The cytochrome bc1 complex of Rhodobacter sphaeroides can restore cytochrome c2-independent photosynthetic growth to a Rhodobacter capsulatus mutant lacking cytochrome bc1
- 1 November 1989
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 171 (11) , 6059-6068
- https://doi.org/10.1128/jb.171.11.6059-6068.1989
Abstract
Plasmids encoding the structural genes for the Rhodobacter capsulatus and Rhodobacter sphaeroides cytochrome (cyt) bc1 complexes were introduced into strains of R. capsulatus lacking the cyt bc1 complex, with and without cyt c2. The R. capsulatus merodiploids contained higher than wild-type levels of cyt bc1 complex, as evidenced by immunological and spectroscopic analyses. On the other hand, the R. sphaeroides-R. capsulatus hybrid merodiploids produced only barely detectable amounts of R. sphaeroides cyt bc1 complex in R. capsulatus. Nonetheless, when they contained cyt c2, they were capable of photosynthetic growth, as judged by the sensitivity of this growth to specific inhibitors of the photochemical reaction center and the cyt bc1 complex, such as atrazine, myxothiazol, and stigmatellin. Interestingly, in the absence of cyt c2, although the R. sphaeroides cyt bc1 complex was able to support the photosynthetic growth of a cyt bc1-less mutant of R. capsulatus in rich medium, it was unable to do so when C4 dicarboxylic acids, such as malate and succinate, were used as the sole carbon source. Even this conditional ability of R. sphaeroides cyt bc1 complex to replace that of R. capsulatus for photosynthetic growth suggests that in the latter species the cyt c2-independent rereduction of the reaction center is not due to a structural property unique to the R. capsulatus cyt bc1 complex. Similarly, the inability of R. sphaeroides to exhibit a similar pathway is not due to some inherent property of its cyt bc1 complex. ImagesThis publication has 35 references indexed in Scilit:
- fbc Operon, encoding the Rieske FeS protein cytochrome b, and cytochrome c1 apoproteins previously described from Rhodopseudomonas sphaeroides, is from Rhodopseudomonas capsulataJournal of Molecular Biology, 1987
- Primary structure of the bc1 complex of Rhodopseudomonas capsulataJournal of Molecular Biology, 1987
- Isolation of the structural genes for the Rieske FeS protein, cytochrome b and cytochrome c1 all components of the ubiquinol: Cytochrome c2 oxidoreductase complex of Rhodopseudomonas capsulataJournal of Molecular Biology, 1987
- Photosynthetic electron transfer in the absence of cytochrome c2 in Rhodopseudomonas capsulata: cytochrome c2 is not essential for electron flow from the cytochrome bc1 complex to the photochemical reaction centerBiochemistry, 1986
- Construction of a broad host range cosmid cloning vector and its use in the genetic analysis of Rhizobium mutantsGene, 1982
- Broad host range DNA cloning system for gram-negative bacteria: construction of a gene bank of Rhizobium meliloti.Proceedings of the National Academy of Sciences, 1980
- Energy transduction in photosynthetic bacteria X. Composition and function of the branched oxidase system in wild type and respiration deficient mutants of Rhodopseudomonas capsulataBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1976
- Asymmetry of an energy transducing membrane. The location of cytochrome c2 in Rhodopseudomonas spheroides and Rhodopseudomonas capsulataBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1975
- The kinetic and redox potentiometric resolution of the carotenoid shifts in Rhodopseudomonas spheroides chromatophores: Their relationship to electric field alterations in electron transport and energy couplingBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1973
- Thermodynamic and Kinetic Characterization of Electron‐Transfer Components in situ in Rhodopseudomonas spheroides and Rhodospirillum rubrumEuropean Journal of Biochemistry, 1972