On the Mechanism of Adenylyl Sulfate Reductase for the Sulfate-Reducing Bacterium, Desulfovibrio vulgaris

Harry D. Peck; Royce Bramlett; Royce Bramlett; Daniel V. Der Vartanian

doi:10.1515/znb-1972-0928

Open Access Published by De Gruyter June 2, 2014

On the Mechanism of Adenylyl Sulfate Reductase for the Sulfate-Reducing Bacterium, Desulfovibrio vulgaris

Harry D. Peck , Royce Bramlett , Royce Bramlett and Daniel V. Der Vartanian

From the journal Zeitschrift für Naturforschung B

https://doi.org/10.1515/znb-1972-0928

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.

Received: 1972-5-10

Published Online: 2014-6-2

Published in Print: 1972-9-1

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

On the Mechanism of Adenylyl Sulfate Reductase for the Sulfate-Reducing Bacterium, Desulfovibrio vulgaris

Journal and Issue

Articles in the same Issue