title: A primer on peroxiredoxin biochemistry.
abstract: Peroxiredoxins were not recognized as a family of enzymes until the 1990s but are now known to be the dominant peroxidases in most organisms. Here, the history and fundamental properties of peroxiredoxins are briefly reviewed, with a special focus on describing how an exquisitely tunable balance between fully folded and locally unfolded conformations plays a large role in peroxiredoxin catalytic properties.
authors.affiliation: Department of Biochemistry and Biophysics, Oregon State University, Corvallis, OR 97331, USA. Electronic address: karplusp@science.oregonstate.edu.
authors.forename: P Andrew
authors.initials: PA
authors.lastname: Karplus
mesh_terms: D000818:Animals; D001419:Bacteria / Q000201:enzymology; D055162:Biocatalysis; D005658:Fungi / Q000201:enzymology; D049673:History, 20th Century; D049674:History, 21st Century; D006801:Humans; D007700:Kinetics; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000145:classification / Q000235:genetics / Q000266:history / Q000378:metabolism*; D005810:Multigene Family; D010084:Oxidation-Reduction; D054464:Peroxiredoxins / Q000145:classification / Q000235:genetics / Q000266:history / Q000378:metabolism*; D011487:Protein Conformation; D017510:Protein Folding; D055503:Protein Multimerization; D013438:Sulfhydryl Compounds / Q000737:chemistry* / Q000378:metabolism
chemical_list: D018832:Molecular Chaperones; D013438:Sulfhydryl Compounds; D054464:Peroxiredoxins
keywords: Chaperone; Floodgate hypothesis; Hydrogen peroxide; Oxidative stress; Redox signaling