Nitric oxide and the respiratory enzyme

被引：63

作者：

Brunori, Maurizio

Forte, Elena

Arese, Marzia

Mastronicola, Daniela

Giuffre, Alessandro

Sarti, Paolo

机构：

[1] Univ Roma La Sapienza, Dept Biochem Sci, I-00185 Rome, Italy

[2] Univ Roma La Sapienza, CNR, Inst Mol Biol & Pathol, I-00185 Rome, Italy

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 2006年 / 1757卷 / 9-10期

关键词：

mitochondrial physiology; reaction mechanism; free radical; cytochrome c oxidase; electron transfer; inhibition of respiration;

D O I：

10.1016/j.bbabio.2006.05.011

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：

Available information on the molecular mechanisms by which nitric oxide (NO) controls the activity of the respiratory enzyme (cytochrome-c-oxidase) is reviewed. We report that, depending on absolute electron flux, NO at physiological concentrations reversibly inhibits cytochrome-c-oxidase by two alternative reaction pathways, yielding either a nitrosyl- or a nitrite-heme a(3) derivative. We address a number of hypotheses, envisaging physiological and/or pathological effects of the reactions between NO and cytochrome-c-oxidase. (c) 2006 Elsevier B.V. All rights reserved.

引用

收藏

页码：1144 / 1154

页数：11

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