configuration, which changes upon oxidation. This oxidation transforms the heme group into a stronger Lewis acid, preventing reversible bonding with O2 and leading to the formation of an oxidized species. Understanding these molecular changes is crucial for comprehending the condition's impact on oxygen transport.

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gravenewworld
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Methemoglobinanemia is when the iron atom in the heme group of hemoglobin is oxidized to the +3 state. In this oxidation state, the heme group is unable to carry oxygen. Why is this? A ton of the sources I have come across explain the condition of methemoglobinanemia and simply say that the ferric ion can't carry O2, but don't explain why the ferric ion can not carry O2. I want to understand this on a molecular level. I already have an understanding of how the iron binds to O2 in the +2 oxidation state from the papers that Pauling has written. Can anyone please explain why O2 can not bind to the heme group when the iron atom is oxidized to the +3 state?
 
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No idea, but I suppose you should look at the changes in electronic configuration of Fe - whatever is able to keep the oxygen, disappears when iron is oxidized.

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It is likely that the much stronger lewis acid cannot reversibly bond to O2 but rather, reacts with it. All 8 positions of the octahedral complex are blocked. It is likely that the oxygen carried by the Fe+2 normal heme group reacts with oxygen to form the Fe+3 oxidized species.
 

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