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  • Title: Protonation state of Asp120 in the binuclear active site of the metallo-beta-lactamase from Bacteroides fragilis.
    Author: Dal Peraro M, Vila AJ, Carloni P.
    Journal: Inorg Chem; 2003 Jul 14; 42(14):4245-7. PubMed ID: 12844290.
    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.
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