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Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation

Title
Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation
Authors
Woo H.A.Chae H.Z.Hwang S.C.Yang K.-S.Kang S.W.Kim K.Rhee S.G.
Ewha Authors
이서구강상원우현애
SCOPUS Author ID
이서구scopusscopus; 강상원scopus; 우현애scopus
Issue Date
2003
Journal Title
Science
ISSN
0036-8075JCR Link
Citation
vol. 300, no. 5619, pp. 653 - 656
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
The active-site cysteine of peroxiredoxins is selectively oxidized to cysteine sulfinic acid during catalysis, which leads to inactivation of peroxidase activity. This oxidation was thought to be irreversible. However, by metabolic labeling of mammalian cells with 35S, we show that the sulfinic form of peroxiredoxin I, produced during the exposure of cells to H2O2, is rapidly reduced to the catalytically active thiol form. The mammalian cells' ability to reduce protein sulfinic acid might serve as a mechanism to repair oxidatively damaged proteins or represent a new type of cyclic modification by which the function of various proteins is regulated.
DOI
10.1126/science.1080273
Appears in Collections:
일반대학원 > 생명·약학부 > Journal papers
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