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Science 25 April 2003:
Vol. 300. no. 5619, pp. 653 - 656
DOI: 10.1126/science.1080273
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Reports

Reversing the Inactivation of Peroxiredoxins Caused by Cysteine Sulfinic Acid Formation

Hyun Ae Woo,1* Ho Zoon Chae,2*{dagger} Sung Chul Hwang,2{ddagger} Kap-Seok Yang,1 Sang Won Kang,1 Kanghwa Kim ,2§ Sue Goo Rhee2||

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.

1 Center for Cell Signaling Research and Division of Molecular Life Sciences, Ewha Womans University, Seoul 120-750, Korea.
2 Laboratory of Cell Signaling, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.



{dagger} Present address: Department of Biological Sciences, College of Natural Sciences, Chonnam National University, Kwangju 500-757, Korea.

{ddagger} Present address: Department of Pulmonary and Critical Care Medicine, Ajou University School of Medicine, Suwon 442-749, Korea.

§ Present address: Department of Food and Nutrition, College of Home Economics, Chonnam National University, Kwangju 500-757, Korea.

* These authors contributed equally to this work.

|| To whom correspondence should be addressed. E-mail: sgrhee{at}nih.gov

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