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- W67150131 endingPage "81" @default.
- W67150131 startingPage "61" @default.
- W67150131 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" @default.
- W67150131 created "2016-06-24" @default.
- W67150131 creator A5044120325 @default.
- W67150131 date "2007-01-01" @default.
- W67150131 modified "2023-10-17" @default.
- W67150131 title "The Catalytic Mechanism of Peroxiredoxins" @default.
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- W67150131 doi "https://doi.org/10.1007/978-1-4020-6051-9_4" @default.
- W67150131 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18084890" @default.
- W67150131 hasPublicationYear "2007" @default.
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