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Hg–C bond protonolysis by a functional model of bacterial enzyme organomercurial lyase MerB

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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.

Graphical abstract: Hg–C bond protonolysis by a functional model of bacterial enzyme organomercurial lyase MerB

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Supplementary files

Article information


Submitted
29 Mar 2020
Accepted
20 May 2020
First published
20 May 2020

Chem. Commun., 2020, Advance Article
Article type
Communication

Hg–C bond protonolysis by a functional model of bacterial enzyme organomercurial lyase MerB

R. Karri, R. Das, R. K. Rai, A. Gopalakrishnan and G. Roy, Chem. Commun., 2020, Advance Article , DOI: 10.1039/D0CC02232B

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