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A primer on peroxiredoxin biochemistry
Affiliation:3. From the Center for Structural Biology and Department of Biochemistry,;4. Section on Molecular Medicine, Department of Internal Medicine, Wake Forest School of Medicine, Winston-Salem, North Carolina 27157;1. Department of Medicine, Section of Internal Medicine, University of Verona, AOUI-Policlinico GB Rossi, 37134 Verona, Italy;2. Department of Biomedical Sciences, University of Sassari, Sassari, Italy;3. Department of Oncology, University of Torino, Torino, Italy;4. Department of Life and Reproduction Sciences, Section of Biochemistry, University of Verona, AOUI-Policlinico GB Rossi, 37134 Verona, Italy;5. School of Biological Science and Technology, Chonnam National University, Gwangjiu, Korea;1. Department of Biochemistry and Molecular Biology, Graduate School of Medical Science, Yamagata University, 2-2-2 Iidanishi, Yamagata 990-9585, Japan;2. Division of Molecular Cell Biology, Department of Biomolecular Sciences, Faculty of Medicine, Saga University, 5-1-1 Nabeshima, Saga 849-8501, Japan;1. Institut de Chimie des Substances Naturelles, UPR2301 CNRS, 91190 Gif-sur-yvette, France;2. Imagif Platform, FRC 3115, 91190 Gif-sur-Yvette, France;3. University Paris-Sud, 91405 Orsay, France
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:Hydrogen peroxide  Oxidative stress  Redox signaling  Chaperone  Floodgate hypothesis
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