On the mechanism of adenylyl sulfate reductase for the sulfate-reducing bacterium, Desulfovibrio vulgaris.

Abstract

The roles of enzyme-bound FAD and non-heme iron in the mechanism of adenylyl sulfate reductase have been investigated by inhibitor studies, stopped-flow techniques and EPR spectroscopy. The results indicate that the non-heme iron found in the purified reductase is catalytically active and that the turnover number of the enzyme-bound FAD is identical with the maximum turnover number for the enzyme.