Overview of Peroxiredoxins in Oxidant Defense and Redox Regulation

Leslie B. Poole1, Andrea Hall2, Kimberly J. Nelson1

1 Department of Biochemistry, Wake Forest University School of Medicine, Winston‐Salem, North Carolina, 2 Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon
Publication Name:  Current Protocols in Toxicology
Unit Number:  Unit 7.9
DOI:  10.1002/0471140856.tx0709s49
Online Posting Date:  August, 2011
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Abstract

Peroxiredoxins are important hydroperoxide detoxification enzymes, yet have only come to the fore in recent years relative to the other major players in peroxide detoxification, heme‐containing catalases and peroxidases and glutathione peroxidases. These cysteine‐dependent peroxidases exhibit high reactivity with hydrogen peroxide, organic hydroperoxides, and peroxynitrite and play major roles not only in peroxide defense, but also in regulating peroxide‐mediated cell signaling. This overview focuses on important peroxiredoxin features that have emerged over the past several decades with an emphasis on catalytic mechanism, regulation, and biological function. Curr. Protoc. Toxicol. 49:7.9.1‐7.9.15. © 2011 by John Wiley & Sons, Inc.

Keywords: peroxidases; antioxidants; antioxidant enzymes; sulfenic acids; hydroperoxides; hydrogen peroxide; thiol peroxidase; Prx; PRDX; redox regulation

     
 
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Table of Contents

  • Introduction
  • Summary
  • Literature Cited
  • Figures
  • Tables
     
 
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Materials

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Literature Cited

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Key References
   Nelson et al., 2011. See above.
  A comprehensive bioinformatics analysis of the peroxiredoxin family of proteins, including subfamily assignments of >3500 peroxiredoxins and a discussion of the insights gained from this analysis.
   Hall et al., 2011. See above.
  An up‐to‐date review of what has been learned from the >70 peroxiredoxin structures in the Protein Data Bank.
   Flohé, 2010. See above.
  Provides a historical perspective of the emerging knowledge about oxidative stress defenses and thiol‐based regulation, including the properties and potential roles for peroxiredoxins in redox signaling.
Internet Resources
  http://www.csb.wfu.edu/prex/
  PREX is a searchable database containing >6000 Prx protein sequences unambiguously classified into one of six distinct subclasses. Subfamily classifications use information around the active sites of structurally characterized subfamily members to search for sequences with conserved functionally relevant motifs (Nelson et al., ; Soito et al., ).
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