Sulfiredoxin, the cysteine sulfinic acid reductase specific to 2-Cys peroxiredoxin: Its discovery, mechanism of action, and biological significance

S. G. Rhee, W. Jeong, T. S. Chang, H. A. Woo

Research output: Contribution to journalArticlepeer-review

123 Scopus citations

Abstract

Peroxiredoxin (Prx) is a family of bifunctional proteins that exhibit peroxidase and chaperone activities. Prx proteins contain a conserved Cys residue that undergoes a redox change between thiol and disulfide states. 2-Cys Prx enzymes, a subgroup of Prx family, are intrinsically susceptible to reversible hyperoxidation to cysteine sulfinic acid during catalysis. Cysteine hyperoxidation of Prx was shown to result in loss of peroxidase activity and a concomitant gain of chaperone activity. Reduction of sulfinic Prx enzymes, the first known biological example of such a reaction, is catalyzed by sulfiredoxin (Srx) in the presence of ATP. Srx appears to exist solely to support the reversible sulfinic modification of 2-Cys Prx enzymes. Srx specifically binds to 2-Cys Prx enzymes by recognizing several critical surface-exposed residues of the Prxs, and transfer the γ-phosphate of ATP to their sulfinic moiety, using its conserved cysteine as the phosphate carrier. The resulting sulfinic phosphoryl ester is reduced to cysteine after oxidation of four thiol equivalents.

Original languageEnglish
Pages (from-to)S3-S8
JournalKidney International
Volume72
Issue numberSUPPL. 106
DOIs
StatePublished - Aug 2007

Keywords

  • Chaperone
  • Cysteine sulfinic acid reductase
  • Hydrogen peroxide
  • Peroxiredoxin
  • Sulfinylation
  • Sulfiredoxin

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