Identification of cytochromes involved in electron transport to trimethylamine N-oxide/dimethylsulphoxide reductase in Rhodobacter capsulatus

McEwan, Alastair G., Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832, Hudig, Hendrik, Ferguson, Stuart J. and Jackson, J. Barry (1989) Identification of cytochromes involved in electron transport to trimethylamine N-oxide/dimethylsulphoxide reductase in Rhodobacter capsulatus. BBA - Bioenergetics, 973 (2). pp. 308-314. ISSN 0005-2728

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Abstract

The role of cytochromes in the electron-transport pathway to trimethylamine N-oxide (TMAO)/dimethylsulphoxide (DMSO) reductase in the photosynthetic bacterium Rhodobacter capsulatus was investigated. Reduced-minus-oxidized difference spectra in intact cells with TMAO or DMSO as oxidant revealed cytochrome absorbance changes with a maximum at 559 nm and a shoulder between 548 nm and 556 nm. The former change indicates a role for a 6-type cytochrome and the latter for a c-type cytochrome, both of which are distinct from the cytochrome bc1 complex. Cytochrome c-556 was identified in a bacterial periplasmic fraction as a redox component which couldbe oxidised by TMAO or DMSO. Cytochrome c-556 was the only cytochrome species which co-fractionated with TMAO/DMSO reductase following gel filtration of a post-chromatophore supernatant produced after French presstreatment of intact cells. The mid-point redox potential (pH 7.6) of cytochrome c-556 was + 105 mV (n = 1). It is suggested that TMAO/DMSO reductase and cytochrome c-556 form a structural and functional association in the periplasm of Rhodobacter capsulatus.

Item Type: Article
Additional Information: Funding Information: This work was supported by the SERC (U.K.) via grants to S.J.F. and J.B.J. and a studentship to D.J.R.
Uncontrolled Keywords: (rb. capsulatus),cytochrome c-556,electron transport,periplasmic protein,photosynthetic bacterium,dmso reductase,biophysics,biochemistry,cell biology ,/dk/atira/pure/subjectarea/asjc/1300/1304
Faculty \ School:
Faculty of Science > School of Biological Sciences
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Depositing User: LivePure Connector
Date Deposited: 15 Jul 2022 13:30
Last Modified: 02 Oct 2022 04:39
URI: https://ueaeprints.uea.ac.uk/id/eprint/86222
DOI: 10.1016/S0005-2728(89)80437-2

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