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• W2079234423 endingPage "12215" @default.
• W2079234423 startingPage "12214" @default.
• W2079234423 abstract "The synthesis of structural and functional models of the active site of the nonheme iron enzyme cysteine dioxygenase (CDO) is reported. A bis(imino)pyridine ligand scaffold was employed to synthesize a mononuclear ferrous complex, FeII(LN3S)(OTf) (1), which contains three neutral nitrogen donors and one anionic thiolato donor. Complex 1 is a good structural model of the Cys-bound active site of CDO. Reaction of 1 with O2 results in oxygenation of the thiolato sulfur, affording the sulfonato complex FeII(LN3SO3)(OTf) (2) under mild conditions. Isotope labeling studies show that O2 is the sole source of O atoms in the product and that the reaction proceeds via a dioxygenase-type mechanism for two out of three O atoms added, analogous to the dioxygenase reaction of CDO. The zinc(II) analog, Zn(LN3S)(OTf) (4), was prepared and found to be completely unreactive toward O2, suggesting a critical role for FeII in the oxygenation chemistry observed for 1. To our knowledge, S-oxygenation mediated by an FeII−SR complex and O2 is unprecedented." @default.
• W2079234423 created "2016-06-24" @default.
• W2079234423 creator A5005123295 @default.
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• W2079234423 creator A5034134306 @default.
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• W2079234423 creator A5079021544 @default.
• W2079234423 date "2010-08-16" @default.
• W2079234423 modified "2023-10-16" @default.
• W2079234423 title "Iron(II)-Thiolate <i>S</i>-Oxygenation by O₂: Synthetic Models of Cysteine Dioxygenase" @default.
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• W2079234423 doi "https://doi.org/10.1021/ja105591q" @default.
• W2079234423 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2938176" @default.
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• W2079234423 hasPublicationYear "2010" @default.
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