Disulphide formation on mitochondrial protein thiols

• DOI: 10.1042/bst20051390
• Publication Date: 2005-10-27T04:32:02Z
• Authors: A. Filipovska; T.R. Hurd; N.J. Costa; C.C. Dahm; M.P. Murphy
• Keywords: 0303 health sciences; Glutathione; Mitochondria; 03 medical and health sciences; Thioredoxins; Peroxynitrous Acid; Disulfides; Sulfhydryl Compounds; Oxidoreductases; Reactive Oxygen Species; Oxidation-Reduction; Glutaredoxins; Signal Transduction

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.