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• W2071119458 endingPage "2603" @default.
• W2071119458 startingPage "2595" @default.
• W2071119458 abstract "Despite the current availability of several crystal structures of purple acid phosphatases, to date there is no direct evidence for solvent-derived ligands occupying terminal positions in the active enzyme. This is of central importance, because catalysis has been shown to proceed through the direct attack on a metal-bound phosphate ester by a metal-activated solvent-derived moiety, which has been proposed to be either (i) a hydroxide ligand terminally bound to the ferric center or (ii) a bridging hydroxide. In this work we use 2H Q-band (35 GHz) pulsed electron−nuclear double resonance (ENDOR) spectroscopy to identify solvent molecules coordinated to the active mixed-valence (Fe3+Fe2+) form of the dimetal center of uteroferrin (Uf), as well as to its complexes with the anions MoO4, AsO4, and PO4. The solvent-derived coordination of the dinuclear center of Uf as deduced from ENDOR data includes a bridging hydroxide and a terminal water/hydroxide bound to Fe2+ but no terminal water/hydroxide bound to Fe3+. The terminal water is lost upon anion binding while the hydroxyl bridge remains. These results are not compatible with a hydrolysis mechanism involving a terminal Fe3+-bound nucleophile, but they are consistent with a mechanism that relies on the bridging hydroxide as the nucleophile." @default.
• W2071119458 created "2016-06-24" @default.
• W2071119458 creator A5006174959 @default.
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• W2071119458 date "2002-02-23" @default.
• W2071119458 modified "2023-09-24" @default.
• W2071119458 title "Electron−Nuclear Double Resonance Spectroscopic Evidence for a Hydroxo-Bridge Nucleophile Involved in Catalysis by a Dinuclear Hydrolase" @default.
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• W2071119458 doi "https://doi.org/10.1021/ja003169l" @default.
• W2071119458 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11890810" @default.
• W2071119458 hasPublicationYear "2002" @default.
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