Nitroxyl (NO-):: a substrate for superoxide dismutase

被引:54
作者
Liochev, SI [1 ]
Fridovich, I [1 ]
机构
[1] Duke Univ, Med Ctr, Dept Biochem, Durham, NC 27710 USA
基金
美国国家卫生研究院;
关键词
D O I
10.1016/S0003-9861(02)00074-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 O-2 NO- acts as a reductant of ferricytochrome c anaerobically, but in the presence ofO(2), causes the oxidation of ferrocytochrome c and NADPH. Equivalent fluxes of NO-, and NO + O-2(-), were able to comparably oxidize NADPH, but the oxidation by NO + 02 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 O-2(-). Plausible mechanisms for those observations are offered and rate constants are estimated. (C) 2002 Elsevier Science (USA). All rights reserved.
引用
收藏
页码:166 / 171
页数:6
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