Disulphide formation on mitochondrial protein thiols

被引：57

作者：

Hurd, TR ^{[1
]}

Filipovska, A ^{[1
]}

Costa, NJ ^{[1
]}

Dahm, CC ^{[1
]}

Murphy, MP ^{[1
]}

机构：

[1] MRC, Dunn Human Nutr Unit, Cambridge CB2 2XY, England

来源：

BIOCHEMICAL SOCIETY TRANSACTIONS | 2005年 / 33卷

关键词：

disulphide; glutathione; mitochondrion; oxidative stress; protein thiol; reactive oxygen species;

D O I：

10.1042/BST0331390

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：

A large number of proteins contain free thiols that can be modified by the formation of internal disulphicles or by mixed disulphides with low-molecular-mass thiols. The majority of these latter modifications result from the interaction of protein thiols with the endogenous glutathione pool. Protein glutathionylation and disulphide formation are of significance both for defence against oxidative damage and in redox signalling. As mitochondria are central to both oxidative damage and redox signalling within the cell, these modifications of mitochondrial proteins are of particular importance. In the present study, we review the mechanisms and physiological significance of these processes.

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收藏

页码：1390 / 1393

页数：4

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