Formation and Functions of Protein Sulfenic Acids

Leslie B. Poole1

1 Wake Forest University School of Medicine, Winston‐Salem, North Carolina
Publication Name:  Current Protocols in Toxicology
Unit Number:  Unit 17.1
DOI:  10.1002/0471140856.tx1701s18
Online Posting Date:  February, 2004
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Protein sulfenic acids are generated as reversibly oxidized cysteinyl residues formed upon reaction of thiols with peroxides, nitric oxide, peroxynitrite, and other reactive oxygen or nitrogen species. They can be stabilized within the protein environment, irreversibly oxidized to sulfinic and sulfonic acids by additional oxidant, condensed with protein or exogenous thiol groups to form disulfide bonds, or directly reduced back to thiols. Sulfenic acids in proteins can act as intermediates in redox catalysis or as critical components in cysteine‚Äźdependent redox regulation.

Keywords: sulfenic acids; cysteine modification; cysteine oxidation; redox regulation; redox catalysis

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Table of Contents

  • Formation, Reactivity, and Detection of Cysteine Sulfenic Acids in Proteins
  • Functions of Protein Sulfenic Acids
  • Summary
  • Literature Cited
  • Figures
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Key References
   Claiborne, A., Yeh, J.I., Mallett, T.C., Luba, J., Crane, E.J., 3rd, Charrier, V., and Parsonage, D. 1999. Protein‐sulfenic acids: Diverse roles for an unlikely player in enzyme catalysis and redox regulation. Biochemistry 38:15407‐15416.
  Review of the role of sulfenic acids in proteins.
   Poole and Ellis, 2002. See above.
  Gives practical details about the use of several protocols, including NBD chloride, TNB, and dimedone‐based methods, for identification of sulfenic acids.
   Poole et al., 2004 See above.
  Review of the role of protein sulfenic acids in redox signaling.
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