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. 1989 Mar 15;258(3):733–737. doi: 10.1042/bj2580733

Vanadium K-edge X-ray-absorption spectroscopy of the functioning and thionine-oxidized forms of the VFe-protein of the vanadium nitrogenase from Azotobacter chroococcum.

J M Arber 1, B R Dobson 1, R R Eady 1, S S Hasnain 1, C D Garner 1, T Matsushita 1, M Nomura 1, B E Smith 1
PMCID: PMC1138426  PMID: 2730564

Abstract

Vanadium K-edge X-ray-absorption spectra were collected for samples of thionine-oxidized, super-reduced (during enzyme turnover) and dithionite-reduced VFe-protein of the vanadium nitrogenase of Azotobacter chroococcum (Acl*). Both the e.x.a.f.s and the x.a.n.e.s. (X-ray-absorption near-edge structure) are consistent with the vanadium being present as part of a VFeS cluster; the environment of the vanadium is not changed significantly in different oxidation states of the protein. The vanadium atom is bound to three oxygen (or nitrogen), three sulphur and three iron atoms at 0.215(3), 0.231(3) and 0.275(3) nm respectively.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Arber J. M., Flood A. C., Garner C. D., Gormal C. A., Hasnain S. S., Smith B. E. Iron K-edge X-ray absorption spectroscopy of the iron-molybdenum cofactor of nitrogenase from Klebsiella pneumoniae. Biochem J. 1988 Jun 1;252(2):421–425. doi: 10.1042/bj2520421. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bishop P. E., Jarlenski D. M., Hetherington D. R. Expression of an alternative nitrogen fixation system in Azotobacter vinelandii. J Bacteriol. 1982 Jun;150(3):1244–1251. doi: 10.1128/jb.150.3.1244-1251.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bishop P. E., Premakumar R., Dean D. R., Jacobson M. R., Chisnell J. R., Rizzo T. M., Kopczynski J. Nitrogen Fixation by Azotobacter vinelandii Strains Having Deletions in Structural Genes for Nitrogenase. Science. 1986 Apr 4;232(4746):92–94. doi: 10.1126/science.232.4746.92. [DOI] [PubMed] [Google Scholar]
  4. Chisnell J. R., Premakumar R., Bishop P. E. Purification of a second alternative nitrogenase from a nifHDK deletion strain of Azotobacter vinelandii. J Bacteriol. 1988 Jan;170(1):27–33. doi: 10.1128/jb.170.1.27-33.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Eady R. R., Robson R. L., Richardson T. H., Miller R. W., Hawkins M. The vanadium nitrogenase of Azotobacter chroococcum. Purification and properties of the VFe protein. Biochem J. 1987 May 15;244(1):197–207. doi: 10.1042/bj2440197. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Eady R. R., Smith B. E., Cook K. A., Postgate J. R. Nitrogenase of Klebsiella pneumoniae. Purification and properties of the component proteins. Biochem J. 1972 Jul;128(3):655–675. doi: 10.1042/bj1280655. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hales B. J., Case E. E., Morningstar J. E., Dzeda M. F., Mauterer L. A. Isolation of a new vanadium-containing nitrogenase from Azotobacter vinelandii. Biochemistry. 1986 Nov 18;25(23):7251–7255. doi: 10.1021/bi00371a001. [DOI] [PubMed] [Google Scholar]
  8. Hales B. J., Langosch D. J., Case E. E. Isolation and characterization of a second nitrogenase Fe-protein from Azotobacter vinelandii. J Biol Chem. 1986 Nov 15;261(32):15301–15306. [PubMed] [Google Scholar]
  9. Joerger R. D., Premakumar R., Bishop P. E. Tn5-induced mutants of Azotobacter vinelandii affected in nitrogen fixation under Mo-deficient and Mo-sufficient conditions. J Bacteriol. 1986 Nov;168(2):673–682. doi: 10.1128/jb.168.2.673-682.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Morningstar J. E., Johnson M. K., Case E. E., Hales B. J. Characterization of the metal clusters in the nitrogenase molybdenum-iron and vanadium-iron proteins of Azotobacter vinelandii using magnetic circular dichroism spectroscopy. Biochemistry. 1987 Apr 7;26(7):1795–1800. doi: 10.1021/bi00381a001. [DOI] [PubMed] [Google Scholar]
  11. Orme-Johnson W. H. Molecular basis of biological nitrogen fixation. Annu Rev Biophys Biophys Chem. 1985;14:419–459. doi: 10.1146/annurev.bb.14.060185.002223. [DOI] [PubMed] [Google Scholar]
  12. Perutz M. F., Hasnain S. S., Duke P. J., Sessler J. L., Hahn J. E. Stereochemistry of iron in deoxyhaemoglobin. Nature. 1982 Feb 11;295(5849):535–538. doi: 10.1038/295535a0. [DOI] [PubMed] [Google Scholar]
  13. Smith B. E., Eady R. R., Lowe D. J., Gormal C. The vanadium-iron protein of vanadium nitrogenase from Azotobacter chroococcum contains an iron-vanadium cofactor. Biochem J. 1988 Feb 15;250(1):299–302. doi: 10.1042/bj2500299. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Smith B. E., Lowe D. J., Bray R. C. Studies by electron paramagnetic resonance on the catalytic mechanism of nitrogenase of Klebsiella pneumoniae. Biochem J. 1973 Oct;135(2):331–341. doi: 10.1042/bj1350331. [DOI] [PMC free article] [PubMed] [Google Scholar]

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