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Reactivity of Nitric Oxide with Cytochrome c Oxidase: Interactions with the Binuclear Centre and Mechanism of Inhibition

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Abstract

Nitric oxide (NO) has recently been recognized as an important biological mediator that inhibits respiration at cytochrome c oxidase (CcO). This inhibition is reversible and shows competition with oxygen, the K i being lower at low oxygen concentrations. Although the species that binds NO in turnover has been suggested to contain a partially reduced binuclear center, the exact mechanism of the inhibition is not clear. Recently, rapid (ms) redox reactions of NO with the binuclear center have been reported, e.g., the ejection of an electron to cytochrome a and the depletion of the intermediates P and F. These observations have been rationalized within a scheme in which NO reacts with oxidized CuB leading to the reduction of this metal center and formation of nitrite in a very fast reaction. Electron migration from CuB to other redox sites within the enzyme is proposed to explain the optical transitions observed. The relevance of these reactions to the inhibition of CcO and metabolism of NO are discussed.

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  1. Department of Biological Sciences, University of Essex, Wivenhoe Park, Central Campus, CO4 3SQ, Colchester, United Kingdom

    Jaume Torres, Chris E. Cooper, Martyn Sharpe & Michael T. Wilson

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  1. Jaume Torres
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  2. Chris E. Cooper
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  4. Michael T. Wilson
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Torres, J., Cooper, C.E., Sharpe, M. et al. Reactivity of Nitric Oxide with Cytochrome c Oxidase: Interactions with the Binuclear Centre and Mechanism of Inhibition. J Bioenerg Biomembr 30, 63–69 (1998). https://doi.org/10.1023/A:1020559528124

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