Skip to main content
SpringerLink
Log in

Engineering of protein bound iron-sulfur clusters

A tool for the study of protein and cluster chemistry and mechanism of iron-sulfur enzymes

  • Chapter
EJB Reviews 1989

Part of the book series: EJB Reviews ((EJB REVIEWS,volume 1989))

  • 115 Accesses

Abstract

An increasing number of iron-sulfur (Fe-S) proteins are found in which the Fe-S cluster is not involved in net electron transfer, as it is in the majority of Fe-S proteins. Most of the former are (de)hydratases, of which the most extensively studied is aconitase. Approaches are described and discussed by which the Fe-S cluster of this enzyme could be brought into states of different structure, ligation, oxidation and isotope composition. The species, so obtained, provided the basis for spectroscopic and chemical investigations. Results from studies by protein chemistry, EPR, Mössbauer, 1H, 2H and 57Fe electron-nuclear double resonance spectroscopy are described. Conclusions, which bear on the electronic structure of the Fe-S cluster, enzyme-substrate interaction and the enzymatic mechanism, were derived from a synopsis of the recent work described here and of previous contributions from several laboratories. These conclusions are discussed and summarized in a final section.

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

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 84.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 109.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

Abbreviations

ENDOR:

electron-nuclear double resonance

References

  1. Adams, M. W. W. & Mortenson, L. E. (1984) J. Biol. Chem. 259, 7045–7055.

    CAS  PubMed  Google Scholar 

  2. Kuchta, R. D., Hanson, G. R., Holmquist, B. & Abeles, R. H. (1986) Biochemistry 25, 7301–7307.

    Article  CAS  PubMed  Google Scholar 

  3. Scopes, R. K. & Griffiths-Smith, K. (1984) Anal. Biochem. 136, 530–534.

    Article  CAS  PubMed  Google Scholar 

  4. Kelly, J. M. & Scopes, R. K. (1986) FEBS Lett. 202, 274–276.

    Article  CAS  Google Scholar 

  5. Dreyer, J.-L. (1985) Eur. J. Biochem. 150, 145–154.

    Article  CAS  PubMed  Google Scholar 

  6. Schweiger, G., Dutscho, R. & Buckel, W. (1987) Eur. J. Biochem. 169, 441–448.

    Article  CAS  PubMed  Google Scholar 

  7. Flint, D. H. & Emptage, M. H. (1988) J. Biol. Chem. 263, 3558–3564.

    CAS  PubMed  Google Scholar 

  8. Emptage, M. H. (1988) Biochemistry 27, 3104.

    Google Scholar 

  9. Kent, T. A., Dreyer, J.-L., Kennedy, M. C., Huynh, B. H., Emptage, M. H., Beinert, H. & Münck, E. (1982) Proc. Natl Acad. Sci. USA 79, 1096–1100.

    Article  CAS  PubMed  Google Scholar 

  10. Martius C. (1937) Z. Physiol. Chem. 247, 104–110.

    Article  CAS  Google Scholar 

  11. Kennedy, C., Rauner, R. & Gawron, O. (1972) Biochem. Biophys. Res. Commun. 47, 740–745.

    Article  CAS  PubMed  Google Scholar 

  12. Ruzicka, F. J. & Beinert, H. (1978) J. Biol. Chem. 253, 2514–2517.

    CAS  PubMed  Google Scholar 

  13. Kennedy, M. C., Emptage, M. H., Dreyer, J.-L. & Beinert, H. (1983) J. Biol. Chem. 258, 11098–11105.

    CAS  PubMed  Google Scholar 

  14. Beinert, H., Emptage, M. H., Dreyer, J.-L., Scott, R. A., Hahn, J. E., Hodgson, K. O. & Thomson, A. J. (1983) Proc. Natl Acad. Sci. USA 80, 393–396.

    Article  CAS  PubMed  Google Scholar 

  15. Emptage, M. H., Dreyer, J.-L., Kennedy, M. C. & Beinert, H. (1983) J. Biol. Chem. 258, 11106–11 111.

    CAS  PubMed  Google Scholar 

  16. Robbins, A. H. & Stout, C. D. (1989) Proteins, structure, function and genetics 5, 289–312.

    Article  CAS  Google Scholar 

  17. Robbins, A. H. & Stout, C. D. (1989) Procl. Natl Acad. Sci. USA 86, 3639–3643.

    Article  CAS  Google Scholar 

  18. Kennedy, M. C., Kent, T. A., Emptage, M. H., Merkle, H., Beinert, H. & Münck, E. (1984) J. Biol. Chem. 259, 14463–14471.

    PubMed  Google Scholar 

  19. Piszkiewicz, D. (1982) Fed. Proc. 41, 890.

    Google Scholar 

  20. Plank, D. W., Kennedy, M. C., Beinert, H. & Howard, J. B. (1989) J. Biol. Chem., in the press.

    Google Scholar 

  21. Kennedy, M. C., Emptage, M. H. & Beinert, H. (1984) J. Biol. Chem. 259, 3145–3151.

    CAS  PubMed  Google Scholar 

  22. Emptage, M. H., Kent, T. A., Kennedy, M. C., Beinert, H. & Münck, E. (1983) Proc. Natl Acad. Sci. USA 80, 4674–4678.

    Article  CAS  PubMed  Google Scholar 

  23. Rabinowitz, J. C. (1972) Methods Enzymol. 24, 440–442.

    Google Scholar 

  24. Kennedy, M. C. & Beinert, H. (1988) J. Biol. Chem. 263, 8194–8198.

    CAS  PubMed  Google Scholar 

  25. Petering, D., Fee, J. A. & Palmer, G. (1971) J. Biol. Chem. 246, 643–653.

    CAS  PubMed  Google Scholar 

  26. Thomson, A. J. (1985) in Top. Mol. Struct. Biol. 6, 79–120.

    CAS  Google Scholar 

  27. Moulis, J.-M. & Meyer, J. (1982) Biochemistry 21, 4762–4771.

    Article  CAS  PubMed  Google Scholar 

  28. Tsibris, J. C. M., Namtvedt, M. J. & Gunsalus, I. C. (1968) Biochem. Biophys. Res. Commun. 30, 323–327.

    Article  CAS  PubMed  Google Scholar 

  29. Wood, J. L. (1987) Methods Enzymol. 143, 25–29.

    CAS  PubMed  Google Scholar 

  30. Rydén, L., Öfverstedt, L.-G., Beinert, H., Emptage, H. H. & Kennedy, M. C. (1984) J. Biol. Chem. 259, 3141–3144.

    PubMed  Google Scholar 

  31. Plank, D. W. & Howard, J. B. (1988) J. Biol. Chem. 263, 8184–8189.

    CAS  PubMed  Google Scholar 

  32. Hagen, K. S., Watson, A. D. & Holm, R. H. (1983) J. Am. Chem. Soc. 705, 3905–3913.

    Article  Google Scholar 

  33. Hausinger, R. P. & Howard, J. B. (1983) J. Biol. Chem. 258, 13486–13492.

    CAS  PubMed  Google Scholar 

  34. Martin, A. E., Burgess, B. K., Stout, C. D., Cash, V., Dean, D. R., Jensen, G. & Stephens, P. J. (1989) Proc. Natl Acad. Sci. USA, in the press.

    Google Scholar 

  35. Girerd, J.-J., Papaefthymiou, G. C., Watson, A. D., Gamp, E., Hagen, K. S., Edelstein, N., Frankel, R. B. & Holm, R. H. (1984) J. Am. Chem. Soc. 106, 5941–5947.

    Article  CAS  Google Scholar 

  36. Dreyer, J.-L., Beinert, H., Keana, J. F. W., Hankovszky, O. H., Hideg, K., Eaton, S. S. & Eaton, G. R. (1983) Biochim. Biophys. Acta 745, 229–236.

    Article  CAS  PubMed  Google Scholar 

  37. Kennedy, M. C., Spoto, G., Emptage, M. H. & Beinert, H. (1988) J. Biol. Chem. 263, 8190–8193.

    CAS  PubMed  Google Scholar 

  38. Kent, T. A., Emptage, M. H., Merkle H., Kennedy, M. C., Beinert, H. & Münck, E. (1985) J. Biol. Chem. 260, 6871–6881.

    CAS  PubMed  Google Scholar 

  39. Cammack, R., Dickson, D. P. E. & Johnson, C. E. (1977) in Iron-sulfur proteins (Lovenberg, W., ed.) vol. 3, pp. 283–330, Academic Press, New York.

    Google Scholar 

  40. Debrunner, P. G., Münck, E., Que, L. & Schulz, C. E. (1977) in Iron-sulfur proteins (Lovenberg, W., ed.) vol. 3, pp. 381–417, Academic Press, New York.

    Google Scholar 

  41. Bill, E., Haas, C., Ding, X.-Q., Maret, W., Winkler, H. & Trautwein, A. C. (1989) Eur. J. Biochem. 180, 111–121.

    Article  CAS  PubMed  Google Scholar 

  42. Robin, M. D. & Day, P. (1967) Adv. Inorg. Chem. Radiochem. 10, 247–405.

    CAS  Google Scholar 

  43. Münck, E., Debrunner, P. G., Tsibris, J. C. M. & Gunsalus, I. C. (1972) Biochemistry 11, 855–863.

    Article  PubMed  Google Scholar 

  44. Rius, G. & Lamotte, B. (1989) J. Am. Chem. Soc. 111, 2464–2469.

    Article  CAS  Google Scholar 

  45. Kanatzidis, M. G., Ryan, M., Coucouvanis, D., Simopoulos, A. & Kostikas, A. (1983) Inorg. Chem. 22, 179–182.

    Article  CAS  Google Scholar 

  46. Johnson, R. E., Papaefthymiou, G. C., Frankel, R. B. & Holm, R. H. (1983) J. Am. Chem. Soc. 105, 7280–7287.

    Article  CAS  Google Scholar 

  47. Noodleman, L., Norman, J. G. Jr, Osborne, J. H., Aizman A. & Case, D. A. (1985) J. Am. Chem. Soc. 107, 3418–3426.

    Article  CAS  Google Scholar 

  48. Meyer, J., Gaillard, J. & Moulis, J.-M. (1988) Biochemistry 27, 6150–6156.

    Article  CAS  PubMed  Google Scholar 

  49. Schloss, J. V., Porter, D. J. D., Bright, H. J. & Cleland, W. W. (1980) Biochemistry 19, 2358–2362.

    Article  CAS  PubMed  Google Scholar 

  50. Telser, J., Emptage, M. H., Merkle, H., Kennedy, M. C., Beinert, H. & Hoffman, B. M. (1986) J. Biol. Chem. 261, 4840–4846.

    CAS  PubMed  Google Scholar 

  51. Kennedy, M. C., Werst, M., Telser, J., Emptage, M. H., Beinert, H. & Hoffman, B. M. (1987) Proc. Natl Acad. Sci. USA 84, 8854–8858.

    Article  CAS  PubMed  Google Scholar 

  52. Rose, I. A. & O’Connell, E. L. (1967) J. Biol. Chem. 242, 1870–1879.

    CAS  PubMed  Google Scholar 

  53. Gawron, O., Glaid, A. J. & Fondy, T. P. (1961) J. Am. Chem. Soc. 83, 3634–3640.

    Article  CAS  Google Scholar 

  54. Münck, E. & Kent, T. A. (1986) Hyperfine Interactions 27, 161–172.

    Article  Google Scholar 

  55. Noodleman, L. (1988) Inorg. Chem. 27, 3677–3679.

    Article  CAS  Google Scholar 

  56. Noodleman, I., Case, D. A. & Aizman, A. (1988) J. Am. Chem. Soc. 110, 1001–1005.

    Article  CAS  Google Scholar 

  57. Orme-Johnson, W. H., Hansen, R. E., Beinert, H., Tsibris, J. C. M., Bartholomaus, R. C. & Gunsalus, I. C. (1968) Proc. Natl Acad Sci. USA 60, 368–372.

    Article  CAS  PubMed  Google Scholar 

  58. Schloss, J. V., Emptage, M. H. & Cleland, W. W. (1984) Biochemistry 23, 4572–4580.

    Article  CAS  PubMed  Google Scholar 

  59. Gahan, L. R., Harrowfield, J. M., Herlt, A. J., Lindoy, L. F., Whimp, P. O. & Sargeson, A. M. (1985) J. Am. Chem. Soc. 107, 6231–6242.

    Article  CAS  Google Scholar 

  60. Glusker, J. P. (1980) Acc. Chem. Res. 13, 345–352.

    Article  CAS  Google Scholar 

  61. Emptage, M. H. (1988) in Metal clusters in proteins (Que, L. Jr, ed.) ACS Symposium Series 372, pp. 343–371, Am. Chem. Soc. Washington, DC.

    Chapter  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Biochemistry, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, Wisconsin, 53226, USA

    Helmut Beinert & Mary Claire Kennedy

  2. National Biomedical ESR Center, Medical College of Wisconsin, Milwaukee, Wisconsin, USA

    Helmut Beinert

Authors
  1. Helmut Beinert
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Mary Claire Kennedy
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

Copyright information

© 1989 Springer-Verlag Berlin Heidelberg

About this chapter

Cite this chapter

Beinert, H., Kennedy, M.C. (1989). Engineering of protein bound iron-sulfur clusters. In: EJB Reviews 1989. EJB Reviews, vol 1989. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-75189-9_11

Download citation

  • DOI: https://doi.org/10.1007/978-3-642-75189-9_11

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-75191-2

  • Online ISBN: 978-3-642-75189-9

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation