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Protein sulfenic acids in redox signaling
Leslie B Poole1, P Andrew Karplus, Al Claiborne
1Department of Biochemistry, Wake Forest University School of Medicine, Winston-Salem, North Carolina 27157, USA. lbpoole@wfubmc.edu
Annual Review of Pharmacology and Toxicology
|January 28, 2004
Abstract:
Reactive (low pKa) cysteine residues in proteins are critical components in redox signaling. A particularly reactive and versatile reversibly oxidized form of cysteine, the sulfenic acid (Cys-SOH), has important roles as a catalytic center in enzymes and as a sensor of oxidative and nitrosative stress in enzymes and transcriptional regulators. Depending on environment, sometimes the sulfenic acid provides a metastable oxidized form, and other times it is a fleeting intermediate giving rise to more stable disulfide, sulfinic acid, or sulfenyl-amide forms.