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Heme

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heme: see coenzyme coenzyme , any one of a group of relatively small organic molecules required for the catalytic function of certain enzymes. A coenzyme may either be attached by covalent bonds to a particular enzyme or exist freely in solution, but in either case it participates
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heme [hēm]
(biochemistry)
C34H32O4N4Fe An iron-protoporphyrin complex associated with each polypeptide unit of hemoglobin.

Heme 

the nonprotein component (the so-called prosthetic group) and the coloring matter of hemoglobin.

Chemically, heme is a compound of protoporphyrin and divalent iron. In the vertebrate body heme is synthesized from simpler nitrogen compounds (glycine and succinate) and from ferritin, a reserve iron-protein complex present in the spleen, liver, and bone marrow. The heme isolated from the blood of various vertebrates always has the same structure:

Free heme readily oxidizes in air to hematin, in which the iron atom is trivalent. Many years of research on the structure of heme were rewarded by the synthesis in 1929 by H. Fischer of hemin, the hydrochloride of heme.



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Once outside the red blood cells, haemoglobin itself can release its heme groups, which leads to the severe symptoms of malaria and eventually to death.
If iron is lacking in the diet, then heme will not be formed and so also hemoglobin.
Other chapter topics are structure and function of [NiFe]-hydrogenases, carbon monoxide and cyanide ligands in the active site of [FeFe]-hydrogenases, the dual role of heme as cofactor and substrate in the biosynthesis of carbon monoxide, copper-carbon bonds in mechanistic and structural probing of proteins, and computational studies of bioorganometallic enzymes and cofactors.
 
 
 
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