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The role of thiosulfate in sulfur metabolism of Rhodopseudomonas globiformis

The role of thiosulfate in sulfur metabolism of Rhodopseudomonas globiformis 203 130 130 2 2 Johann Then Hans G. Trüper Institut für Mikrobiologie Rheinische Friedrich-Wilhelms-Universität Meckenheimer Allee 168 D-5300 Bonn 1 Germany Abstract Rhodopseudomonas globiformis is able to assimilate both sulfur moieties of thiosulfate. During growth on 35 S-labelled thiosulfate the amino acids cysteine, homocysteine and methionine were labelled. The bulk of thiosulfate, however, was oxidized to tetrathionate and accumulated in the medium. A thiosulfate: acceptor oxidoreductase was partially purified and characterized. The enzyme oxidized thiosulfate to tetrathionate in the presence of ferricyanide. A c -type cytochrome isolated from this organism was reduced by this enzyme. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Microbiology Springer Journals

The role of thiosulfate in sulfur metabolism of Rhodopseudomonas globiformis

Archives of Microbiology , Volume 130 (2) – Oct 1, 1981

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References (22)

Publisher
Springer Journals
Copyright
Copyright © 1981 by Springer-Verlag GmbH & Co. KG
Subject
Life Sciences; Biotechnology; Biochemistry, general; Cell Biology; Ecology; Microbial Ecology; Microbiology
ISSN
0302-8933
eISSN
1432-072X
DOI
10.1007/BF00411067
Publisher site
See Article on Publisher Site

Abstract

203 130 130 2 2 Johann Then Hans G. Trüper Institut für Mikrobiologie Rheinische Friedrich-Wilhelms-Universität Meckenheimer Allee 168 D-5300 Bonn 1 Germany Abstract Rhodopseudomonas globiformis is able to assimilate both sulfur moieties of thiosulfate. During growth on 35 S-labelled thiosulfate the amino acids cysteine, homocysteine and methionine were labelled. The bulk of thiosulfate, however, was oxidized to tetrathionate and accumulated in the medium. A thiosulfate: acceptor oxidoreductase was partially purified and characterized. The enzyme oxidized thiosulfate to tetrathionate in the presence of ferricyanide. A c -type cytochrome isolated from this organism was reduced by this enzyme.

Journal

Archives of MicrobiologySpringer Journals

Published: Oct 1, 1981

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