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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred


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Aspects of the biological redox chemistry of cysteine: from simple redox responses to sophisticated signalling pathways

Claus Jacob1 / Iona Knight2 / Paul G. Winyard3

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Corresponding author

Citation Information: Biological Chemistry. Volume 387, Issue 10/11, Pages 1385–1397, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2006.174, November 2006

Publication History

Published Online:
2006-11-02

Abstract

The last decade has witnessed an increased interest in cysteine modifications such as sulfenic and sulfinic acids, thiyl radicals, sulfenyl-amides and thiosulfinates, which come together to enable redox sensing, activation, catalysis, switching and cellular signalling. While glutathionylation, sulfenyl-amide formation and disulfide activation are examples of relatively simple redox responses, the sulfinic acid switch in peroxiredoxin enzymes is part of a complex signalling system that involves sulfenic and sulfinic acids and interacts with kinases and sulfiredoxin. Although the in vivo evaluation of sulfur species is still complicated by a lack of appropriate analytical techniques, research into biological sulfur species has gained considerable momentum and promises further excitement in the future.

Keywords: oxidative stress; peroxiredoxin; sulfenic acid; sulfenyl amide; sulfinic acid; thiosulfinate

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