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Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation.

Authors
Woo, HA | Chae, HZ | Hwang, SC  | Yang, KS | Kang, SW | Kim, K | Rhee, SG
Citation
Science (New York, N.Y.), 300(5619). : 653-656, 2003
Journal Title
Science (New York, N.Y.)
ISSN
0036-80751095-9203
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.
MeSH

DOI
10.1126/science.1080273
PMID
12714748
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Medical Science
Ajou Authors
황, 성철
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