heme

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heme:

see coenzymecoenzyme
, 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 intimately in
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.

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.

heme

[hēm]
(biochemistry)
C34H32O4N4Fe An iron-protoporphyrin complex associated with each polypeptide unit of hemoglobin.
References in periodicals archive ?
Charcoal dextran-stripped FBS (CD-FBS) was purchased from Biological Industries (Kibbutz Beit Haeme of Israel).
Studies with the haeme oxygenase inhibitor Sn-protoporphyrin in patients with primary biliary cirrhosis and idiopathic haemochromatosis.
53] suggested that a higher intake of haeme iron might be harmful, whereas a higher intake of zinc might be beneficial in relation to CVD mortality in the presence of a trigger that can disturb iron homeostasis, such as alcohol consumption.