Phosphoester Hydrolysis: The Incoming Substrate Turns the Bridging Hydroxido Nucleophile into a Terminal One |
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Authors: | Dr. Eric Gouré Dr. Michaël Carboni Angélique Troussier Colette Lebrun Dr. Jacques Pécaut Jean‐François Jacquot Patrick Dubourdeaux Dr. Martin Clémancey Dr. Geneviève Blondin Dr. Jean‐Marc Latour |
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Affiliation: | 1. Univ. Grenoble Alpes, LCBM/PMB and CEA, IRTSV/CBM/PMB and CNRS, LCBM UMR 5249, PMB 38000 Grenoble (France);2. Univ. Grenoble Alpes and CEA, INAC/SCIB/RICC, 38000 Grenoble (France) |
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Abstract: | Identifying the active nucleophile in hydrolysis reactions catalyzed by binuclear hydrolases is a recurrent problem and a matter of intense debate. We report on the phosphate ester hydrolysis by a FeIIIFeII complex of a binucleating ligand. This complex presents activities in the range of those observed for similar biomimetic compounds in the literature. The specific electronic properties of the FeIIIFeII complex allowed us to use 1H NMR and Mössbauer spectroscopies to investigate the nature of the various species present in the solution in the pH range of 5–10. Both techniques showed that the hydrolysis activity is associated to a μ‐hydroxido FeIIIFeII species. Further 1H NMR experiments show that binding of anions or the substrate changes this bonding mode suggesting that a terminal hydroxide is the likely nucleophile in these hydrolysis reactions. This view is further supported by the structure determination of the hydrolysis product. |
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Keywords: | binuclear hydrolases diiron centers Mö ssbauer spectroscopy NMR spectroscopy phosphate esters |
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