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• W2000601135 abstract "Superoxide reductases (SORs) are cysteine-ligated, non-heme iron enzymes that reduce toxic superoxide radicals (O2-). The functional role of the trans cysteinate, as well as the mechanism by which SOR reduces O2-, is unknown. Herein is described a rare example of a functional metalloenzyme analogue, which catalytically reduces superoxide in a proton-dependent mechanism, via a trans thiolate-ligated iron-peroxo intermediate, the first example of its type. Acetic-acid-promoted H2O2 release, followed by Cp2Co reduction, regenerates the active Fe(II) catalyst. The thiolate ligand and its trans positioning relative to the substrate are shown to contribute significantly to the catalyst's function, by lowering the redox potential, changing the spin state, and dramatically lowering the νFe-O stretching frequency well-below that of any other reported iron-peroxo, while leaving νO-O high, so as to favor superoxide reduction and Fe−O, as opposed to O−O, bond cleavage. Thus we provide critical insight into the relationship between the SOR structure and its function, as well as important benchmark parameters for characterizing highly unstable thiolate-ligated iron-peroxo intermediates." @default.
• W2000601135 created "2016-06-24" @default.
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• W2000601135 date "2006-10-25" @default.
• W2000601135 modified "2023-10-16" @default.
• W2000601135 title "A Functional Model for the Cysteinate-Ligated Non-Heme Iron Enzyme Superoxide Reductase (SOR)" @default.
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• W2000601135 doi "https://doi.org/10.1021/ja064870d" @default.
• W2000601135 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2532059" @default.
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