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Journal of Bioenergetics and Biomembranes

, Volume 23, Issue 2, pp 365–379 | Cite as

Functional characterization of the lesion in the ubiquinol: Cytochromec oxidoreductase complex isolated from the nonphotosynthetic strain R126 ofRhodobacter capsulatus

  • Javier G. Fernández-Velasco
  • Silvia Cocchi
  • Mauro Neri
  • Günter Hauska
  • B. Andrea Melandri
Research Articles

Abstract

The cytochromebc1 complexes from the nonphotosynthetic strain R126 ofRhodobacter 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: cytochromec 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 cytochromeb. Both preparations, however, showed an antimycin-induced red shift of cytochromeb, as well as antimycin-sensitive reduction of cytochromeb by ubiquinol. In accordance with a preceding study of chromatophores (Robertsonet 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.

Key Words

Cytochromebc1 complex ubiquinol oxidation ubiquinone reduction electron transport Rhodobacter capsulatus photosynthetic bacteria 

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Copyright information

© Plenum Publishing Corporation 1991

Authors and Affiliations

  • Javier G. Fernández-Velasco
    • 1
  • Silvia Cocchi
    • 1
  • Mauro Neri
    • 1
  • Günter Hauska
    • 2
  • B. Andrea Melandri
    • 1
  1. 1.Istituto ed Orto BotanicoUniversità di BolognaBolognaItaly
  2. 2.Institut fuer Zellbiologie und PflanzenphysiologieUniversitaet RegensburgRegensburgGermany

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