Cited by 463Redox biology and oxidative stressNeutrophil, Myeloperoxidase and Oxidative MechanismsSelenium in Biological Systems

Multiple Functions of Peroxiredoxins: Peroxidases, Sensors and Regulators of the Intracellular Messenger H 2 O 2 , and Protein Chaperones

Rhee, Sue Goo, Woo, Hyun Ae·2011·Antioxidants & Redox Signaling

Abstract

Peroxiredoxins (Prxs) are a family of peroxidases that reduce peroxides, with a conserved cysteine residue (the peroxidatic Cys) serving as the site of oxidation by peroxides. Peroxides oxidize the peroxidatic Cys-SH to Cys-SOH, which then reacts with another cysteine residue (typically the resolving Cys [C(R)]) to form a disulfide that is subsequently reduced by an appropriate electron donor. On the basis of the location or absence of the C(R), Prxs are classified into 2-Cys, atypical 2-Cys, and 1-Cys Prx subfamilies. In addition to their peroxidase activity, members of the 2-Cys Prx subfamily appear to serve as peroxide sensors for other proteins and as molecular chaperones. During catalysis, the peroxidatic Cys-SOH of 2-Cys Prxs is occasionally further oxidized to Cys-SO(2)H before disulfide formation, resulting in inactivation of peroxidase activity. This hyperoxidation, which is reversed by the ATP-dependent enzyme sulfiredoxin, modulates the sensor and chaperone functions of 2-Cys Prxs. The peroxidase activity of 2-Cys Prxs is extensively regulated via tyrosine and threonine phosphorylation, which allows modulation of the local concentration of the intracellular messenger H(2)O(2). Finally, 2-Cys Prxs interact with a variety of proteins, with such interaction having been shown to modulate the function of the binding partners in a reciprocal manner.

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Crossref · 10.1089/ars.2010.3393

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Authors
Rhee, S. G., & Woo, H. A.
Affiliations
Ewha Womans University (KR)
Venue
Antioxidants & Redox Signaling
Published
2011-08
Volume
15
Issue
3
Pages
781-794
ISSN
  • 1523-0864 (ISSN-L)
  • 1557-7716
OpenAlex
W2153831810
Cited by
463
References
112
Citations by year
2026: 26 · 2025: 24 · 2024: 21 · 2023: 30 · 2022: 24 · 2021: 24 · 2020: 29 · 2019: 28 · 2018: 21 · 2017: 30 · 2016: 38 · 2015: 43 · 2014: 38 · 2013: 31 · 2012: 40
FWCI
2.44
Type
journal article
Language
en
Open access
closed
Locations
  • Antioxidants and Redox Signaling (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
  • Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
  • Health Sciences › Nursing › Nutrition and Dietetics › Selenium in Biological Systems
Keywords
peroxiredoxin, 2-Cys peroxiredoxin, 1-Cys peroxiredoxin, peroxidatic cysteine, disulfide bond formation, molecular chaperones, hydrogen peroxide signaling, sulfiredoxin, hyperoxidation, phosphorylation, protein-protein interaction
MeSH terms
Animals, Antioxidants, Catalysis, Cysteine, Disulfides, Humans, Hydrogen Peroxide, Kinetics, Oxidation-Reduction, Peroxides, Phosphorylation, Threonine, Tyrosine, Molecular Chaperones, Peroxiredoxins

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