Abstract
Klebsiella pneumoniae M5a1 grows well in the presence or absence of molybdenum in media containing excess NH4+. However, growth on N2 is completely dependent on the presence of molybdenum in the medium. Tungstate competes with the molybdate requirement during growth on N2. In molybdenum-depleted medium, neither protein component of nitrogenase is active and neither component can be detected antigenically. These data provide evidence that molybdenum is an inducer of nitrogenase synthesis.
Full text
PDF
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- 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]
- Bulen W. A., LeComte J. R. The nitrogenase system from Azotobacter: two-enzyme requirement for N2 reduction, ATP-dependent H2 evolution, and ATP hydrolysis. Proc Natl Acad Sci U S A. 1966 Sep;56(3):979–986. doi: 10.1073/pnas.56.3.979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Burns R. C., Holsten R. D., Hardy R. W. Isolation by crystallization of the Mo-Fe protein of Azotobacter nitrogenase. Biochem Biophys Res Commun. 1970 Apr 8;39(1):90–99. doi: 10.1016/0006-291x(70)90762-x. [DOI] [PubMed] [Google Scholar]
- Dalton H., Morris J. A., Ward M. A., Mortenson L. E. Purification and some properties of molybdoferredoxin, a component of nitrogenase from Clostridium pasteurianum. Biochemistry. 1971 May 25;10(11):2066–2072. doi: 10.1021/bi00787a016. [DOI] [PubMed] [Google Scholar]
- Davis L. C., Shah V. K., Brill W. J., Orme-Johnson W. H. Nitrogenase. II. Changes in the EPR signal of component I (iron-molybdenum protein) of Azotobacter vinelandii nitrogenase during repression and derepression. Biochim Biophys Acta. 1972 Feb 28;256(2):512–523. doi: 10.1016/0005-2728(72)90079-5. [DOI] [PubMed] [Google Scholar]
- Dilworth M. J. Acetylene reduction by nitrogen-fixing preparations from Clostridium pasteurianum. Biochim Biophys Acta. 1966 Oct 31;127(2):285–294. doi: 10.1016/0304-4165(66)90383-7. [DOI] [PubMed] [Google Scholar]
- 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]
- Gasper E., Heimsch R. C., Anderson A. W. Quantitative detection of type A staphylococcal enterotoxin by Laurell electroimmunodiffusion. Appl Microbiol. 1973 Mar;25(3):421–426. doi: 10.1128/am.25.3.421-426.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- 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]
- Laurell C. B. Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies. Anal Biochem. 1966 Apr;15(1):45–52. doi: 10.1016/0003-2697(66)90246-6. [DOI] [PubMed] [Google Scholar]
- Shah V. K., Davis L. C., Brill W. J. Nitrogenase. I. Repression and derepression of the iron-molybdenum and iron proteins of nitrogenase in Azotobacter vinelandii. Biochim Biophys Acta. 1972 Feb 28;256(2):498–511. doi: 10.1016/0005-2728(72)90078-3. [DOI] [PubMed] [Google Scholar]
- 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]