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.
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- 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]