hemoglobin oxidation stops oxygen transport

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Hemoglobin oxidation stops oxygen transport.

http://en.wikipedia.org/wiki/Hemoglobin :

"The iron atom in the heme group must be in the ferrous (Fe2+) oxidation state to support oxygen and other gases' binding and transport. Oxidation to the ferric (Fe3+) state converts hemoglobin into hemiglobin or methaemoglobin (pronounced "MET-hemoglobin"), which cannot bind oxygen. Hemoglobin in normal red blood cells is protected by a reduction system to keep this from happening. ...

The iron ion may either be in the Fe2+ or Fe3+ state, but ferrihemoglobin (methemoglobin) (Fe3+) cannot bind oxygen.[6] In binding, oxygen temporarily oxidizes Fe to (Fe3+), so iron must exist in the +2 oxidation state in order to bind oxygen. The enzyme methemoglobin reductase reactivates hemoglobin found in the inactive (Fe3+) state by reducing the iron center."

I'm thinking that we are getting close to producing a tentative

summary of the good and bad points of MMS. When taking

lots of MMS the above needs to be considered.

Mo