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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular evolution 7 (1976), S. 159-165 
    ISSN: 1432-1432
    Keywords: Nitrogenases ; ATP-ases ; Amino Acid Compositions ; S△Q ; Evolutionary Relationships
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Comparisons of the amino acid compositions of the nitrogenase proteins from different organisms and their correlation with cross-reactivities and taxonomical data suggest an evolution within bacterial genomes rather than within plasmids. Comparisons of the amino acid compositions of nitrogenases and other ATP-ases show similarities which might be due to the evolution of these ATP-ases from a common ancestral protein.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 104 (1975), S. 163-169 
    ISSN: 1432-072X
    Keywords: Azotobacter vinelandii ; Nitrogenase ; Glutamine Synthetase ; Ammonium Pool ; Ammonium Transport ; Citrate Transport ; Repression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Both the changes in the activities of nitrogenase, glutamine synthetase and glutamate dehydrogenase and in the extracellular and intracellular NH4 + concentrations were investigated during the transition from an NH4 + free medium to one containing NH4 + ions for a continuous culture of Azotobacter vinelandii. If added in amounts causing 80–100% repression of nitrogenase, ammonium acetate, lactate and phosphate are absorbed completely, whereas chloride, sulfate and citrate are only taken up to about 80%. After about 1–2 hrs the NH4 + remaining in the medium is absorbed too, indicating the induction or activation of a new NH4 + transport system. One of the new permeases allows the uptake of citrate in the presence of sucrose. Addition of inorganic NH4 + salts leads to acidification of the culture. Anaerobiosis suppresses NH4 + transport. A rise in the extracellular NH4 + level leads to a reversible rise in the glutamine synthetase activity, which is not prevented by chloramphenicol, and to a reversible decrease in nitrogenase activity. During these measurements glutamate dehydrogenase activity remains close to zero. The intracellular NH4 + level of about 0.6 mM does not change when extracellular NH4 + is taken up and repression of nitrogenase starts.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 120 (1979), S. 263-270 
    ISSN: 1432-072X
    Keywords: Enzyme regulation ; Ammonium metabolism ; Nitrogenase ; Glutamine synthetase ; Glutamate synthase ; Glutamate dehydrogenase ; Asparagine synthetase ; Amino acid pools ; Clostridium pasteurianum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Addition of ammonium salts to N2 fixing continuous cultures of Clostridium pasteurianum caused immediate stop of nitrogenase synthesis, while the levels of glutamine synthetase, glutamate dehydrogenase and asparagine synthetase remained constant. No evidence for an interconversion of the glutamine synthetase was found. The activities of glutamate synthase in crude extracts were inversely related to the nitrogenase levels. The intracellular glutamine pool rapidly expanded during nitrogenase repression and decreased as fast during derepression while the pool sizes of all other amino acids were not strongly related to the rate of nitrogenase formation. These investigations suggest glutamine as corepressor of nitrogenase synthesis.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 111 (1976), S. 85-91 
    ISSN: 1432-072X
    Keywords: Ammonium metabolism ; Ammonium transport ; Glutamine synthetase ; Nitrogenase ; Glutamate synthase ; Glutamate dehydrogenase ; Nitrate reductase (dissimilatory) ; Klebsiella pneumoniae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The primary steps of N2, ammonia and nitrate metabolism in Klebsiella pneumoniae grown in a continuous culture are regulated by the kind and supply of the nitrogenous compound. Cultures growing on N2 as the only nitrogen source have high activities of nitrogenase, unadenylated glutamine synthetase and glutamate synthase and low levels of glutamate dehydrogenase. If small amounts of ammonium salts are added continuously, initially only part of it is absorbed by the organisms. After 2–3 h complete absorption of ammonia against an ammonium gradient coinciding with an increased growth rate of the bacteria is observed. The change in the extracellular ammonium level is paralleled by the intracellular glutamine concentration which in turn regulates the glutamine synthetase activity. An increase in the degree of adenylation correlates with a repression of nitrogenase synthesis and an induction of glutamate dehydrogenase synthesis. Upon deadenylation these events are reversed.—After addition of nitrate ammonia appears in the medium, probably due to the action of a membrane bound dissimilatory nitrate reductase.—Addition of dinitrophenol causes transient leakage of intracellular ammonium into the medium.
    Type of Medium: Electronic Resource
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