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Updated: Dec 18, 2025

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Hg-C bond protonolysis by a functional model of bacterial enzyme organomercurial lyase MerB
Ramesh Karri1, Ranajit Das, Rakesh Kumar Rai
1Department of Chemistry, School of Natural Sciences, Shiv Nadar University, NH91, Dadri, Gautam Buddha Nagar, UP 201314, India.
Abstract:
Herein, we report a novel synthetic compound 1, having a highly nucleophilic selenolate (Se-) moiety and a thiol (-SH) functional group, which showed efficient Hg-C bond protonolysis of various R-Hg-X molecules including neurotoxic methylmercury and thimerosal, via direct -SH proton transfer to the highly activated C-atom of a departed R group with low activation energy barrier at room temperature (21 °C), in the absence of any external proton source and, thus, acts as a functional model of MerB.
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