Methemoglobin

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Methemoglobin (British English: methaemoglobin) (pronounced "met-hemoglobin") is a form of the oxygen-carrying metalloprotein hemoglobin, in which the iron in the heme group is in the Fe3+ (ferric) state, not the Fe2+ (ferrous) of normal hemoglobin. Methemoglobin cannot release bound oxygen, unlike oxyhemoglobin. It is a bluish chocolate-brown in color. The NADH-dependent enzyme methemoglobin reductase (diaphorase I) is responsible for converting methemoglobin back to hemoglobin.

Normally one to two percent of people's hemoglobin is methemoglobin; a higher percentage than this can be genetic or caused by exposure to various chemicals and depending on the level can cause health problems known as methemoglobinemia. A higher level of methemoglobin will tend to cause a pulse oximeter to read closer to 85% regardless of the true level of oxygen saturation.[1]

Contents

[edit] Common causes

[edit] Therapeutic uses

Amyl nitrite is administered to treat cyanide poisoning. It works by converting hemoglobin to methemoglobin, which allows for the binding of cyanide and the formation of non-toxic cyanomethemoglobin.[2]

[edit] Methemoglobin saturation

Methemoglobin saturation is expressed as the percentage of hemoglobin in the methemoglobin state; That is MetHb as a proportion of Hb.

[edit] See also

[edit] References

  1. ^ Denshaw-Burke, Mary (2006-11-07). "Methemoglobinema". http://www.emedicine.com/med/TOPIC1466.HTM. Retrieved 2008-03-31. 
  2. ^ Vale, J. A. (2001). "Cyanide Antidotes: from Amyl Nitrite to Hydroxocobalamin - Which Antidote is Best?". Toxicology 168 (1): 37–38. 

[edit] External links

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