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. We report a synthetic molecule 1 , which shows a remarkable ability to protolytically cleave the Hg-C bonds of a wide variety of organomercurials to hydrocarbon and Hg 2+ products under mild conditions, similar to the bacterial enzyme MerB.