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. 1981 Feb;145(2):743–751. doi: 10.1128/jb.145.2.743-751.1981

Molybdenum accumulation and storage in Klebsiella pneumoniae and Azotobacter vinelandii.

P T Pienkos, W J Brill
PMCID: PMC217174  PMID: 7007348

Abstract

In Klebsiella pneumoniae, Mo accumulation appeared to be coregulated with nitrogenase synthesis. O2 and NH+4, which repressed nitrogenase synthesis, also prevented Mo accumulation. In Azotobacter vinelandii, Mo accumulation did not appear to be regulated Mo was accumulated to levels much higher than those seen in K. pneumoniae even when nitrogenase synthesis was repressed. Accumulated Mo was bound mainly to a Mo storage protein, and it could act as a supply for the Mo needed in component I synthesis when extracellular Mo had been exhausted. When A. vinelandii was grown in the presence of WO2-(4) rather than MoO2-(4), it synthesized a W-containing analog of the Mo storage protein. The Mo storage protein was purified from both NH+4 and N2-grown cells of A. vinelandii and found to be a tetramer of two pairs of different subunits binding a minimum of 15 atoms of Mo per tetramer.

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Selected References

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

  1. Benemann J. R., Smith G. M., Kostel P. J., McKenna C. E. Tungsten incorporation into Azotobacter vinelandii nitrogenase. FEBS Lett. 1973 Feb 1;29(3):219–221. doi: 10.1016/0014-5793(73)80023-7. [DOI] [PubMed] [Google Scholar]
  2. Brill W. J., Steiner A. L., Shah V. K. Effect of molybdenum starvation and tungsten on the synthesis of nitrogenase components in Klebsiella pneumonia. J Bacteriol. 1974 Jun;118(3):986–989. doi: 10.1128/jb.118.3.986-989.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Brill W. J., Westphal J., Stieghorst M., Davis L. C., Shah V. K. Detection of nitrogenase components and other nonheme iron proteins in polyacrylamide gels. Anal Biochem. 1974 Jul;60(1):237–241. doi: 10.1016/0003-2697(74)90149-3. [DOI] [PubMed] [Google Scholar]
  4. Cardenas J., Mortenson L. E. Determination of molybdenum and tungsten in biological materials. Anal Biochem. 1974 Aug;60(2):372–381. doi: 10.1016/0003-2697(74)90244-9. [DOI] [PubMed] [Google Scholar]
  5. DE WITT C. W., ROWE J. A. N,O-Diacetylneuraminic acid and N-acetylneuraminic acid in Escherichia coli. Nature. 1959 Aug 1;184(Suppl 6):381–382. doi: 10.1038/184381b0. [DOI] [PubMed] [Google Scholar]
  6. Elliott B. B., Mortenson L. E. Transport of molybdate by Clostridium pasteurianum. J Bacteriol. 1975 Dec;124(3):1295–1301. doi: 10.1128/jb.124.3.1295-1301.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Mortenson L. E., Thorneley R. N. Structure and function of nitrogenase. Annu Rev Biochem. 1979;48:387–418. doi: 10.1146/annurev.bi.48.070179.002131. [DOI] [PubMed] [Google Scholar]
  8. Nagatani H. H., Brill W. J. Nitrogenase V. The effect of Mo, W and V on the synthesis of nitrogenase components in Azotobacter vinelandii. Biochim Biophys Acta. 1974 Aug 7;362(1):160–166. doi: 10.1016/0304-4165(74)90037-3. [DOI] [PubMed] [Google Scholar]
  9. Pienkos P. T., Shah V. K., Brill W. J. Molybdenum cofactors from molybdoenzymes and in vitro reconstitution of nitrogenase and nitrate reductase. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5468–5471. doi: 10.1073/pnas.74.12.5468. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. ROBRISH S. A., MARR A. G. Location of enzymes in Azotobacteragilis. J Bacteriol. 1962 Jan;83:158–168. doi: 10.1128/jb.83.1.158-168.1962. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Rawlings J., Shah V. K., Chisnell J. R., Brill W. J., Zimmermann R., Münck E., Orme-Johnson W. H. Novel metal cluster in the iron-molybdenum cofactor of nitrogenase. Spectroscopic evidence. J Biol Chem. 1978 Feb 25;253(4):1001–1004. [PubMed] [Google Scholar]
  12. Shah V. K., Brill W. J. Isolation of an iron-molybdenum cofactor from nitrogenase. Proc Natl Acad Sci U S A. 1977 Aug;74(8):3249–3253. doi: 10.1073/pnas.74.8.3249. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Shah V. K., Brill W. J. Nitrogenase. IV. Simple method of purification to homogeneity of nitrogenase components from Azotobacter vinelandii. Biochim Biophys Acta. 1973 May 30;305(2):445–454. doi: 10.1016/0005-2728(73)90190-4. [DOI] [PubMed] [Google Scholar]
  14. Shah V. K., Brill W. J. Nitrogenase. IV. Simple method of purification to homogeneity of nitrogenase components from Azotobacter vinelandii. Biochim Biophys Acta. 1973 May 30;305(2):445–454. doi: 10.1016/0005-2728(73)90190-4. [DOI] [PubMed] [Google Scholar]
  15. Shah V. K., Chisnell J. R., Brill W. J. Acetylene reduction by the iron-molybdenum cofactor from nitrogenase. Biochem Biophys Res Commun. 1978 Mar 15;81(1):232–236. doi: 10.1016/0006-291x(78)91654-6. [DOI] [PubMed] [Google Scholar]
  16. St John R. T., Shah V. K., Brill W. J. Regulation of nitrogenase synthesis by oxygen in Klebsiella pneumoniae. J Bacteriol. 1974 Jul;119(1):266–269. doi: 10.1128/jb.119.1.266-269.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Strandberg G. W., Wilson P. W. Formation of the nitrogen-fixing enzyme system in Azotobacter vinelandii. Can J Microbiol. 1968 Jan;14(1):25–31. doi: 10.1139/m68-005. [DOI] [PubMed] [Google Scholar]
  18. Yoch D. C., Pengra R. M. Effect of amino acids on the nitrogenase system of Klebsiella pneumoniae. J Bacteriol. 1966 Sep;92(3):618–622. doi: 10.1128/jb.92.3.618-622.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]

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