Skip to main content
SpringerLink
Log in

Mutational analysis of assembly and function of the iron-sulfur protein of the cytochromebc 1 complex inSaccharomyces cerevisiae

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

Abstract

The iron-sulfur protein of the cytochromebc 1 complex oxidizes ubiquinol at center P in the protonmotive Q cycle mechanism, transferring one electron to cytochromec 1 and generating a low-potential ubisemiquinone anion which reduces the low-potential cytochromeb-566 heme group. In order to catalyze this divergent transfer of two reducing equivalents from ubiquinol, the iron-sulfur protein must be structurally integrated into the cytochromebc 1 complex in a manner which facilitates electron transfer from the iron-sulfur cluster to cytochromec 1 and generates a strongly reducing ubisemiquinone anion radical which is proximal to theb-566 heme group. This radical must also be sequestered from spurious reactivities with oxygen and other high-potential oxidants. Experimental approaches are described which are aimed at understanding how the iron-sulfur protein is inserted into center P, and how the iron-sulfur cluster is inserted into the apoprotein.

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

Access this article

Log in via an institution

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

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

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

    Google Scholar 

  • Beckmann, J. D., Ljungdahl, P. O., and Trumpower, B. L. (1989).J. Biol. Chem. 264, 3713–3722.

    Google Scholar 

  • Bowyer, J. R., and Trumpower, B. L. (1981).J. Biol. Chem. 256, 2245–2251.

    Google Scholar 

  • Bowyer, J. R., Edwards, C. A., and Trumpower, B. L. (1981).FEBS Lett. 126, 93–97.

    Google Scholar 

  • Brandt, U., Schägger, H., and Von Jagow, G. (1988).Eur. J. Biochem. 173, 499–506.

    Google Scholar 

  • Brandt, U., Yu, L., Yu, C.-A., Trumpower, B. L. (1993).J. Biol. Chem. 268, 8387–8390.

    Google Scholar 

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

    Google Scholar 

  • Cheng, M. Y., Hartl, F. U., Martin, J., Pollock, R. A., Kalousek, F., Neupert, W., Hallberg, E. M., Hallberg, R. I., and Horwich, A. L. (1989).Nature (London) 337, 620–625.

    Google Scholar 

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

    Google Scholar 

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

    Google Scholar 

  • Edwards, C. A., Bowyer, J. R., and Trumpower, B. L. (1982).J. Biol. Chem. 257, 3705–3713.

    Google Scholar 

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

    Google Scholar 

  • Graham, L. A., Phillips, J. D., and Trumpower, B. L. (1992).FEBS Lett. 313, 251–254.

    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 

  • Harnisch, U., Weiss, H., and Sebald, W. (1985).Eur. J. Biochem. 149, 95–99.

    Google Scholar 

  • Hartl, F. U., Schmidt, B., Wachter, E., Weiss, H., and Neupert, W. (1986).Cell 47, 939–951.

    Google Scholar 

  • Hendrick, J. P., Hodges, P. E., and Rosenberg, L. I. (1989).Proc. Natl. Acad. Sci. USAS 86, 4056–4060.

    Google Scholar 

  • Huang, J., Struck, F., Matzinger, D. F., and Levings, C. S. (1991).Proc. Natl. Acad. Sci. USA 88, 10716–10720.

    Google Scholar 

  • Japa, S., and Beattie, D. S. (1989).Arch. Biochem. Biophys. 268, 716–720.

    Google Scholar 

  • Kallas, T., Spiller, S., and Malkin, R. (1989).Proc. Natl. Acad. Sci. USA 85, 5794–5798.

    Google Scholar 

  • Kuila, D., Fee, J. A., Schoonover, J. R., Woodruff, W. H., Batie, C. J., and Ballou, D. P. (1987).J. Am. Chem. Soc. 109, 1559–1561.

    Google Scholar 

  • Kurowski, B., and Ludwig, B. (1987).J. Biol. Chem. 262, 13805–13811.

    Google Scholar 

  • Ljungdahl, P. O., Beckmann, J. D., and Trumpower, B. L. (1989).J. Biol. Chem. 264, 3723–3731.

    Google Scholar 

  • Majewski, C., and Trebst, A. (1990).Mol. Gen. Genet. 224, 373–382.

    Google Scholar 

  • Nishikimi, M., Hosokawa, Y., Toda, H., Suzuki, H., and Ozawa, T. (1989).Biochem. Biophys. Res. Commun. 159, 19–25.

    Google Scholar 

  • Nishikimi, M., Hosokawa, Y., Toda, H., Suzuki, H., and Ozawa, T. (1990).Biochem. Int. 20, 155–160.

    Google Scholar 

  • Phillips, J. D., Schmitt, M. E., Brown, T. A., Beckmann, J. D., and Trumpower, B. L. (1990).J. Biol. Chem. 265, 20813–20821.

    Google Scholar 

  • Rich, P. R. (1983).Biochim. Biophys. Acta 722, 271–280.

    Google Scholar 

  • Rieske, J. S. (1976).Biochim. Biophys. Acta 456, 195–247.

    Google Scholar 

  • Rieske, J. S., Baum, H., Stoner, C. D., and Lipton, S. HJ. (1967).J. Biol. Chem. 242, 4854–4866.

    Google Scholar 

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

    Google Scholar 

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

    Google Scholar 

  • Thoeny-Meyer, L., Stax, D., and Hennecke, H. (1989).Cell 57, 683–697.

    Google Scholar 

  • Trumpower, B. L. (1981).Biochim. Biophys. Acta 639, 129–155.

    Google Scholar 

  • Trumpower, B. L. (1990a).Microbiol. Rev. 54, 102–129.

    Google Scholar 

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

    Google Scholar 

  • Usui, S., Yu, L., and Yu, C. A. (1990).Biochem. Biophys. Res. Commun. 167, 575–579.

    Google Scholar 

  • Verbist, J., Lang, F., Gabellini, N., and Oesterhelt, D. (1989).Mol. Gen. Genet. 219, 445–452.

    Google Scholar 

  • Widger, W. R., GenBank Accession No. M74514.

Download references

Author information

Authors and Affiliations

  1. Department of Biochemistry, Dartmouth Medical School, 03755, Hanover, New Hampshire

    Laurie A. Graham, Ulrich Brandt, John S. Sargent & Bernard L. Trumpower

Authors
  1. Laurie A. Graham
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Ulrich Brandt
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. John S. Sargent
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Bernard L. Trumpower
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Graham, L.A., Brandt, U., Sargent, J.S. et al. Mutational analysis of assembly and function of the iron-sulfur protein of the cytochromebc 1 complex inSaccharomyces cerevisiae . J Bioenerg Biomembr 25, 245–257 (1993). https://doi.org/10.1007/BF00762586

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00762586

Key words

Search

Navigation