ScholarLens Back to search
1972•Zeitschrift für Naturforschung BOpen access

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

Harry D. Peck, Royce Bramlett, Royce Bramlett, Daniel V. VARTANIAN

Open full text 11 citations

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.

Open-access reader

About this research paper

What this paper is about

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.

Why it matters

OpenAlex reports 11 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available 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.

Key concepts: Desulfovibrio vulgaris, Reductase, Chemistry, Heme, Enzyme, Biochemistry, Sulfate, Nitrite reductase

Related papers

Related paper 1Related paper 2Related paper 3
Back to paper searchBrowse research topicsOriginal source
On the Mechanism of Adenylyl Sulfate Reductase for the Sulfate-Reducing Bacterium, Desulfovibrio vulgaris — Research Paper | ScholarLens