Advertisement

Iron-Sulfur Proteins, the Most Numerous and Most Diversified Components of the Mitochondrial Electron Transfer System

  • Helmut Beinert
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 74)

Abstract

The field of iron-sulfur (Fe-S) proteins has developed rapidly in the past ten years, in depth and in breadth, as is best witnessed by the appearance within the past few years of three volumes of a treatise exclusively devoted to these compounds (1). The great number and variety of recently discovered plant, bacterial and mammalian Fe-S proteins and of the reactions catalyzed by them, exemplify this progress. This presentation will focus on the last mentioned area, namely that of Fe-S proteins in mammalian systems, more precisely on those occurring in the electron transfer system of mitochondria.

Keywords

Xanthine Oxidase Succinate Dehydrogenase NADH Dehydrogenase Midpoint Potential Electron Transfer System 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    “Iron-Sulfur Proteins”, Vol. 1, 1973; Vol. II, 1973; Vol. Ill, in press. (W. Lovenberg, ed.), Academic Press, New York.Google Scholar
  2. 2.
    S.P.J. Albracht, Biochim. Biophys. Acta 347 (1974), 183–192.PubMedCrossRefGoogle Scholar
  3. 3.
    S.P.J. Albracht and H.-G. Heidrich, Biochim. Biophys. Acta 376 (1975), 231–236.PubMedCrossRefGoogle Scholar
  4. 4.
    S.P.J. Albracht and G. Dooijewaard (1976). In “Electron Transfer Chains and Oxidative Phosphorylation”, (E. Quagliarello, et al., ed.) North Holland Publishing Co., Amsterdam, in press.Google Scholar
  5. 5.
    H. Beinert and F. J. Ruzicka (1976). In “Electron Transfer Chains and Oxidative Phosphorylation”, (E. Quagliarello, et al. ed.) North Holland Publishing Co., Amsterdam, in press.Google Scholar
  6. 6.
    T. Ohnishi, Biochem. Biophys. Acta 387 (1975), 475–490.PubMedCrossRefGoogle Scholar
  7. 7.
    T. Ohnishi, D. B. Winter, J. Lim, and T. E. King, Biochem. Biophys. Res. Commun. 53 (1973), 231–237.CrossRefGoogle Scholar
  8. 8.
    T. Ohnishi, J. S. Leigh, C. I. Ragan, and E. Racker, Biochem. Biophys. Res. Commun. 56 (1974), 775–782.CrossRefGoogle Scholar
  9. 9.
    T. Ohnishi, D. Winter, J. Lim, and T. E. King, Biochem. Biophys. Res. Commun. 61 (1974), 1017–1025.CrossRefGoogle Scholar
  10. 10.
    N. R. Orme-Johnson, R. E. Hansen, and H. Beinert, J. Biol. Chem. 249 (1974), 1922–1927.PubMedGoogle Scholar
  11. 11.
    N. R. Orme-Johnson, R. E. Hansen, and H. Beinert, J. Biol. Chem. 249 (1974), 1928–1939.PubMedGoogle Scholar
  12. 12.
    F. J. Ruzicka and H. Beinert, Biochem. Biophys. Res. Commun. 58 (1974), 556–563.PubMedCrossRefGoogle Scholar
  13. 13.
    F. J. Ruzicka and H. Beinert, Biochem. Biophys. Res. Commun. 66 (1975), 622–631.PubMedCrossRefGoogle Scholar
  14. 14.
    H. Beinert, B.A.C. Ackrell, E. B. Kearney, and T. P. Singer, Biochem. Biophys. Res. Commun. 58 (1974), 564–572.PubMedCrossRefGoogle Scholar
  15. 15.
    H. Beinert, B.A.C. Ackrell, E. B. Kearney, and T. P. Singer, Eur. J. Biochem. 54 (1975), 185–194.PubMedCrossRefGoogle Scholar
  16. 16.
    T. Ohnishi, D. F. Wilson, T. Asakura, and B. Chance, Biochem. Biophys. Res. Commun. 46 (1972), 1631–1638.PubMedCrossRefGoogle Scholar
  17. 17.
    H. Beinert (1963). In “The Enzymes”, Vol. VII, pgs. 467–476, Academic Press, Inc.Google Scholar
  18. 18.
    F. L. Crane, and H. Beinert, J. Biol. Chem. 218 (1956), 717–731.PubMedGoogle Scholar
  19. 19.
    J. S. Rieske, R. E. Hansen, and W. S. Zaugg, J. Biol. Chem. 239 (1964), 3017–3022.PubMedGoogle Scholar
  20. 20.
    J. S. Leigh, Jr., and M. Erecinska, Biochim. Biophys. Acta 387 (1975), 95–106.PubMedCrossRefGoogle Scholar
  21. 21.
    R. Malkin and P. J. Aparicio, Biochem. Biophys. Res. Commun. 63 (1975), 1157–1160.PubMedCrossRefGoogle Scholar
  22. 22.
    R. C. Prince, J. G. Lindsay, and P. L. Dutton, FEBS Letters 51 (1975), 108–111.PubMedCrossRefGoogle Scholar
  23. 23.
    T. Ohnishi, W. J. Ingledew, and S. Shiraishi, Biochem. Biophys. Res. Commun. 63 (1975), 894–899.PubMedCrossRefGoogle Scholar
  24. 24.
    D. Bäckström, I. Hoffström, I. Gustafsson, and A. Ehrenberg, Biochem. Biophys. Res. Commun. 53 (1973), 596–602.PubMedCrossRefGoogle Scholar
  25. 25.
    J. S. Olson, D. P. Ballou, G. Palmer, and V. Massey, J. Biol. Chem. 249 (1974), 4363–4382.PubMedGoogle Scholar
  26. 26.
    H. Beinert, Iron-sulfur proteins, Vol. III, (W. Lovenberg, ed.), Academic Press, New York, in press.Google Scholar
  27. 27.
    C. W. Carter, Jr., J. Kraut, S. T. Freer, R. A. Alden, L. C. Sieker, E. Adman, and L. H. Jensen, Proc. Nat. Acad. Sci. U.S. 69 (1972), 3526–3529.CrossRefGoogle Scholar
  28. 28.
    K. Dus, H. De Klerk, K. Sletten, and R. G. Bartsch, Biochem. Biophys. Acta 140 (1967), 291–311.PubMedCrossRefGoogle Scholar
  29. 29.
    T. Herskovitz, B. A. Averill, R. H. Holm, J. A. Ibers, W. D. Phillips, and J. F. Weiher, Proc. Nat. Acad. Sci. U.S. 69 (1972), 2437–2441.CrossRefGoogle Scholar
  30. 30.
    R. Cammack, Biochem. Biophys. Res. Commun. 54 (1973), 538–554.CrossRefGoogle Scholar
  31. 31.
    D. F. Erbes, R. H. Burris, and W. H. Orme-Johnson, Proc. Nat. Acad. Sci. U.S. (1975), in press.Google Scholar
  32. 32.
    W. V. Sweeney and J. C. Rabinowitz, and D. C. Yoch, J. Biol. Chem. 250 (1975), 7842–7847.PubMedGoogle Scholar
  33. 33.
    D. C. Yoch, W. V. Sweeney, and D. I. Arnon, J. Biol. Chem. 250 (1975), 8330–8336.PubMedGoogle Scholar
  34. 34.
    T. Ohnishi, Biochem. Biophys. Acta 301 (1973), 105–128.CrossRefGoogle Scholar
  35. 35.
    J. G. Cobley, S. Grossman, T. P. Singer, and H. Beinert, J. Biol. Chem. 250 (1975), 211–217.PubMedGoogle Scholar
  36. 36.
    F. J. Ruzicka, H. Beinert, K. L. Schepler, W. R. Dunham, and R. H. Sands, Proc. Nat. Acad. Sci. U.S., 72, (1975), 2886–2890.CrossRefGoogle Scholar
  37. 37.
    T. Ohnishi, J. S. Leigh, C. I. Ragan, and E. Racker, Biochem. Biophys. Res. Commun. 56 (1974), 775–782.CrossRefGoogle Scholar
  38. 38.
    R. Mathews, S. Charlton, R. H. Sands, and G. Palmer, J. Biol. Chem. 249 (1974), 4326–4328.PubMedGoogle Scholar
  39. 39.
    D. J. Lowe, R. M. Lynden-Bell, and R. C. Bray, Biochem. J. 130 (1972), 239–249.PubMedGoogle Scholar

Copyright information

© Plenum Press, New York 1976

Authors and Affiliations

  • Helmut Beinert
    • 1
  1. 1.Institute for Enzyme ResearchUniversity of WisconsinMadisonUSA

Personalised recommendations