Glycogen content and nitrogenase activity in Anabaena variabilis

1984 ◽  
Vol 140 (2-3) ◽  
pp. 120-125 ◽  
Author(s):  
Anneliese Ernst ◽  
Heide Kirschenlohr ◽  
Jesus Diez ◽  
Peter B�ger
Keyword(s):  
Glycogen Content ◽  
Nitrogenase Activity ◽  
Anabaena Variabilis

Effect of Ammonium on the Nitrogenase Activity of Anabaena Variabilis

1991 ◽  
pp. 531-532
Author(s):  
M. Jha ◽  
A. F. Yakunin ◽  
Chan Van Ni ◽  
I. N. Gogotov
Keyword(s):  
Nitrogenase Activity ◽  
Anabaena Variabilis

scholarly journals High-Affinity Vanadate Transport System in the Cyanobacterium Anabaena variabilis ATCC 29413

2006 ◽  
Vol 188 (2) ◽  
pp. 464-468 ◽  
Author(s):  
Brenda S. Pratte ◽  
Teresa Thiel
Keyword(s):  
Transport System ◽  
Azotobacter Vinelandii ◽  
Nitrogenase Activity ◽  
Rhodopseudomonas Palustris ◽  
Methanosarcina Barkeri ◽  
Anabaena Variabilis ◽  
Transport Systems ◽  
Bacterial Strains ◽  
High Affinity ◽  
Major Cluster

ABSTRACT High-affinity vanadate transport systems have not heretofore been identified in any organism. Anabaena variabilis, which can fix nitrogen by using an alternative V-dependent nitrogenase, transported vanadate well. The concentration of vanadate giving half-maximum V-nitrogenase activity when added to V-starved cells was about 3 × 10−9 M. The genes for an ABC-type vanadate transport system, vupABC, were found in A. variabilis about 5 kb from the major cluster of genes encoding the V-nitrogenase, and like those genes, the vupABC genes were repressed by molybdate; however, unlike the V-nitrogenase genes the vanadate transport genes were expressed in vegetative cells. A vupB mutant failed to grow by using V-nitrogenase unless high levels of vanadate were provided, suggesting that there was also a low-affinity vanadate transport system that functioned in the vupB mutant. The vupABC genes belong to a family of putative metal transport genes that include only one other characterized transport system, the tungstate transport genes of Eubacterium acidaminophilum. Similar genes are not present in the complete genomes of other bacterial strains that have a V-nitrogenase, including Azotobacter vinelandii, Rhodopseudomonas palustris, and Methanosarcina barkeri.

scholarly journals Comparing Short-Term Effects of Ammonia and Methylamine on Nitrogenase Activity in Anabaena variabilis (ATCC 29413)

1987 ◽  
Vol 42 (7-8) ◽  
pp. 902-906 ◽  
Author(s):  
Sabine Reich ◽  
Helmar Almon ◽  
Peter Böger
Keyword(s):  
Protein Synthesis ◽  
Light Intensity ◽  
Nitrogenase Activity ◽  
Anabaena Variabilis ◽  
Short Term ◽  
Heterocystous Cyanobacterium ◽  
Nitrogenase Regulation ◽  
Methyl Amine ◽  
Cyanobacterium Anabaena ◽  
Nitrogenase Inhibition

Cyanobacterium . Anabaena variabilis, Nitrogenase Regulation, Ammonia, Methylamine Using the heterocystous cyanobacterium A nabaena variabilis (ATCC 29413) in an alkaline environment its nitrogenase activity is rapidly inhibited by ammonia and methylamine. Nitro­genase inhibition by ammonia is probably caused by a mechanism comparable to the switch-off effect, which has been described for several species of the Rhodospirillaceae, whereas methyl-amine-induced inhibition is caused by an uncoupling effect only. Evidence for these different effects is obtained by comparing nitrogenase activity in cell-free extracts of filaments pretreated by ammonia or methylamine. In addition, ammonia-dependent nitrogenase inhibition is shown to be dependent on protein synthesis and on light intensity.

scholarly journals Nitrogenase Activity and Membrane Electrogenesis in the Cyanobacterium Anabaena variabilis Kütz

2005 ◽  
Vol 115 (3) ◽  
pp. 519-523 ◽  
Author(s):  
Malcolm J. HAWKESFORD ◽  
Peter ROWELL ◽  
William D. P. STEWART ◽  
Robert H. REED
Keyword(s):  
Nitrogenase Activity ◽  
Anabaena Variabilis ◽  
Cyanobacterium Anabaena
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