Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation

Hyun Ae Woo, Ho Zoon Chae, Sung Chul Hwang, Kap Seok Yang, Sang Won Kang, Kanghwa Kim, Sue Goo Rhee

Research output: Contribution to journalArticlepeer-review

466 Scopus citations

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.

Original languageEnglish
Pages (from-to)653-656
Number of pages4
JournalScience
Volume300
Issue number5619
DOIs
StatePublished - 25 Apr 2003

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