Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1961 Jul;82(1):130–134. doi: 10.1128/jb.82.1.130-134.1961

EFFECT OF TUNGSTATE ON THE UPTAKE AND FUNCTION OF MOLYBDATE IN AZOTOBACTER AGILIS

William A Bulen 1
PMCID: PMC279125  PMID: 16561910

Abstract

Bulen, William A. (Charles F. Kettering Foundation, Yellow Springs, Ohio). Effect of tungstate on the uptake and function of molybdate in Azotobacter agilis. J. Bacteriol. 82:130–134. 1961.—The reported competitive inhibition of molybdate by tungstate was investigated in an effort to elucidate molybdenum functions associated with nitrogen fixation by Azotobacter agilis (A. vinelandii). Growth, respiration, and N215-incorporation experiments with normal and molybdenum-deficient cells indicated that tungstate inhibits the uptake of molybdate but does not compete with the metabolically functional molybdenum of cells metabolizing N2. Neither a molybdenum requirement nor a tungstate inhibition was observed with cells metabolizing urea.

Full text

PDF
130

Selected References

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

  1. Burk D., Lineweaver H. THE INFLUENCE OF FIXED NITROGEN ON AZOTOBACTER. J Bacteriol. 1930 Jun;19(6):389–414. doi: 10.1128/jb.19.6.389-414.1930. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. ESPOSITO R. G., WILSON P. W. Trace metal requirements of Azotobacter. Proc Soc Exp Biol Med. 1956 Dec;93(3):564–567. doi: 10.3181/00379727-93-22820. [DOI] [PubMed] [Google Scholar]
  3. HIGGINS E. S., RICHERT D. A., WESTERFELD W. W. Molybdenum deficiency and tungstate inhibition studies. J Nutr. 1956 Aug 10;59(4):539–559. doi: 10.1093/jn/59.4.539. [DOI] [PubMed] [Google Scholar]
  4. HIGGINS E. S., RICHERT D. A., WESTERFELD W. W. Tungstate antagonism of molybdate in Aspergillus niger. Proc Soc Exp Biol Med. 1956 Jul;92(3):509–511. doi: 10.3181/00379727-92-22527. [DOI] [PubMed] [Google Scholar]
  5. KEELER R. F. Influence of culture conditions on uptake and distribution of molybdenum in Azotobacter vinelandii. J Bacteriol. 1957 Apr;73(4):582–583. doi: 10.1128/jb.73.4.582-583.1957. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. KEELER R. F., VARNER J. E. Tungstate as an antagonist of molybdate in Azotobacter vinelandii. Arch Biochem Biophys. 1957 Aug;70(2):585–590. doi: 10.1016/0003-9861(57)90146-7. [DOI] [PubMed] [Google Scholar]
  7. LENHOFF H. M., NICHOLAS D. J., KAPLAN N. O. Effects of oxygen, iron, and molybdenum on routes of electron transfer in Pseudomonas fluorescens. J Biol Chem. 1956 Jun;220(2):983–995. [PubMed] [Google Scholar]
  8. MAHLER H. R., MACKLER B., GREEN D. E. Studies on metalloflavoproteins. III. Aldehyde oxidase: a molybdoflavoprotein. J Biol Chem. 1954 Sep;210(1):465–480. [PubMed] [Google Scholar]
  9. NICHOLAS D. J., NASON A. Mechanism of action of nitrate reductase from Neurospora. J Biol Chem. 1954 Nov;211(1):183–197. [PubMed] [Google Scholar]
  10. RICHERT D. A., WESTERFELD W. W. Isolation and identification of the xanthine oxidase factor as molybdenum. J Biol Chem. 1953 Aug;203(2):915–923. [PubMed] [Google Scholar]
  11. TAKAHASHI H., NASON A. Tungstate as competitive inhibitor of molybdate in nitrate assimilation and in N2 fixation by Azotobacter. Biochim Biophys Acta. 1957 Feb;23(2):433–435. doi: 10.1016/0006-3002(57)90351-7. [DOI] [PubMed] [Google Scholar]
  12. TOTTER J. R., BURNETT W. T., Jr, MONROE R. A., WHITNEY I. B., COMAR C. L. Evidence that molybdenum is a nondialyzable component of xanthine oxidase. Science. 1953 Nov 6;118(3071):555–555. doi: 10.1126/science.118.3071.555. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES