Bacterial Organomercurial Lyase: Novel Enzymatic Protonolysis of Organostannanes

Article abstract of DOI:10.1021/ja00214a047

Pure bacterial organomercurial lyase has been found to catalyze a protonolytic cleavage of the carbon-tin bond in certain organostannanes.Of the compounds tested tetravinyltin is turned over with the highest specific activity, yielding ethylene as the organic product.Similarly, triethylvinyltin undergoes turnover by the lyase to yield ethylene and ethane in a 97:3 ratio, at 1/60th the rate of tetravinyltin turnover.Finally, tetramethyltin and trimethyltin fluoride yield small amounts of methane (2-5 turnovers/mol of enzyme) prior to eventual loss of enzyme activity.The decrease in activity observed during turnover of the organostannanes is consistent with the observed inhibition of the enzyme by dimethyltin dibromide.