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The iron atom in the heme group must initially be in the ferrous ( Fe < sup > 2 +</ sup >) oxidation state to support oxygen and other gases ' binding and transport ( it temporarily switches to ferric during the time oxygen is bound, as explained above ).
Initial oxidation to the ferric ( Fe < sup > 3 +</ sup >) state without oxygen converts hemoglobin into " hemiglobin " or methemoglobin ( pronounced " MET-hemoglobin "), which cannot bind oxygen.
Hemoglobin in normal red blood cells is protected by a reduction system to keep this from happening.
Nitric oxide is capable of converting a small fraction of hemoglobin to methemoglobin in red blood cells.
The latter reaction is a remnant activity of the more ancient nitric oxide dioxygenase function of globins.

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