Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Letter
  • Published:

The alternative nitrogenase of Azotobacter chroococcum is a vanadium enzyme

Nature volume 322, pages 388–390 (1986)Cite this article

Abstract

The requirement for molybdenum in biological dinitrogen fixation, first reported by Bortels1, is due to its involvement at or near the site of reduction of N2 in conventional nitrogenase. To date, all nitrogenases which have been purified to homogeneity consist of an iron protein (component 2) and a molybdoprotein (component 1)2. Azotobacter vinelandii, an obligately aerobic diazotrophic bacterium, has two systems for nitrogen fixation: a conventional nitrogenase involving molybdenum and an alternative system which functions under conditions of Mo deficiency and does not require the structural genes for conventional nitrogenase3–6. The properties of the nitrogenase in extracts of comparable deletion strains of A. vinelandii are consistent with a two-component system6,7 in which the component 1-containing fraction has no detectable Mo (ref. 6). Recently, an alternative nitrogen fixation system has been demonstrated in Azotobacter chroococcum strain MCD1155, in which the structural genes for conventional nitrogenase are deleted8. We demonstrate here that nitrogen fixation by this strain depends on vanadium and we show that its purified nitrogenase is a binary system in which the conventional molybdoprotein is replaced by a vanadoprotein.

This is a preview of subscription content, access via your institution

Access options

Buy this article

  • Purchase on Springer Link
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

Similar content being viewed by others

References

  1. Bortels, H. Arch. Mikrobiol. 1, 333–342 (1930).

    Article  CAS  Google Scholar 

  2. Burgess, B. K. in Advances in Nitrogen Fixation Research (eds Veeger, C. & Newton, W. E.) 103–114 (Nijhoff/Junk, Pudoc, 1984).

    Book  Google Scholar 

  3. Bishop, P. E., Jarlneski, D. M. L. & Hetherington, D. R. Proc. natn. Acad. Sci. U.S.A. 77, 7342–7346 (1980).

    Article  ADS  CAS  Google Scholar 

  4. Bishop, P. E., Jarlenski, D. M. L. & Hetherington, D. R. J. Bact. 150, 1244–1251 (1982).

    CAS  PubMed  Google Scholar 

  5. Bishop, P. E. & Eady, R. R. in Nitrogen Fixation Research Progress (eds Evans, H. J., Bottomley, P. J. & Newton, W. E.) 622 (Nijhoff, Dordrecht, 1985).

  6. Hales, B. J., Case, E. E. & Langosch, D. in Nitrogen Fixation Research Progress (eds Evans, H. J., Bottomley, P. J. & Newton, W. E.) 612 (Nijhoff, Dordrecht, 1985).

    Google Scholar 

  7. Chisnell, J. R. & Bishop, P. E. in Nitrogen Fixation Research Progress (eds Evans, H. J., Bottomley, P. J. & Newton, W. E.) 623 (Nijhoff, Dordrecht, 1985).

    Google Scholar 

  8. Robson, R. L. Archiv. Microbiol. (in the press).

  9. Yates, M. G. & Planqué, K. Eur. J. Biochem. 60, 467–476 (1975).

    Article  CAS  Google Scholar 

  10. Jones, R., Woodley, P. R. & Robson, R. L. Molec. gen. Genet. 197, 318–327 (1984).

    Article  CAS  Google Scholar 

  11. Takahashi, H. & Nason, A. Biochim. biophys. Acta 23, 433–435 (1957).

    Article  CAS  Google Scholar 

  12. Keeler, R. F. & Varner, J. E. Archs Biochem. Biophys. 70, 585–590 (1957).

    Article  CAS  Google Scholar 

  13. Bortels, H. Zentre. Bakteriol. Parasitenk. Abt. II 95, 193–218 (1936).

    CAS  Google Scholar 

  14. Nicholas, D. J. D., Fisher, D. J., Redmond, W. J. & Wright, M. A. J. gen. Microbiol. 22, 191–205 (1960).

    Article  CAS  Google Scholar 

  15. Becking, J. H. Pl. Soil 2, 171–201 (1962).

    Article  Google Scholar 

  16. McKenna, C. E., Benemann, J. R. & Traylor, T. C. Biochem. biophys. Res. Commun. 41, 1501–1508 (1970).

    Article  CAS  Google Scholar 

  17. Burns, R. C., Fuchsman, W. H. & Hardy, R. W. F. Biochem. biophys. Res. Commun. 42, 353–358 (1971).

    Article  CAS  Google Scholar 

  18. Benemann, J. R., McKenna, C. E., Lie, R. F., Traylor, T. G. & Kamen, M. D. Biochim. biophys. Acta 264, 25–38 (1972).

    Article  CAS  Google Scholar 

  19. Eady, R. R., Smith, B. E., Cook, K. A. & Postgate, J. R. Biochem. J. 128, 655–675 (1972).

    Article  CAS  Google Scholar 

  20. Robson, R., Woodley, P. & Jones, R. EMBO J. 5, 1159–1163.

  21. Krylova, N. B. Dokl. Mosk. Sel' Kokhoz. Akad. 84, 293–299 (1963).

    Google Scholar 

  22. Singh, N. H., Vaishampayan, A. & Singh, R. K. Biochem. biophys. Res. Commun. 81, 67–74 (1978).

    Article  CAS  Google Scholar 

  23. Bowen, H. J. M. Trace Elements in Biochemistry (Academic, London, 1966).

    Google Scholar 

  24. Denisov, N. T., Efimov, O. N., Shuvalova, N. I., Shilova, A. K. & Shilov, A. E. Russ. J. phys. Chem. 44, 1693–1694 (1970).

    Google Scholar 

  25. Nikinova, L. A., Ovcharenko, A. G., Eflmov, O. N., Avilov, V. A. & Shilov, A. E. Kin. i. Kat. 13, 1602–1603 (1972).

    Google Scholar 

  26. Eady, R. R. Meth. Enzym. 69, 751–776 (1980).

    Google Scholar 

  27. Laemmli, U. K. Nature 227, 680–685 (1970).

    Article  ADS  CAS  Google Scholar 

  28. Bulen, W. A. & Le Comte, J. R. Proc. natn. Acad. Sci. U.S.A. 51, 979–989 (1966).

    Article  ADS  Google Scholar 

  29. Jensen, H. L. & Spencer, D. Proc. Linn. Soc. N. S. Wales 72, 73–86.

Download references

Author information

Author notes

  1. Richard W. Miller: Chemistry and Biology Research Institute, Agriculture Canada, Ottawa, Canada K1A 0C6

Authors and Affiliations

  1. AFRC Unit of Nitrogen Fixation, University of Sussex, Brighton, BN1 9RQ, UK

    Robert L. Robson, Robert R. Eady, Toby H. Richardson, Richard W. Miller, Marie Hawkins & John R. Postgate

Authors
  1. Robert L. Robson
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Robert R. Eady
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Toby H. Richardson
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Richard W. Miller
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Marie Hawkins
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. John R. Postgate
    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

Robson, R., Eady, R., Richardson, T. et al. The alternative nitrogenase of Azotobacter chroococcum is a vanadium enzyme. Nature 322, 388–390 (1986). https://doi.org/10.1038/322388a0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/322388a0

This article is cited by

Comments

By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing