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

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.