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.
Keywords:
Chaperone; Floodgate hypothesis; Hydrogen peroxide; Oxidative stress; Redox signaling.
Copyright © 2014 Elsevier Inc. All rights reserved.
Publication types
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Historical Article
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Research Support, N.I.H., Extramural
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Review
MeSH terms
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Animals
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Bacteria / enzymology
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Biocatalysis
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Fungi / enzymology
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History, 20th Century
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History, 21st Century
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Humans
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Kinetics
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Models, Molecular
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Molecular Chaperones / classification
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Molecular Chaperones / genetics
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Molecular Chaperones / history
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Molecular Chaperones / metabolism*
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Multigene Family
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Oxidation-Reduction
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Peroxiredoxins / classification
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Peroxiredoxins / genetics
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Peroxiredoxins / history
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Peroxiredoxins / metabolism*
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Protein Conformation
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Protein Folding
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Protein Multimerization
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Sulfhydryl Compounds / chemistry*
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Sulfhydryl Compounds / metabolism
Substances
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Molecular Chaperones
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Sulfhydryl Compounds
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Peroxiredoxins