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

Title
Sulfiredoxin, the cysteine sulfinic acid reductase specific to 2-Cys peroxiredoxin: Its discovery, mechanism of action, and biological significance
Authors
Rhee S.G.Jeong W.Chang T.-S.Woo H.A.
Ewha Authors
이서구정우진창동신우현애
SCOPUS Author ID
이서구scopusscopus; 정우진scopus; 창동신scopus; 우현애scopus
Issue Date
2007
Journal Title
Kidney International
ISSN
0085-2538JCR Link
Citation
vol. 72, no. SUPPL. 106, pp. S3 - S8
Indexed
SCI; SCIE; SCOPUS WOS scopus
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. © 2007 International Society of Nephrology.
DOI
10.1038/sj.ki.5002380
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일반대학원 > 생명·약학부 > Journal papers
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