Abstract
The cytochromebc 1 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.
Similar content being viewed by others
References
Andrews, K. M., Crofts, A. R., and Gennis, R. B. (1990).Biochemistry 29, 2645–2651.
Clayton, R. K. (1963).Biochim. Biophys. Acta 75, 312–323.
Crane, F. L., and Barr, R. (1971).Methods Enzymol. 18C, 137–165.
Crofts, A. R., and Wraight, C. A. (1983).Biochim. Biophys. Acta 726, 149–185.
Crofts, A. R., Meinhardt, S. W., Jones, K. R., and Snozzi, M. (1983).Biochim. Biophys. Acta 723, 202–218.
Daldal, F., Tokito, M. K., Davidson, E., and Faham, M. (1989).EMBO J. 8, 3951–3961.
Drews, G. (1985).Microbiol. Rev. 49, 59–70.
Dutton, P. L., and Prince, R. C. (1978). In:The Photosynthetic Bacteria (Clayton, R. K., and Sistrom, W. R., eds.), Plenum Press, New York, pp. 525–570.
Fernández-Velasco, J. G., Neri, M., Cocchi, S., Hauska, G., and Melandri, B. A. (1986).4th Eur. Bioenerg. Confer., short reports, Congress Edition, Prague, p. 119.
Gabellini, N. (1988).J. Bioenerg, Biomembr. 20, 59–83.
Gabellini, N., and Hauska, G. (1983).FEBS Lett. 153, 146–150.
Gabellini, N., and Sebald, W. (1986).Eur. J. Biochem. 154, 569–579.
Gabellini, N., and Bowyer, J. R., Hurt, E., Melandri, B. A., and Hauska, G. (1982).Eur. J. Biochem. 126, 101–111.
Gabellini, N., Harnisch, U., McCarthy, J. E. G., Hauska, G., and Sebald, W. (1985).EMBO J. 4, 549–553.
García, A. F., Venturoli, G., Gad'on, N., Fernández-Velasco, J. G., Melandri, B. A., and Drews, G. (1987).Biochim. Biophys. Acta 890, 335–345.
Glaser, E. G., Meinhardt, S. W., and Crofts, A. R. (1984).FEBS Lett. 178, 336–342.
Hauska, G. (1986).Methods Enzymol. 126, 271–285.
Hauska, G., Hurt, E., Gabellini, N., and Lockau, W. (1983).Biochim. Biophys. Acta 726, 97–133.
Laemmli, U. K. (1970).Nature (London)227, 680–685.
Link, T., and von Jagow, G. (1986).Methods Enzymol. 126, 253–271.
Ljungdahl, P. O., Pennoyer, J. D., and Trumpower, B. L. (1986).Methods Enzymol. 126, 181–191.
Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951).J. Biol. Chem. 193, 265–275.
Marrs, B. L. (1978).Curr. Top. Bioenerg. 8, 261–294.
Marrs, B. L., Stahl, C. L., Lien, S., and Gest, H. (1972).Proc. Natl. Acad. Sci. USA 69, 916–920.
Matsuura, K., Bowyer, J. R., Ohnishi, T., and Dutton, P. L. (1983).J. Biol. Chem. 258, 1571–1579.
Meinhardt, S. W., and Crofts, A. R. (1982).FEBS Lett. 149, 217–222.
Melandri, B. A., and Venturoli, G. (1984). InBioenergetics (Ernster, L., ed.), Elsevier, Amsterdam, pp. 95–148.
Mitchell, P. (1976).J. Theor. Biol. 62, 327–367.
Ormerod, J. G., Ormerod, K. S., and Gest, H. (1961).Arch. Biochem. Biophys. 94, 449–456.
Purvis, D. J., Theiler, R., and Niederman, R. A. (1990).J. Biol. Chem. 265, 1208–1215.
Rieske, J. S. (1967).Methods Enzymol. 10, 239–245.
Robertson, D. E., and Dutton, P. L. (1988).Biochim. Biophys. Acta 935, 273–291.
Robertson, D. E., Giangiacomo, K. M., De Vries, S., Moser, C. C., and Dutton, P. L. (1984).FEBS Lett. 178, 343–350.
Robertson, D. E., Davidson, E., Prince, R. C., van den Berg, W. H., Marrs, B. L., and Dutton, P. L. (1986).J. Biol. Chem. 261, 584–591.
Takamiya, K., Doi, M., and Okimatsu, H. (1982).Plant Cell. Physiol. 23, 987–997.
Thomas, P. E., Ryan, D., and Wayne, L. (1976).Anal. Biochem. 75, 168–176.
Venturoli, G., Fernández-Velasco, J. G., Crofts, A. R., and Melandri, B. A. (1986).Biochim. Biophys. Acta 851, 340–352.
Venturoli, G., Fernández-Velasco, J. G., Crofts, A. R., and Melandri, B. A. (1988).Biochim. Biophys. Acta 935, 258–272.
von Jagow, G., and Engel, W. D. (1981).FEBS Lett. 136, 19–24.
Wikström, M., and Krab, K. (1986).J. Bioenerg. Biomembr. 18, 181–193.
Wood, P. M. (1980).Biochem. J. 189, 385–391.
Yu, L., and Yu, C-A. (1987).Biochemistry 26, 3658–3664.
Yu, L., Mei, Q-C., and Yu, C-A. (1984).J. Biol. Chem. 259, 5752–5760.
Zannoni, D., and Marrs, B. L. (1981).Biochim. Biophys. Acta 637, 96–106.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Fernández-Velasco, J.G., Cocchi, S., Neri, M. et al. Functional characterization of the lesion in the ubiquinol: Cytochromec oxidoreductase complex isolated from the nonphotosynthetic strain R126 ofRhodobacter capsulatus . J Bioenerg Biomembr 23, 365–379 (1991). https://doi.org/10.1007/BF00762228
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF00762228