Journal
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 33, Issue -, Pages 1378-1381Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BST0331378
Keywords
antioxidant; disulphide; glutathione; glutathionylation; redox regulation; thiol
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Protein cysteines can undergo various forms of oxidation, some of them reversible (disulphide formation, glutathionylation and S-nitrosylation). While in the past these were viewed as protein damage in the context of oxidative stress, there is growing interest in oxidoreduction of protein thiols/disulphides as a regulatory mechanism. This review discusses the evolution of the concept of redox regulation from that of oxidative stress and the redox state of protein cysteines in different cellular compartments.
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