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Inhibition of Nitrogenase Activity by Ammonium Chloride in Azotobacter Vinelandii

Overview
Journal J Bacteriol
Specialty Microbiology
Date 1984 Jan 1
PMID 6581156
Citations 18
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Abstract

In Azotobacter vinelandii cells, the short-term inhibition of nitrogenase activity by NH4Cl was found to depend on several factors. The first factor is the dissolved oxygen concentration during the assay of nitrogenase. When cells are incubated with low concentrations of oxygen, nitrogenase activity is low and ammonia inhibits strongly. With more oxygen, nitrogenase activity increases. Cells incubated with an optimum amount of oxygen have maximum nitrogenase activity, and the extent of inhibition by ammonia is small. With higher amounts of oxygen, the nitrogenase activity of the cells is decreased and strongly inhibited by ammonia. The second factor found to be important for the inhibition of nitrogenase activity by NH4Cl was the pH of the medium. At a low pH, NH4+ inhibits more strongly than at a higher pH. The third factor that influenced the extent of ammonia inhibition was the respiration rate of the cells. When cells are grown with excess oxygen, the respiration rate of the cells is high and inhibition of nitrogenase activity by ammonia is small. Cells grown under oxygen-limited conditions have a low respiration rate and NH4Cl inhibition of nitrogenase activity is strong. Our results explain the contradictory reports described in the literature for the NH4Cl inhibition of nitrogenase in A. vinelandii.

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References
1.
Haaker H, Laane C, Hellingwerf K, Houwer B, Konings W, Veeger C . Short-term regulation of the nitrogenase activity in Rhodopseudomonas sphaeroides. Eur J Biochem. 1982; 127(3):639-45. DOI: 10.1111/j.1432-1033.1982.tb06920.x. View

2.
Tubb R, POSTGATE J . Control of nitrogenase synthesis in Klebsiella pneumoniae. J Gen Microbiol. 1973; 79(1):103-17. DOI: 10.1099/00221287-79-1-103. View

3.
Yoch D, Gotto J . Effect of light intensity and inhibitors of nitrogen assimilation on NH4+ inhibition of nitrogenase activity in Rhodospirillum rubrum and Anabaena sp. J Bacteriol. 1982; 151(2):800-6. PMC: 220328. DOI: 10.1128/jb.151.2.800-806.1982. View

4.
Daesch G, Mortenson L . Effect of ammonia on the synthesis and function of the N 2 -fixing enzyme system in Clostridium pasteurianum. J Bacteriol. 1972; 110(1):103-9. PMC: 247384. DOI: 10.1128/jb.110.1.103-109.1972. View

5.
Sweet W, BURRIS R . Inhibition of nitrogenase activity by NH+4 in Rhodospirillum rubrum. J Bacteriol. 1981; 145(2):824-31. PMC: 217185. DOI: 10.1128/jb.145.2.824-831.1981. View