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Science 13 July 2007:
Vol. 317. no. 5835, p. 165
DOI: 10.1126/science.317.5835.165c
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This Week in Science
Bacteria have evolved a group of enzymes that can deactivate highly toxic alkyl mercury contaminants, but many of the molecular details underlying their mode of action remain unclear. The organomercurial lyase MerB specifically accomplishes scission of Hg-C bonds. Melnick and Parkin (p. 225; see the Perspective by Omichinski) report that a ligand bearing three coordinating sulfur groups, analogous to active-site cysteines in the enzyme, efficiently induces reaction of a mercury methyl, ethyl, or cyanomethyl center with a thiol to liberate the alkane or nitrile. Characterization of the Hg methyl and ethyl complexes in the solid state and in solution reveals that although an overall two-coordinate geometry is favored, the metal interacts rapidly with the additional sulfur groups in the ligand, which appear to promote reactivity lacking in other molecular Hg compounds.
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Science. ISSN 0036-8075 (print), 1095-9203 (online)
