scholarly journals Effect of some pesticides on growth, nitrogen fixation and nifgenes in Azotobacter chroococcum and Azotobacter vinelandii isolated from soil

2013 ◽  
Vol 5 (9) ◽  
pp. 166-171 ◽  
Author(s):  
Mohammed Khudhur
Keyword(s):  
Nitrogen Fixation ◽  
Azotobacter Vinelandii ◽  
Azotobacter Chroococcum

Nitrogen fixation by cell-free extracts of Klebsiella pneumoniae

1968 ◽  
Vol 14 (1) ◽  
pp. 33-38 ◽  
Author(s):  
M. C. Mahl ◽  
P. W. Wilson
Keyword(s):  
Nitrogen Fixation ◽  
Klebsiella Pneumoniae ◽  
Azotobacter Vinelandii ◽  
Ammonium Ion ◽  
Michaelis Constant ◽  
Nitrogen Gas ◽  
Aerobacter Aerogenes ◽  
Free System ◽  
Evolving System ◽  
A Cell

A cell-free system which permits nitrogen fixation by extracts of Klebsiella pneumoniae M5al (formerly Aerobacter aerogenes) has been developed. It is, essentially, that system described by Bulen and associates for Azotobacter vinelandii, utilizing ATP as a source of energy and dithionite as a source of electrons. The Michaelis constant for fixation has been estimated to be 0.12 atm. The extracts possessed an ATP-dependent hydrogen evolving system. Hydrogen evolution from these extracts was less under nitrogen than under helium in the presence of ATP. Nitrogen gas appears to be the inducer of nitrogen fixation. In the absence of N2, no induction of nitrogenase occurs. Nitrogenase is absent in cells grown on NH4+-N. There is a lag of about 13 h after the introduction of N2 gas into a culture which has depleted its supply of NH4+-N before nitrogenase can be detected. For reasons discussed in the text, this conclusion must be regarded as tentative at this time. Ammonium ion appears to prevent the synthesis of new molecules of nitrogenase without affecting the activity of those already formed.

Metabolism of glycolic acid by Azotobacter chroococcum PRL H62

1973 ◽  
Vol 19 (3) ◽  
pp. 321-324 ◽  
Author(s):  
W. G. W. Kurz ◽  
T. A. G. LaRue
Keyword(s):  
Nitrogen Fixation ◽  
Dicarboxylic Acid ◽  
Glycolic Acid ◽  
Tca Cycle ◽  
Azotobacter Chroococcum ◽  
Acid Cycle ◽  
Isocitric Dehydrogenase ◽  
Tca Cycle Enzymes ◽  
The Tca Cycle ◽  
Reduced Nitrogen

When Azotobacter chroococcum grows on glycolic acid as sole C source, it cannot utilize N2 and must be provided with reduced nitrogen. Glycolic acid is metabolized via Kornberg's dicarboxylic acid cycle. The TCA cycle enzymes are low in activity, and isocitric dehydrogenase is absent. It is likely that isocitric dehydrogenase is the source of reductant for nitrogen fixation by Azotobacter nitrogenase.

Note on the effect of temperature on a mixed culture of two organisms in symbiotic relation

1939 ◽  
Vol 29 (2) ◽  
pp. 302-305 ◽  
Author(s):  
E. H. Richards
Keyword(s):  
Nitrogen Fixation ◽  
Mixed Culture ◽  
Azotobacter Chroococcum ◽  
Mixed Cultures ◽  
Effect Of Temperature ◽  
Two Temperatures ◽  
Symbiotic Relation

1. A study was made of nitrogen-fixation byAzotobacter chroococcumalone in a medium containing dextrose (which it can utilize) and in mixture with a coliform organism on a medium containing no carbohydrate except starch, whichAzotobactercannot utilize unless it be hydrolysed by the coliform organism or some other agency.2. The amount of nitrogen fixed in the mixed cultures was found to be maximal at two temperatures, and a discussion is given of the causes thought to be operative in producing the double maximum.

The flavin transferase ApbE flavinylates the ferredoxin:NAD+-oxidoreductase Rnf required for N2 fixation in Azotobacter vinelandii

2021 ◽  
Author(s):  
Yulia V Bertsova ◽  
Marina V Serebryakova ◽  
Alexander A Baykov ◽  
Alexander V Bogachev
Keyword(s):  
Nitrogen Fixation ◽  
Azotobacter Vinelandii ◽  
Growth Defect ◽  
Deficient Mutant ◽  
Fixed Nitrogen ◽  
Oxidoreductase Activity ◽  
Threonine Residue ◽  
Ferredoxin Reductase ◽  
Relative Contribution ◽  
Fixation System

Abstract Azotobacter vinelandii, the model microbe in nitrogen fixation studies, uses the ferredoxin:NAD+-oxidoreductase Rnf to regenerate ferredoxin (flavodoxin) acting as an electron donor for nitrogenase. However, the relative contribution of Rnf into nitrogenase functioning is unknown because this bacterium contains another ferredoxin reductase, FixABCX. Furthermore, Rnf is flavinylated in the cell, but the importance and pathway of this modification reaction also remain largely unknown. We have constructed A. vinelandii cells with impaired activities of FixABCX and/or putative flavin transferase ApbE. The ApbE-deficient mutant could not produce covalently flavinylated membrane proteins and demonstrated a markedly decreased flavodoxin:NAD+ oxidoreductase activity and significant growth defect under diazotrophic conditions. The double ΔFix/ΔApbE mutation abolished the flavodoxin:NAD+ oxidoreductase activity and the ability of A. vinelandii to grow in the absence of fixed nitrogen source. ApbE flavinylated a truncated RnfG subunit of Rnf1 by forming a phosphoester bond between FMN and a threonine residue. These findings indicate that Rnf (presumably its Rnf1 form) is the major ferredoxin-reducing enzyme in the nitrogen fixation system and that the activity of Rnf depends on its covalent flavinylation by the flavin transferase ApbE.

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