The response of Azotobacter chroococcum to oxygen: superoxide-mediated effects
- 1 November 1977
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Microbiology
- Vol. 23 (11) , 1548-1553
- https://doi.org/10.1139/m77-228
Abstract
Nitrogenase in Azotobacter chroococcum whole cells was inhibited by enzymically generated superoxide anion (O2−), hydrogen peroxide, and ethyl hydrogen peroxide. The degree of inhibition produced by O2− was related to the quantity of oxygen supplied to the organisms in continuous cultures. O2− also inhibited oxygen uptake by whole cells. These O2−-mediated inhibitions were prevented by bovine superoxide dismutase. The quantities of superoxide dismutase (SOD), and catalase associated with cells grown under varying oxygen concentrations were determined. The role of hydrogen peroxide, and of the hydroxyl radical (∙OH) in nitrogenase inhibition was examined. The response of Azotobacter chroococcum to oxygen was evaluated with respect to the observed effects of O2− on the organism, and some explanation is given to account for nitrogenase sensitivity to oxygen.This publication has 7 references indexed in Scilit:
- Hydrogen peroxide lowers ATP levels in platelets without altering adenyalte energy charge and platelet function.Journal of Biological Chemistry, 1977
- Effect of Hyperoxide Radicals on Bovine-Erythrocyte MembraneEuropean Journal of Biochemistry, 1977
- The growth of nitrogen-fixing Azotobacter chroococcum in continuous culture under intense aerationCanadian Journal of Microbiology, 1976
- Nitrogenase of Azotobacter chroococcum. Kinetics of the reduction of oxidized iron-protein by sodium dithioniteBiochemical Journal, 1976
- Energy-Linked Pyridine Nucleotide Reduction: Inhibitory Effects of Hyperbaric Oxygen In Vitro and In VivoNature, 1965
- The Measurement of Bacterial Viabilities by Slide CultureJournal of General Microbiology, 1961
- Oxidation of some oxidation-reduction systems by oxygen at high pressuresArchives of Biochemistry and Biophysics, 1955