FERNANDEZVELASCO, JG and COCCHI, S and NERI, M and HAUSKA, G and MELANDRI, BA (1991) FUNCTIONAL-CHARACTERIZATION OF THE LESION IN THE UBIQUINOL - CYTOCHROME-C OXIDOREDUCTASE COMPLEX ISOLATED FROM THE NONPHOTOSYNTHETIC STRAIN-R126 OF RHODOBACTER-CAPSULATUS. JOURNAL OF BIOENERGETICS AND BIOMEMBRANES, 23 (2). pp. 365-379. ISSN 0145-479X,
Full text not available from this repository.Abstract
The cytochrome bc1 complexes from the nonphotosynthetic strain R126 of Rhodobacter capsulatus and from its revertant MR126 were purified. Between both preparations, no difference could be observed in the stoichiometries of the cytochromes, in their spectral properties, and in their midpoint redox potentials. Both also showed identical polypeptide patterns after electrophoresis on polyacrylamide gels in the presence of sodium dodecylsulfate. The ubiquinol: cytochrome c oxidoreductase activity was strongly inhibited in the complex from the mutant compared to the one from the revertant. So was the oxidant-induced extra reduction of cytochrome b. Both preparations, however, showed an antimycin-induced red shift of cytochrome b, as well as antimycin-sensitive reduction of cytochrome b by ubiquinol. In accordance with a preceding study of chromatophores (Robertson et al. (1986). J. Biol. Chem. 261, 584-591), it is concluded that the mutation affects specifically the ubiquinol oxidizing site, leaving the ubiquinol reducing site unchanged.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | ELECTRON-TRANSFER CHAIN; RHODOPSEUDOMONAS-SPHAEROIDES; UBIQUINOL-CYTOCHROME-C2 OXIDOREDUCTASE; PHOTOSYNTHETIC BACTERIUM; QUINONE POOL; B/C1 COMPLEX; FES PROTEIN; FBC OPERON; SITE; ANTIMYCIN; CYTOCHROME-BC1 COMPLEX; UBIQUINOL OXIDATION; UBIQUINONE REDUCTION; ELECTRON TRANSPORT; RHODOBACTER-CAPSULATUS; PHOTOSYNTHETIC BACTERIA |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:46 |
| URI: | https://pred.uni-regensburg.de/id/eprint/55038 |
Actions (login required)
 |
View Item |
