Disulphide formation on mitochondrial protein thiols.

TitleDisulphide formation on mitochondrial protein thiols.
Publication TypeJournal Article
Year of Publication2005
AuthorsHurd, TR, Filipovska, A, Costa, NJ, Dahm, CC, Murphy, MP
JournalBiochem Soc Trans
IssuePt 6
Date Published2005 Dec
KeywordsDisulfides, Glutaredoxins, Glutathione, Mitochondria, Oxidation-Reduction, Oxidoreductases, Peroxynitrous Acid, Reactive Oxygen Species, Signal Transduction, Sulfhydryl Compounds, Thioredoxins

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.

Alternate JournalBiochem. Soc. Trans.
Citation Key10.1042/BST20051390
PubMed ID16246126