Aerobic and anaerobic respiratory systems in Campylobacter fetus subsp. jejuni grown in atmospheres containing hydrogen
- 30 September 1982
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 152 (1) , 306-314
- https://doi.org/10.1128/jb.152.1.306-314.1982
Abstract
Maximum growth of C. fetus ssp. jejuni, strain C-61, occurred when the cultures were incubated with shaking in atmospheres containing .apprx. 30% H2, 5% O2 and 10% CO2. Suspensions of cells grown under these conditions consumed O2 with formate as the substrate in the presence of 0.33 mM cyanide, which completely inhibited respiration with ascorbate-N,N,N'',N''-tetramethyl-p-phenylenediamine and with lactate. Spectroscopic evidence with intact cells suggested that a form of cytochrome c, reducible with formate but not with lactate or ascorbate-N,N,N'',N''-tetramethyl-p-phenylenediamine, can be reoxidized by a cyanide-insensitive system. Analysis of membranes from the cells showed high- and low-potential forms of cytochrome c, cytochrome b and various enzymes, including hydrogenase, formate dehydrogenase and fumarate reductase. The predominant CO-binding pigment appeared to be a form of cytochrome c, but the spectra also showed evidence of cytochrome o. The membrane cytochromes were reduced by H2 in the presence of 2-heptyl-4-hydroxyquinoline-N-oxide at concentrations which prevented the reduction of cytochrome c with succinate as the electron donor. Reoxidation of the substrate-reduced cytochromes by O2 was apparently mediated by cyanide-sensitive and cyanide-insensitive systems. The membranes also had hydrogen-fumarate oxidoreductase activity mediated by cytochrome b. C. fetus ssp. jejuni has high- and low-potential forms of cytochrome which are associated with a complex terminal oxidase system.This publication has 15 references indexed in Scilit:
- The two cytochromes c in the facultative methylotroph Pseudomonas AM1Biochemical Journal, 1980
- The purification and properties of the soluble cytochromes c of the obligate methylotroph Methylophilus methylotrophusBiochemical Journal, 1980
- Oxygen consumption by Campylobacter sputorum subspecies Bubulus with formate as substrateArchiv für Mikrobiologie, 1980
- Bacterial iron-sulfur proteins.1979
- Flavoproteins, Iron Proteins, and Hemoproteins as Electron-Transfer Components of the Sulfate-Reducing BacteriaPublished by Elsevier ,1979
- [22] Bacterial cytochromes and their spectral characterizationPublished by Elsevier ,1978
- The effect of respiratory chain composition on the growth efficiencies of aerobic bacteriaArchiv für Mikrobiologie, 1977
- The Function of the b Cytochromes in the Electron Transport from Formate to Fumarate of Vibrio succinogenesEuropean Journal of Biochemistry, 1976
- The Function of Menaquinone, Covalently Bound FAD and Iron‐Sulfur Protein in the Electron Transport from Formate to Fumarate of Vibrio succinogenesEuropean Journal of Biochemistry, 1976
- A simple technique for eliminating interference by detergents in the Lowry method of protein determinationAnalytical Biochemistry, 1975