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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / 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 Jacob / Iona Knight
  • Peninsula Medical School, Universities of Exeter and Plymouth, St. Luke's Campus, Magdalen Road, Exeter EX1 2LU, UK
  • Other articles by this author:
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/ Paul G. Winyard
  • Peninsula Medical School, Universities of Exeter and Plymouth, St. Luke's Campus, Magdalen Road, Exeter EX1 2LU, UK
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2006-11-02 | DOI: https://doi.org/10.1515/BC.2006.174


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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Published Online: 2006-11-02

Published in Print: 2006-10-01

Citation Information: Biological Chemistry, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2006.174.

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