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Cleaving C-Hg bonds: two thiolates are better than one

Organomercurial lyase (MerB) catalyzes the difficult cleavage of C-Hg bonds to hydrocarbon and mercuric dithiol products. Model compounds providing two or three thiolate ligands activate organomercurials toward acidic cleavage under mild conditions, which supports a mechanism in which MerB enzymes use two conserved active-site cysteines to activate the substrate.

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Figure 1: Mechanistic hypotheses showing varied roles of conserved active-site cysteine residues in protolysis.

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S.M.M. studies the mechanisms and interactions of the proteins in the mercury detoxification pathway, including MerB, in work funded by the Department of Energy, Office of Science, grant, DE GF02-ERB4120.

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Miller, S. Cleaving C-Hg bonds: two thiolates are better than one. Nat Chem Biol 3, 537–538 (2007). https://doi.org/10.1038/nchembio0907-537

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