The mechanism of cytochrome C oxidase inhibition by nitric oxide
The mechanism of cytochrome C oxidase inhibition by nitric oxide
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DOI：
10.2741/2118
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发表时间：
2007-01-01
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影响因子：
--
通讯作者：
Cadenas, Enrique
中科院分区：
文献类型：
--
作者：
Antunes, Fernando;Cadenas, Enrique
本文综述了一氧化氮（NO）抑制细胞色素氧化酶的基本生物化学机制。将NO结合到完全还原的Fe - a3 - Cu - B位点、半还原的Fe - a3 - Cu - B位点以及完全氧化的Fe - a3 - Cu - B位点这三种可能的机制与实验数据进行了对比。运用数学模型来辅助分析并解决有关NO抑制细胞色素氧化酶的令人困惑的观察结果。结论是，NO对细胞色素氧化酶的抑制是混合性的，既有竞争性成分也有非竞争性成分，但在生理电子流情况下，竞争性成分占主导地位。简要讨论了这种抑制作用在生理和病理方面的相关性。
The basic biochemistry of the inhibition of cytochrome oxidase by NO is reviewed. Three possible mechanisms that include the binding of NO to the fully reduced Fe-a3-Cu-B site, to the semi-reduced Fe-a3-Cu-B site, and to the fully oxidized Fe-a3-Cu-B site are confronted with the experimental data. Mathematical models are used to facilitate the analysis and to solve puzzling observations concerning the NO inhibition of cytochrome oxidase. It is concluded that the inhibition of cytochrome oxidase by NO is mixed, having both competitive and uncompetitive components, but under physiological electron flows the competitive component is largely predominant. The physiological and pathological relevance of this inhibition is briefly discussed.