Archives of biochemistry and biophysics · 2002
Nitroxyl (NO-): a substrate for superoxide dismutase.
СтатьяПоддержка исследования: вне правительства СШАПоддержка службы здравоохранения СШАНазвание и аннотация: Перевод в очереди
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Liochev Stefan I, Fridovich Irwin
Аннотация
The interactions of Cu, Zn superoxide dismutase (SOD) with nitroxyl (NO-) and nitric oxide (NO), both of which are thought to be biologically significant, have been studied but remain undefined. Having previously noted that NO- can reduce Cu (II), Zn SOD aerobically, we now report that it also can do so anaerobically and that Cu, Zn SOD can catalyze the elimination of NO(-) in the absence of O2.NO- acts as a reductant of ferricytochrome c anaerobically, but in the presence of O2 causes the oxidation of ferrocytochrome c and NADPH. Equivalent fluxes of NO-, and NO + O2- were able to comparably oxidize NADPH, but the oxidation by NO + O2- was more than fivefold more sensitive to inhibition by Cu, Zn SOD than was the oxidation by NO-. Thus Cu, Zn SOD inhibited NADPH oxidation by NO- by a route independent of catalyzing the dismutation of O2. Plausible mechanisms for those observations are offered and rate constants are estimated.