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J Biol Chem. 2012 Feb 10;287(7):4403-10. doi: 10.1074/jbc.R111.283432. Epub 2011 Dec 6.

Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides.

Author information

1
Division of Life and Pharmaceutical Sciences, Ewha Womans University,Seoul 120-750, Korea. rheesg@ewha.ac.kr

Abstract

Peroxiredoxins (Prxs) contain an active site cysteine that is sensitive to oxidation by H(2)O(2). Mammalian cells express six Prx isoforms that are localized to various cellular compartments. The oxidized active site cysteine of Prx can be reduced by a cellular thiol, thus enabling Prx to function as a locally constrained peroxidase. Regulation of Prx via phosphorylation in response to extracellular signals allows the local accumulation of H(2)O(2) and thereby enables its messenger function. The fact that the oxidation state of the active site cysteine of Prx can be transferred to other proteins that are less intrinsically susceptible to H(2)O(2) also allows Prx to function as an H(2)O(2) sensor.

PMID:
22147704
PMCID:
PMC3281607
DOI:
10.1074/jbc.R111.283432
[Indexed for MEDLINE]
Free PMC Article

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