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

doi:10.1126/science.1080273

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 journal › Article › peer-review

489 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 language	English
Pages (from-to)	653-656
Number of pages	4
Journal	Science
Volume	300
Issue number	5619
DOIs	https://doi.org/10.1126/science.1080273
State	Published - 25 Apr 2003

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title = "Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation",

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.",

author = "Woo, {Hyun Ae} and Chae, {Ho Zoon} and Hwang, {Sung Chul} and Yang, {Kap Seok} and Kang, {Sang Won} and Kanghwa Kim and Rhee, {Sue Goo}",

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AU - Woo, Hyun Ae

AU - Chae, Ho Zoon

AU - Hwang, Sung Chul

AU - Yang, Kap Seok

AU - Kang, Sang Won

AU - Kim, Kanghwa

AU - Rhee, Sue Goo

PY - 2003/4/25

Y1 - 2003/4/25

N2 - 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.

AB - 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.

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VL - 300

SP - 653

EP - 656

JO - Science

JF - Science

IS - 5619

ER -

Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation

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