Identification of nitric oxide reductase activity in Rhodobacter capsulatus:The electron transport pathway can either use or bypass both cytochrome c2 and the cytochrome bc1 complex

Tools

Bell, L. C., Richardson, D. J. ORCID: https://orcid.org/0000-0002-6847-1832 and Ferguson, S. J. (1992) Identification of nitric oxide reductase activity in Rhodobacter capsulatus:The electron transport pathway can either use or bypass both cytochrome c2 and the cytochrome bc1 complex. Journal of General Microbiology, 138 (3). pp. 437-443. ISSN 0022-1287

Full text not available from this repository. (Request a copy)

Abstract

Several strains of Rhodobacter capsulatus have been shown to possess a nitric oxide reductase activity (reaction product nitrous oxide) after anaerobic phototrophic growth, but not after aerobic growth. The reductase is associated with the cytoplasmic membrane and electrons can reach the enzyme via the cytochrome bc1 complex. However, use of appropriate strains has shown that neither the latter, cytochrome c2 nor cytochrome c' is essential for the reduction of nitric oxide. Inhibition by myxothiazol of nitric oxide reduction in a strain that lacks a cytochrome c2 establishes that in phototrophically grown R. capsulatus the cytochrome bc1, complex is able to transfer electrons to an acceptor that is alternative to cytochrome c2. Electron transport to nitric oxide from NADH or succinate generated a membrane potential. When isoascorbate plus 2,3,5,6-tetramethyl-p-phenylenediamine (DAD) was the electron donor a membrane potential was not generated. This observation implies that nitric oxide is reduced at the periplasmic surface of the membrane and that the reductase is not proton translocating.

Item Type:	Article
Uncontrolled Keywords:	microbiology ,/dk/atira/pure/subjectarea/asjc/2400/2404
Faculty \ School:	Faculty of Science > School of Biological Sciences
UEA Research Groups:	Faculty of Science > Research Groups > Organisms and the Environment Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry
Related URLs:	http://www.scopus.com/inward/record.url?...
Depositing User:	LivePure Connector
Date Deposited:	15 Jul 2022 13:30
Last Modified:	14 May 2023 14:30
URI:	https://ueaeprints.uea.ac.uk/id/eprint/86214
DOI:	10.1099/00221287-138-3-437

Actions (login required)

View Item