Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1982 Jun;150(3):1091–1097. doi: 10.1128/jb.150.3.1091-1097.1982

Nitrate reductase from Rhodopseudomonas sphaeroides.

N L Kerber, J Cardenas
PMCID: PMC216327  PMID: 6978883

Abstract

The facultative phototroph Rhodopseudomonas sphaeroides DSM158 was incapable of either assimilating or dissimilating nitrate, although the organism could reduce it enzymatically to nitrite either anaerobically in the light or aerobically in the dark. Reduction of nitrate was mediated by a nitrate reductase bound to chromatophores that could be easily solubilized and functioned with chemically reduced viologens or photochemically reduced flavins as electron donors. The enzyme was solubilized, and some of its kinetic and molecular parameters were determined. It seemed to be nonadaptive, ammonia did not repress its synthesis, and its activity underwent a rapid decline when the cells entered the stationary growth phase. Studies with inhibitors and with metal antagonists indicated that molybdenum and possibly iron participate in the enzymatic reduction of nitrate. The conjectural significance of this nitrate reductase in phototrophic bacteria is discussed.

Full text

PDF
1091

Selected References

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

  1. Alef K., Klemme J. H. Assimilatory nitrate reductase of Rhodopseudomonas capsulata AD2: a molybdo-hemeprotein. Z Naturforsch C. 1979 Jan-Feb;34(1-2):33–37. doi: 10.1515/znc-1979-1-210. [DOI] [PubMed] [Google Scholar]
  2. Alef K., Klemme J. H. Characterization of a soluble NADH-independent nitrate reductase from the photosynthetic bacterium Rhodopseudomonas capsulata. Z Naturforsch C. 1977 Nov-Dec;32(11-12):954–956. doi: 10.1515/znc-1977-11-1213. [DOI] [PubMed] [Google Scholar]
  3. Daniel R. M., Gray J. Nitrate reductase from anaerobically grown Rhizobium japonicum. J Gen Microbiol. 1976 Oct;96(2):247–251. doi: 10.1099/00221287-96-2-247. [DOI] [PubMed] [Google Scholar]
  4. Guerrero M. G., Vega J. M., Leadbetter E., Losada M. Preparation and characterization of a soluble nitrate reductase from Azotobacter chroococcum. Arch Mikrobiol. 1973 Jun 25;91(4):287–304. doi: 10.1007/BF00425049. [DOI] [PubMed] [Google Scholar]
  5. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  6. MARTIN R. G., AMES B. N. A method for determining the sedimentation behavior of enzymes: application to protein mixtures. J Biol Chem. 1961 May;236:1372–1379. [PubMed] [Google Scholar]
  7. Malofeeva I. V., Bogorov L. V., Gogotov I. N. Ispol'zovanie nitratov purpurnymi bakteriiami. Mikrobiologiia. 1974 Nov-Dec;43(6):967–972. [PubMed] [Google Scholar]
  8. Neilson A. H., Nordlund S. Regulation of nitrogenase synthesis in intact cells of Rhodospirillum rubrum: inactivation of nitrogen fixation by ammonia, L-glutamine and L-asparagine. J Gen Microbiol. 1975 Nov;91(1):53–62. doi: 10.1099/00221287-91-1-53. [DOI] [PubMed] [Google Scholar]
  9. Paneque A., Del Campo F. F., Ramírez J. M., Losada M. Flavin nucleotide nitrate reductase from spinach. Biochim Biophys Acta. 1965 Sep 27;109(1):79–85. doi: 10.1016/0926-6585(65)90092-0. [DOI] [PubMed] [Google Scholar]
  10. Rigaud J., Puppo A. Effect of nitrite upon leghemoglobin and interaction with nitrogen fixation. Biochim Biophys Acta. 1977 May 26;497(3):702–706. doi: 10.1016/0304-4165(77)90291-4. [DOI] [PubMed] [Google Scholar]
  11. Siegel L. M., Monty K. J. Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of sulfite and hydroxylamine reductases. Biochim Biophys Acta. 1966 Feb 7;112(2):346–362. doi: 10.1016/0926-6585(66)90333-5. [DOI] [PubMed] [Google Scholar]
  12. Villalobo A., Roldán J. M., Rivas J., CárdenasJ Assimilatory nitrate reductase from Acinetobacter calcoaceticus. Arch Microbiol. 1977 Mar 1;112(2):127–132. doi: 10.1007/BF00429324. [DOI] [PubMed] [Google Scholar]

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

RESOURCES