Isolation and characterization of a prokaryotic sulfurtransferase.

A sulfurtransferase has been purified to apparent homogeneity from the prokaryote Acinetobacter calcoaceticus lwoffi by conventional protein fractionation techniques. Steady-state kinetic studies of the enzyme revealed that its formal mechanism varies with the acceptor substrate employed. With inorganic thiosulfate as the sulfane sulfur-donor substrate and cyanide anion as the acceptor, the enzyme was shown to catalyze the reaction by a double displacement mechanism like that of mammalian rhodanese (thiosulfate:cyanide sulfurtransferase, EC 2.8.1.1). In contrast, with a thiol as the acceptor substrate at relatively high concentrations, the reaction proceeds by a single displacement mechanism, reminiscent of catalysis by another sulfur-transferase, thiosulfate reductase, glutathione-dependent (EC 2.8.1.3). When dithiothreitol is the acceptor substrate, the enzyme cycles through both the single and double displacement pathways, with the flux through each depending differentially on the concentration of dithiothreitol employed. In view of both the relaxed acceptor substrate specificity and the corresponding variability of formal mechanism, the more general name of sulfane sulfurtransferase is proposed for this bacterial enzyme.