Methemoglobin

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The structure of the enzyme that converts methemoglobin to hemoglobin[1]

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 bind oxygen, unlike oxyhemoglobin.[2] It is bluish chocolate-brown in color. In human blood a trace amount of methemoglobin is normally produced spontaneously. But when it is present in excess the blood becomes abnormally dark bluish brown. The NADH-dependent enzyme methemoglobin reductase (diaphorase I) is responsible for converting methemoglobin back to hemoglobin.

Normally one to two percent of a person'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.[3]

Common causes of elevated methemoglobin[edit]

Therapeutic uses[edit]

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.[7]

Methemoglobin saturation[edit]

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

Blood stains[edit]

Increased levels of methemoglobin are found in blood stains. Upon exiting the body, bloodstains transit from bright red to dark brown, which is attributed to oxidation of oxy-hemoglobin (HbO2) to methemoglobin (met-Hb) and hemichrome (HC).[8]

See also[edit]

References[edit]

  1. ^ Bando, S.; Takano, T.; Yubisui, T.; Shirabe, K.; Takeshita, M.; Nakagawa, A. (2004). "Structure of human erythrocyte NADH-cytochromeb5reductase". Acta Crystallographica Section D Biological Crystallography 60 (11): 1929–1934. doi:10.1107/S0907444904020645. PMID 15502298.  edit
  2. ^ http://www.rtso.ca/methemoglobin-causes-effects/
  3. ^ Denshaw-Burke, Mary (2006-11-07). "Methemoglobinema". Retrieved 2008-03-31. 
  4. ^ Manassaram, D. M.; Backer, L. C.; Messing, R.; Fleming, L. E.; Luke, B.; Monteilh, C. P. (2010). "Nitrates in drinking water and methemoglobin levels in pregnancy: A longitudinal study". Environmental Health 9: 60. doi:10.1186/1476-069X-9-60. PMC 2967503. PMID 20946657.  edit
  5. ^ http://www.fda.gov/Drugs/DrugSafety/ucm250024.htm
  6. ^ http://abcnews.go.com/Health/blue-skinned-people-kentucky-reveal-todays-genetic-lesson/story?id=15759819#.T2oS0HqV2So
  7. ^ Vale, J. A. (2001). "Cyanide Antidotes: from Amyl Nitrite to Hydroxocobalamin - Which Antidote is Best?". Toxicology 168 (1): 37–38. 
  8. ^ Bremmer et al PloS One 2011 http://www.plosone.org/article/info:doi/10.1371/journal.pone.0021845

External links[edit]