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The Catalytic Mechanism of Peroxiredoxins

  • Chapter
Peroxiredoxin Systems

Part of the book series: Subcellular Biochemistry ((SCBI,volume 44))

Abstract

Peroxiredoxins carry out the efficient reduction of a typically broad range of peroxide substrates through an absolutely conserved, activated cysteine residue within a highly conserved active site pocket structure. Though details of reductive recycling after cysteine sulfenic acid formation at the active site vary among members of different Prx classes, local unfolding around the active site cysteine is likely generally required in these proteins for disulfide bond formation with a second resolving cysteine and/or for access of the reductant to the oxidized active site. The conformational change associated with the catalytic cycle and the redox-dependent decamer formation occurring in at least some typical 2-Cys Prxs have interesting implications in the interplay between active site loop dynamics, oligomerization state, catalytic efficiency and propensity toward inactivation during turnover in these important antioxidant enzymes

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Authors and Affiliations

  1. Department of Biochemistry, Center for Structural Biology, BGTC, Wake Forest University School of Medicine, Winston-Salem, NC, 27157, USA

    Leslie B. Poole

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  1. Leslie B. Poole
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  1. MOLISA GmbH Magdeburg, Magdeburg, Germany

    Leopold Flohé

  2. University of Mainz, Mainz, Germany

    J. Robin Harris

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© 2007 Springer

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Poole, L.B. (2007). The Catalytic Mechanism of Peroxiredoxins. In: Flohé, L., Harris, J.R. (eds) Peroxiredoxin Systems. Subcellular Biochemistry, vol 44. Springer, Dordrecht. https://doi.org/10.1007/978-1-4020-6051-9_4

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