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• W2075614999 abstract "Phosphotriesterase (PTE) is a binuclear metalloenzyme that catalyzes the hydrolysis of organophosphates, including pesticides and chemical warfare agents, at rates approaching the diffusion controlled limit. The catalytic mechanism of this enzyme features a bridging solvent molecule that is proposed to initiate nucleophilic attack at the phosphorus center of the substrate. X-band EPR spectroscopy is utilized to investigate the active site of Mn/Mn-substituted PTE. Simulation of the dominant EPR spectrum from the coupled binuclear center of Mn/Mn-PTE requires slightly rhombic zero-field splitting parameters. Assuming that the signal arises from the S = 2 manifold, an exchange coupling constant of J = −2.7 ± 0.2 cm-1 (Hex = −2JS1·S2) is calculated. A kinetic pKa of 7.1 ± 0.1 associated with loss in activity at low pH indicates that a protonation event is responsible for inhibition of catalysis. Analysis of changes in the EPR spectrum as a function of pH provides a pKa of 7.3 ± 0.1 that is assigned as the protonation of the hydroxyl bridge. From the comparison of kinetic and spectral pKa values, it is concluded that the loss of catalytic activity at acidic pH results from the protonation of the hydroxide that bridges the binuclear metal center." @default.
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• W2075614999 date "2005-07-29" @default.
• W2075614999 modified "2023-10-03" @default.
• W2075614999 title "Protonation of the Binuclear Metal Center within the Active Site of Phosphotriesterase" @default.
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• W2075614999 doi "https://doi.org/10.1021/bi0506270" @default.
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