Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation.
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Woo HA, Chae HZ, Hwang SC, Yang KS, Kang SW, Kim K, Rhee SG
Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation.
Science. 2003 Apr 25;300(5619):653-6.
- PubMed ID
- 12714748 [ View in PubMed]
- 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.