An organomercurial lyase catalyzes the protonolysis of the carbon-Hg bond to give a hydrocarbon and a mercuric ion (Summers 1985; Robinson and Tuovinen 1984; Summers and Silver 1978). Mercuric reductase then catalyzes the reduction of mercuric Hg to elemental Hg. NADPH is the coenzyme in that reaction (Fox and Walsh 1982, 1983; Brown et al. 1983). Because elemental Hg is volatile, it evaporates from the bacterial culture.
GI absorption of MeHg is decreased by intestinal flora that convert MeHg to inorganic Hg (mercuric ion) (Nakamura et al. 1977; Rowland et al. 1980), which is poorly absorbed. Organomercurial lyase has been purified from Escherichia coli (Begley et al. 1986). The enzyme is encoded on the plasmid R831. No cofactors are required for enzyme activity, and the enzyme structure does not contain any metals. The enzyme can catalyze protonolysis of the C-Hg bond in primary, secondary, and tertiary alkyl, vinyl, allyl, and aryl organomercurial salts to the hydrocarbon and mercuric ion. A thiol must be present for activity, cysteine being the most active thiol compound, for demethylation of organic mercurials.