Abstract
Heme oxygenase [EC 1:14.99.3, heme, hydrogen donor: oxygen oxidoreductase, (α-methene hydroxylating, decyclizing)] catalyzes the rate-limiting step in the oxidative catabolism of heme. In a coupled reaction with NADPH: cytochrome p-450 reductase, HO generates equimolar carbon monoxide (CO), ferrous iron, and biliverdin IXα per heme oxidized. Cytosolic NAD(P)H: biliverdin reductase (BVR) [E.C. 1:3:1:24] subsequently converts biliverdin-IXα to bilirubin-IXα (Tenhunen et al., 1968; Tenhunen et al., 1969). In addition to HO-1, the inducible form, two genetically distinct isozymes exist (HO-2, and HO-3). Many mammalian tissues constitutively express HO-2 including the brain, testes, and vascular endothelium. HO-1 and HO-2 catalyze an identical reaction with different kinetic parameters, whereas HO-3 displays little enzymatic activity (Maines et al., 1986; McCoubrey et al., 1997). Taken together, HO enzymes serve an essential physiological function in regulating intracellular heme turnover (Maines, 1992).
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Ryter, S.W., Otterbein, L.E., Morse, D., Choi, A.M.K. (2002). Carbon Monoxide. In: Abraham, N.G. (eds) Heme Oxygenase in Biology and Medicine. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0741-3_2
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