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Dependence of oxygen-tolerant nitrogenase activity on divalent cations in Azotobacter vinelandii
- Source :
- Journal of Bacteriology. 174:3399-3402
- Publication Year :
- 1992
- Publisher :
- American Society for Microbiology, 1992.
-
Abstract
- Nitrogenase activity of washed Azotobacter vinelandii cells was enhanced by the addition of Ca2+ and Mg2+, and the enhancement increased with the O2 concentration. In assays provided with a level of O2 that was initially supraoptimal and inhibitory to nitrogenase activity, the addition of Ca2+ or Mg2+ affected both the maximum respiration rate (Vmax) of the cells and the apparent affinity [KS(O2)] of cell respiration for O2. Changes in these parameters correlated with changes in nitrogenase activity. Aeration-dependent increases in Vmax and KS(O2) were inhibited by rifampin and chloramphenicol and were also observed in ammonium-grown cultures.
- Subjects :
- Cations, Divalent
Cellular respiration
Microbiology
Divalent
Oxygen Consumption
Nitrogen Fixation
Nitrogenase
Magnesium
Molecular Biology
Azotobacteraceae
chemistry.chemical_classification
Azotobacter vinelandii
biology
Acetylene
biology.organism_classification
Oxygen
Quaternary Ammonium Compounds
Chloramphenicol
Enzyme
chemistry
Biochemistry
Nitrogen fixation
Calcium
Rifampin
Respiration rate
Oxidation-Reduction
Research Article
Subjects
Details
- ISSN :
- 10985530 and 00219193
- Volume :
- 174
- Database :
- OpenAIRE
- Journal :
- Journal of Bacteriology
- Accession number :
- edsair.doi.dedup.....44ae07e323dd133303be4c7c1311761c
- Full Text :
- https://doi.org/10.1128/jb.174.10.3399-3402.1992