Aspects of the biological redox chemistry of cysteine: from simple redox responses to sophisticated signalling pathways.
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.
Jacob
Claus
C
School of Pharmacy, Saarland University, P.O. Box 151150, D-66041 Saarbrücken, Germany. c.jacob@mx.uni-saarland.de
Knight
Iona
I
Winyard
Paul G
PG
D000818:Animals; D003545:Cysteine / Q000737:chemistry* / Q000378:metabolism*; D004789:Enzyme Activation; D006801:Humans; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D009195:Peroxidase / Q000378:metabolism; D015398:Signal Transduction
D009195:Peroxidase; D003545:Cysteine