The mechanism of cytochrome C oxidase inhibition by nitric oxide

被引：17

作者：

Antunes, Fernando

Cadenas, Enrique

机构：

[1] Inst Invest Cient Bento Rocha Cabral, P-125004 Lisbon, Portugal

[2] Ctr Quim & Bioquim, Grp Bioquim Oxidantes & Antioxidantes, P-125004 Lisbon, Portugal

[3] CBS, Lisbon, Portugal

[4] Univ So Calif, Sch Pharm, Dept Mol Pharmacol & Toxicol, Los Angeles, CA 90033 USA

来源：

FRONTIERS IN BIOSCIENCE | 2007年 / 12卷

关键词：

mitochondria; respiration; competitive inhibition; uncompetitive inhibition; mathematical model; cytochrome C oxidase; deficiency; diseases; excess; capacity; cytochrome C; oxidase; review;

D O I：

10.2741/2118

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

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.

引用

页码：975 / 985

页数：11

共 54 条

[1]

On the mechanism and biology of cytochrome oxidase inhibition by nitric oxide [J].