Abstract
Organomercury-decomposing activity in Clostridium cochlearium T-2P harboring a plasmid which mediates mercury resistance was studied. The results obtained indicated that the splitting of the CHg bond was catalyzed by an enzyme present in the cell extract which requires glucose, but not SH compounds, for its activity. The ability to degrade organomercurials was induced specifically by mercury compounds, particularly by organic mercury, but not by other metal ions. Alkylmercury was a better substrate for the decomposing enzyme than arylmercury. The properties of the decomposing enzyme were very different from those of the other splitting enzymes reported so far.
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