20 221

Cited 419 times in

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, 300(5619):653-656, 2003
Journal Title
Science
ISSN
0193-4511
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 terms
AnimalsCatalysisCell LineCycloheximide/pharmacologyCysteine/analogs & derivatives*Cysteine/metabolism*DimerizationHela CellsHumansHydrogen Peroxide/metabolism*Methionine/metabolismMiceNeurotransmitter AgentsOxidation-ReductionPeroxidases/chemistryPeroxidases/metabolism*PeroxiredoxinsProtein Synthesis Inhibitors/pharmacologySpectrometry, Mass, Electrospray IonizationSulfhydryl Compounds/metabolismSulfinic Acids/metabolismTumor Cells, Cultured
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
Full Text Link
Export
RIS (EndNote)
XLS (Excel)
XML

qrcode

해당 아이템을 이메일로 공유하기 원하시면 인증을 거치시기 바랍니다.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse