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Biochem Soc Trans. 2005 Dec;33(Pt 6):1390-3.

Disulphide formation on mitochondrial protein thiols.

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Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge CB2 2XY, UK.


A large number of proteins contain free thiols that can be modified by the formation of internal disulphides 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.

[Indexed for MEDLINE]

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