Nitric oxide ejects electrons from the binuclear centre of cytochrome c oxidase by reacting with oxidised copper: a general mechanism for the interaction of copper proteins with nitric oxide?
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作者:
Cooper, CE
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机构:Department of Biological Sciences, University of Essex, Central Campus, Colchester CO4 3SQ, Wivenhoe Park
Cooper, CE
Torres, J
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机构:Department of Biological Sciences, University of Essex, Central Campus, Colchester CO4 3SQ, Wivenhoe Park
Torres, J
Sharpe, MA
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机构:Department of Biological Sciences, University of Essex, Central Campus, Colchester CO4 3SQ, Wivenhoe Park
Sharpe, MA
Wilson, MT
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机构:Department of Biological Sciences, University of Essex, Central Campus, Colchester CO4 3SQ, Wivenhoe Park
Wilson, MT
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[1] Department of Biological Sciences, University of Essex, Central Campus, Colchester CO4 3SQ, Wivenhoe Park
Small increases in NO concentration can inhibit mitochondrial oxygen consumption by reacting at the binuclear haem a(3)/Cu-B oxygen reduction site of cytochrome c oxidase, Here we demonstrate that under normal turnover conditions NO reacts initially with the oxidised CUB rather than the haem a(3). We propose that hydration of an initial Cu+/NO+ complex forms nitrite, a proton and CUB+; the latter ejects an electron from the binuclear centre and results in the observed (100 s(-1)) reduction of other electron transfer centres in the enzyme (haem a and CUA) These reactions may have implications for the interactions of NO with other copper proteins. (C) 1997 Federation of European Biochemical Societies.