In:
Science, American Association for the Advancement of Science (AAAS), Vol. 300, No. 5619 ( 2003-04-25), p. 653-656
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 35 S, we show that the sulfinic form of peroxiredoxin I, produced during the exposure of cells to H 2 O 2 , 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.
Type of Medium:
Online Resource
ISSN:
0036-8075
,
1095-9203
DOI:
10.1126/science.1080273
Language:
English
Publisher:
American Association for the Advancement of Science (AAAS)
Publication Date:
2003
detail.hit.zdb_id:
128410-1
detail.hit.zdb_id:
2066996-3
detail.hit.zdb_id:
2060783-0
SSG:
11
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