Fungistatic Action of Azotobacter chroococcum and A. vinelandii on Different Fungi

1982 ◽  
Vol 137 (1) ◽  
pp. 55-62
Author(s):  
R.R. Mallikarjunaiah ◽  
V.P. Bhide
Keyword(s):  
Azotobacter Chroococcum ◽  
Fungistatic Action

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.

scholarly journals The vanadium nitrogenase of Azotobacter chroococcum. Reduction of acetylene and ethylene to ethane

1988 ◽  
Vol 249 (3) ◽  
pp. 745-751 ◽  
Author(s):  
M J Dilworth ◽  
R R Eady ◽  
M E Eldridge
Keyword(s):  
Electron Flux ◽  
Azotobacter Chroococcum ◽  
Ph Values ◽  
Fe Protein ◽  
C2h2 Reduction ◽  
Vanadium Nitrogenase

1. The vanadium (V-) nitrogenase of Azobacter chroococcum transfers up to 7.4% of the electrons used in acetylene (C2H2) reduction for the formation of ethane (C2H6). The apparent Km for C2H2 (6 kPa) is the same for either ethylene (C2H4) or ethane (C2H6) formation and much higher than the reported Km values for C2H2 reduction to C2H4 by molybdenum (Mo-) nitrogenases. Reduction of C2H2 in 2H2O yields predominantly [cis-2H2]ethylene. 2. The ratio of electron flux yielding C2H6 to that yielding C2H4 (the C2H6/C2H4 ratio) is increased by raising the ratio of Fe protein to VFe protein and by increasing the assay temperature up to at least 40 degrees C. pH values above 7.5 decrease the C2H6/C2H4 ratio. 3. C2H4 and C2H6 formation from C2H2 by V-nitrogenase are not inhibited by H2. CO inhibits both processes much less strongly than it inhibits C2H4 formation from C2H2 with Mo-nitrogenase. 4. Although V-nitrogenase also catalyses the slow CO-sensitive reduction of C2H4 to C2H6, free C2H4 is not an intermediate in C2H6 formation from C2H2. 5. Propyne (CH3C identical to CH) is not reduced by the V-nitrogenase. 6. Some implications of these results for the mechanism of C2H6 formation by the V-nitrogenase are discussed.

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