Advertisement

EPR and Electron Spin Echo Studies of Iron-Sulfur Clusters S-1 And S-2 in Bovine Heart Succinate Dehydrogenase

  • Russell LoBrutto
  • Paul E. Haley
  • Chang-An Yu
  • Tomoko Ohnishi

Summary

The ligands of the three iron-sulfur clusters in bovine heart succinate dehydrogenase (BH-SDH) have not been determined to date. We have made a detailed comparison of the electron spin echo envelope modulation (ESEEM) spectra from the [2Fe-2S] (+1,+2) cluster S-I with spectra obtained from two better-characterized iron-sulfur proteins. X- ray crystallographic data (1) demonstrated that the [2Fe-2S](+1,+2) cluster in Spirulina platensis ferredoxin has four cysteine sulfur ligands, but that there are several nitrogens in the polypeptide backbone that are close enough to form NH..S hydrogen bonds to the cluster. The ESEEM spectrum of the dithionite-reduced protein shows intense modulations characteristic of 14N at all g-values. At g = 1.94, four distinct modulation frequencies are evident: 0.6, 1.9, 2.9 and 4.4 MHz. The ESEEM spectrum of spinach ferredoxin is virtually identical to that of S. platensis feredoxin at g = 1.94, and at the other principal g-values. The ESEEM spectrum of cluster S-I in BH-SDH contains four very similar frequencies at g = 1.94. It does not exhibit any additional modulation frequencies which might be attributed to nitrogen from an imidazole ligand. The data indicate that cluster S-I also has only non- imidazole ligands, probably all sulfur.

Keywords

Contact Term Electron Spin Echo Envelope Modulation Bovine Heart Electron Spin Echo Imidazole Ligand 
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.
    Tsukihara, T., Fukuyama, K., Nakamura, T., Katsube, Y., Tanaka, N., Kakudo, Wada, M.K., Hase, T. and Matsubara, H. (1981) J. Biochem. 90, 1763–1773.Google Scholar
  2. 2.
    Johnson, M. K., Morningstar, J. E., Bennett, D. E., Ackrell, B.A.C. and Kearney, E.B. (1985) J. Biol. Chem. 260(12), 7368–7378.Google Scholar
  3. 3.
    Maguire, M. K. Johnson, J.E. Morningstar, B. A. C. Ackrell and E. B. Kearney (1985) J. Biol. Chem. 260, 10909–10912.Google Scholar
  4. 4.
    Huynh, J.J. G. Moura, I. Moura, T. A. Kent, J. Legall, A.V. Xavier, and E. Munck (1980) J. Biol. Chem. 255, 3242–3244.Google Scholar
  5. 5.
    J.F. Cline, B. M. Hoffman, W.B. Mims, E. LaHaie, D.P. Ballou, and J. A. Fee (1985) J. Biol. Chem. 260 (6), 3251–3254.Google Scholar
  6. 6.
    C.-A. Yu and L. Yu (1980) Biochim. Biophys. Acta 591 409–420.CrossRefGoogle Scholar
  7. 7.
    LoBrutto and J. S. Leigh, manuscript in preparation; b) R. LoBrutto, G.W. Smithers, G.H. Reed, W.H. Orme-Johnson, S.L. Tan, and J. S. Leigh Jr. (1986) Biochemistry, in press.Google Scholar
  8. 8.
    Thomann, L.R. Dalton, and L.A. Dalton, in: Biological Magnetic Resonance, Vol. 6, L. Berliner and J. Reuben, eds, Plenum, New York (1984), p.153.Google Scholar
  9. 9.
    Linden and A.G. Ferringe (1979) J. Mag. Res. 36, 277–280.CrossRefGoogle Scholar
  10. 10.
    Darlison and J.R. Guest (1984) Biochem. J. 223, 507–517.Google Scholar
  11. 11.
    Wood, M.G. Darlison, R.J. Wilde and J.R. Guest (1984) Biochem J. 222 , 519–534.Google Scholar
  12. 12.
    Cole, S.T., Grundstrom, T., Jaurin, B., Robinson, J.J. and Weiner J. H. (1982) Eur. J. Biochem. 126, 211–216.CrossRefGoogle Scholar
  13. 13.
    Cole, S.T. (1982) Eur. J. Biochem. 122, 479–484.CrossRefGoogle Scholar
  14. 14.
    Tsukihara, T., Kobayashi, M., Nakamura, M., Katsube, Y., Hase, T. Wada, K. and Matsubara, H. (1982) Biosystems (15), 243–257.CrossRefGoogle Scholar
  15. 15.
    L. Dederstedt, J.J. Maguire, A.J. Waring and T. Ohnishi (1985) J. Biol. Chem. 260, 5554–5562.Google Scholar
  16. 16.
    W.B. Mims and J. Peisach (1978) J. Chem. Phys. 69, 4921–4930.CrossRefGoogle Scholar
  17. 17.
    Salerno, J.C., Lim, J., King, T.E., Blum, H., and Ohnishi, T. (1979) J. Biol. Chem. 254, 4828–4835.Google Scholar

Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Russell LoBrutto
    • 1
  • Paul E. Haley
    • 1
    • 2
  • Chang-An Yu
    • 1
    • 2
  • Tomoko Ohnishi
    • 1
  1. 1.Department of Biochemistry and BiophysicsUniversity of PennsylvaniaPhiladelphiaUSA
  2. 2.Department of BiochemistryOklahoma State UniversityStillwaterUSA

Personalised recommendations