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

Sue Goo Rhee, Hyun Ae Woo, In Sup Kil, Soo Han Bae

Research output: Contribution to journalShort surveypeer-review

396 Scopus citations

Abstract

Peroxiredoxins (Prxs) contain an active site cysteine that is sensitive to oxidation by H 2O 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 2O 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 2O 2 also allows Prx to function as an H 2O 2 sensor.

Original languageEnglish
Pages (from-to)4403-4410
Number of pages8
JournalJournal of Biological Chemistry
Volume287
Issue number7
DOIs
StatePublished - 10 Feb 2012

Fingerprint

Dive into the research topics of 'Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides'. Together they form a unique fingerprint.

Cite this