Skip to main content
Log in

Thebc 1 complexes ofRhodobacter sphaeroides andRhodobacter capsulatus

  • Minireview
  • Published:
Journal of Bioenergetics and Biomembranes Aims and scope Submit manuscript

Abstract

Photosynthetic bacteria offer excellent experimental opportunities to explore both the structure and function of the ubiquinol-cytochromec oxidoreductase (bc 1 complex). In bothRhodobacter sphaeroides andRhodobacter capsulatus, thebc 1 complex functions in both the aerobic respiratory chain and as an essential component of the photosynthetic electron transport chain. Because thebc 1 complex in these organisms can be functionally coupled to the photosynthetic reaction center, flash photolysis can be used to study electron flow through the enzyme and to examine the effects of various amino acid substitutions. During the past several years, numerous mutations have been generated in the cytochromeb subunit, in the Rieske iron-sulfur subunit, and in the cytochromec 1 subunit. Both site-directed and random mutagenesis procedures have been utilized. Studies of these mutations have identified amino acid residues that are metal ligands, as well as those residues that are at or near either the quinol oxidase (Qo) site or the quinol reductase (Qi) site. The postulate that these two Q-sites are located on opposite sides of the membrane is supported by these studies. Current research is directed at exploring the details of the catalytic mechanism, the nature of the subunit interactions, and the assembly of this enzyme.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Andrews, K. M., Crofts, A. R., and Gennis, R. B. (1990).Biochemistry 29, 2645–2651.

    Google Scholar 

  • Atta-Asafo-Adjei, E., and Daldal, F. (1991).Proc. Natl. Acad. Sci. USA 88, 492–496.

    Google Scholar 

  • Baciou, L., Sinning, I., and Sebban, P. (1991).Biochemistry 30, 9110–9116.

    Google Scholar 

  • Beckmann, J. D., Ljungdahl, P. O., Lopez, J. L., and Trumpower, B. L. (1987).J. Biol. Chem. 262, 8901–8909.

    Google Scholar 

  • Brantd, U., and von Jagow, G. (1991).Eur. J. Biochem. 195, 163–170.

    Google Scholar 

  • Brandt, U., Haase, U., Schägger, H., and von Jagow, G. (1991).J. Biol. Chem. 266, 19958–19964.

    Google Scholar 

  • Brasseur, R. (1988).J. Biol. Chem. 263, 12571–12575.

    Google Scholar 

  • Britt, R. D., Sauer, K., Klein, M. P., Knaff, D. B., Kriaucuinas, A., Yu, C.-A., Yu, L., and Malkin, R. (1991).Biochemistry 30, 1892–1901.

    Google Scholar 

  • Crofts, A. R., and Wraight, C. A. (1983).Biochim. Biophys. Acta 726, 149–185.

    Google Scholar 

  • Crofts, A., Robinson, H., Andrews, K., VanDoren, S., and Berry, E. (1987). InCatalytic Sites for Reduction and Oxidation of Quinones (Papa, S., Chance, B., and Ernster, L., eds.), Plenum, New York, pp. 617–624.

    Google Scholar 

  • Crofts, A., Hacker, B., Barquera, B., Yun, C.-H., and Gennis, R. (1992).Biochim. Biophys. Acta 1101, 162–165.

    Google Scholar 

  • Daldal, F., Davidson, E., and Cheng, S. (1987).J. Mol. Biol. 194, 1–12.

    Google Scholar 

  • Daldal, F., Tokito, M. K., Davidson, E., and Faham, M. (1989).EMBO J. 8, 3951–3961.

    Google Scholar 

  • Davidson, E., and Daldal, F. (1987a).J. Mol. Biol. 195, 25–29.

    Google Scholar 

  • Davidson, E., and Daldal, F. (1987b).J. Mol. Biol. 195, 13–24.

    Google Scholar 

  • Davidson, E., Ohnishi, T., Atta-Asafo-Adjei, E., and Daldal, F. (1992a).Biochemistry 31, 3342–3351.

    Google Scholar 

  • Davidson, E., Ohnishi, T., Tokito, M., and Daldal, F. (1992b).Biochemistry 31, 3351–3358.

    Google Scholar 

  • Degli Esposti, M., De Vries, S., Crimi, M., Ghelli, A., Patarnello, T., and Meyer, A. (1993).Biochem. Biophys. Acta, submitted.

  • Ding, H., Robertson, D. E., Daldal, F., and Dutton, P. L. (1992).Biochemistry 31, 3144–3158.

    Google Scholar 

  • diRago, J. P., and Colson, A.-M. (1988).J. Biol. Chem. 263, 12564–12570.

    Google Scholar 

  • diRago, J.-P., Perea, X., and Colson, A.-M. (1986).FEBS Lett. 208, 208–210.

    Google Scholar 

  • diRago, J.-P., Coppée, J.-Y., and Colson, A.-M. (1989).J. Biol. Chem. 264, 14543–14548.

    Google Scholar 

  • diRago, J.-P., Perea, J., and Colson, A.-M. (1990).FEBS. Lett. 263, 93–98.

    Google Scholar 

  • Doyle, P. M., Li, L.-B., Yu, L., and Yu, C.-A. (1989)J. Biol. Chem. 264, 1387–1392.

    Google Scholar 

  • Erecinska, M., Wilson, D. F., and Blasie, J. K. (1978).Biochim. Biophys. Acta 501, 63–71.

    Google Scholar 

  • Gabellini, N. (1988).J. Bioenerg. Biomembr. 20, 59–83.

    Google Scholar 

  • Gabellini, N., and Sebald, W. (1986).Eur. J. Biochem. 154, 569–579.

    Google Scholar 

  • Gadsby, P. M. A., and Thomson, A. J. (1990).J. Am. Chem. Soc. 112, 5003–5011.

    Google Scholar 

  • Gatti, D. L., Meinhardt, S. W., Ohnishi, T., and Tzagoloff, A. (1989).J. Mol. Biol. 205, 421–435.

    Google Scholar 

  • Gerhus, E., Steinrücke, P., and Ludwig, B. (1990).J. Bacteriol. 172, 2392–2400.

    Google Scholar 

  • Glaser, E. G., and Crofts, A. R. (1984).Biochim. Biophys. Acta 766, 322–333.

    Google Scholar 

  • Gonzalez-Halphen, D., Vazquez-Acevedo, M., and Garcia-Ponce, B. (1991).J. Biol. Chem. 266, 3870–3876.

    Google Scholar 

  • Graham, L. A., and Trumpower, B. L. (1991).J. Biol. Chem. 266, 22485–22492.

    Google Scholar 

  • Gray, K. A., Davidson, E., and Daldal, F. (1992).Biochemistry 31, 11864–11873.

    Google Scholar 

  • Güner, S., Robertson, D. E., Yu, L., Qui, Z.-h., Yu, C.-A., and Knaff, D. B. (1991).Biochim. Biophys. Acta 1058, 269–279.

    Google Scholar 

  • Gurbiel, R. J., Batie, C. J., Sivaraja, M., True, A. E., Fee, J. A., Hoffman, B. M., and Ballou, D. P. (1989).Biochemistry 28, 4861–4871.

    Google Scholar 

  • Gurbiel, R. J., Ohnishi, T., Robertson, D. E., Daldal, F., and Hoffman, B. M. (1991).Biochemistry 30, 11579–11584.

    Google Scholar 

  • Hauska, G., Nitschke, W., and Herrmann, R. G. (1988).J. Bioenerg. Biomembr. 20, 211–228.

    Google Scholar 

  • Howell, N., and Gilbert, K. (1988).J. Mol. Biol. 203, 607–618.

    Google Scholar 

  • Howell, N., Appel, J., Cook, J. P., Howell, B., and Hauswirth, W. W. (1987).J. Biol. Chem. 262, 2411–2414.

    Google Scholar 

  • Irie, S., Doi, S., Yorifuji, T., Takagi, M., and Yano, K. (1987).J. Bacteriol. 169, 5174–5179.

    Google Scholar 

  • Knaff, D. B. (1992).Photosyn. Res., in press.

  • Konishi, K., Van Doren, S. R., Kramer, D. M., Crofts, A. R., and Gennis, R. B. (1991).J. Biol. Chem. 266, 14270–14276.

    Google Scholar 

  • Kurkela, S., Lehväslaiho, H., Palva, E. T., and Teeri, T. H. (1988).Gene 73, 355–362.

    Google Scholar 

  • Li, Y., DeVries, S., Leonard, K., and Weiss, H. (1981).FEBS Lett. 135, 277–280.

    Google Scholar 

  • Meinhardt, S. W., and Crofts, A. R. (1982).FEBS Lett. 149, 217–221.

    Google Scholar 

  • Mitchell, P. (1976).J. Theor. Biol. 62, 327–367.

    Google Scholar 

  • Myatt, J. F., Cotton, N. P. J., and Jackson, J. B. (1987).Biochim. Biophys. Acta 890, 251–259.

    Google Scholar 

  • Nobrega, F. G., and Tzagoloff, A. (1980).J. Biol. Chem. 255, 9828–9837.

    Google Scholar 

  • Paddock, M. L., Feher, G., and Okamura, M. Y. (1991).Photosyn. Res. 27, 109–119.

    Google Scholar 

  • Prince, R. C. (1983).Biochim. Biophys. Acta 723, 133–138.

    Google Scholar 

  • Robertson, D. E., and Dutton, P. L. (1988).Biochim. Biophys. Acta 935, 273–291.

    Google Scholar 

  • Robertson, D. E., Davidson, E., Prince, R. C., van den Berg, W., Marcs, B. L., and Dutton, P. L. (1986).J. Biol. Chem. 261, 584–591.

    Google Scholar 

  • Robertson, D. E., Daldal, F., and Dutton, P. L. (1990).Biochemistry 29, 11249–11260.

    Google Scholar 

  • Robertson, D. E., Ding, H., Chelminski, P. R., Slaughter, C., Hsu, J., Moonraw, C., Tokito, M., Daldal, F., and Dutton, P. L. (1993).Biochemistry 32, 1310–1317.

    Google Scholar 

  • Robertson, D. E., Giangiacono, K. M., deVries, S., Moser, C. C., and Dutton, P.L. (1984).FEBS Lett. 178, 343–350.

    Google Scholar 

  • Salerno, J. C., Blum, H. and Ohnishi, T. (1979).Biochim. Biophys. Acta 547, 270–281.

    Google Scholar 

  • Saraste, M. (1984).FEBS Lett. 166, 367–372.

    Google Scholar 

  • Schägger, H., Borchart, U., Machleidt, W., Link, T. A., and Von Jagow, G. (1987).FEBS Lett. 219, 161–168.

    Google Scholar 

  • Simpkin, D., Palmer, G., Devlin, F. J., McKenna, M. C., Jensen, G. M., and Stephens, P. J. (1989).Biochemistry 28, 8033–8039.

    Google Scholar 

  • Sinning, I. (1992).Trends Biochem. Sci. 17, 150–154.

    Google Scholar 

  • Steppuhn, J., Rother, C., Hermans, J., Jansen, T., Salnikow, J., Hauska, G., and Herrmann, R. G. (1987).Mol. Gen. Genet. 210, 171–177.

    Google Scholar 

  • Tehiler, R., and Niederman, R. A. (1991).J. Biol. Chem. 266, 23163–23168.

    Google Scholar 

  • Tron, T., Crimi, M., Colson, A.-M., and Degli Esposti, M. (1991).Eur. J. Biochem. 199, 753–760.

    Google Scholar 

  • Trumpower, B. L. (1990a).Microbiol. Rev. 54, 101–129.

    Google Scholar 

  • Trumpower, B. L. (1990b).J. Biol. Chem. 265, 11409–11412.

    Google Scholar 

  • Usui, S., and Yu, L. (1991).J. Biol. Chem. 266, 15644–15649.

    Google Scholar 

  • Van Doren, S. R., Gennis, R. B., Barquera, B., and Crofts, A. R. (1993a).Biochemistry, in press.

  • Van Doren, S. R., Yun, C.-H., Crofts, A. R., and Gennis, R. B. (1993b).Biochemistry 32, 628–636.

    Google Scholar 

  • von Jagow, G., and Ohnishi, T. (1985).FEBS Lett. 185, 311–315.

    Google Scholar 

  • von Jagow, G., Gribble, G. W., and Trumpower, B. L. (1986).Biochemistry 25, 775–780.

    Google Scholar 

  • Weber, S., and Wolf, K. (1988).FEBS Lett. 237, 31–34.

    Google Scholar 

  • Widger, W. R., Cramer, W. A., Herrmann, R. G., and Trebst, A. (1984).Proc. Natl. Acad. Sci. 81, 674–678.

    Google Scholar 

  • Yu, L., and Yu, C.-A. (1991).Biochemistry 30, 4934–4939.

    Google Scholar 

  • Yun, C.-H., Beci, R., Crofts, A. R., Kaplan, S., and Gennis, R. B. (1990).Eur. J. Biochem. 194, 399–411.

    Google Scholar 

  • Yun, C.-H., Crofts, A. R., and Gennis, R. B. (1991a).Biochemistry 30, 6747–6754.

    Google Scholar 

  • Yun, C.-H., Van Doren, S. R., Crofts, A. R., and Gennis, R. B. (1991b).J. Biol. Chem. 266, 10967–10973.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Gennis, R.B., Barquera, B., Hacker, B. et al. Thebc 1 complexes ofRhodobacter sphaeroides andRhodobacter capsulatus . J Bioenerg Biomembr 25, 195–209 (1993). https://doi.org/10.1007/BF00762582

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00762582

Key words

Navigation