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Heme oxygenase or haem oxygenase (HO) is an enzyme that catalyzes the degradation of heme. This produces biliverdin, iron, and carbon monoxide.〔Ryter, Stefan W.; Alam, Jawed; Choi, Augustine M. K. "Heme oxygenase-1/carbon monoxide: from basic science to therapeutic applications" Physiological Reviews (2006), 86(2), 583-650. 〕 ==Reaction== Heme oxygenase cleaves the heme ring at the alpha-methene bridge to form either biliverdin or, if the heme is still attached to a globin, verdoglobin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. The reaction occurs as follows: :: This reaction can occur in virtually every cell; the classic example is the formation of a bruise, which goes through different colors as it gradually heals: red heme to green biliverdin to yellow bilirubin. Under normal physiological conditions, the activity of heme oxygenase is highest in the spleen, where old erythrocytes are sequestrated and destroyed. In terms of molecular mechanisms, the enzyme facilitates the intramolecular hydroxylation of one meso carbon centre in the heme. 〔Tadashi Yoshida, Catharina Taiko Migita "Focused Review Mechanism of heme degradation by heme oxygenase" Journal of Inorganic Biochemistry 2000, Volume 82, Issues 1–4, pages 33–41. 〕 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「Heme oxygenase」の詳細全文を読む スポンサード リンク
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