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• W2000939204 abstract "The determination of the protonation state of enzyme active sites may be crucial for the investigation of their mechanism of action. In the bizinc beta-lactamase family of enzymes, no consensus has been reached on the protonation state of a fully conserved amino acid present in the active site, Asp120. To address this issue, we carry out here density functional theory (DFT) calculations on large models (based on Bacteroides fragilis X-ray structure) which include the metal coordination polyhedron and groups interacting with it. Our calculations suggest that Asp120 is ionized. The relevance of this finding for site-directed mutagenesis experiments on the 120 position and on the mechanism of action is discussed." @default.
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• W2000939204 date "2003-06-12" @default.
• W2000939204 modified "2023-09-30" @default.
• W2000939204 title "Protonation State of Asp120 in the Binuclear Active Site of the Metallo-β-Lactamase from Bacteroides fragilis" @default.
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• W2000939204 doi "https://doi.org/10.1021/ic026059j" @default.
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