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  • Blackwell Publishing Ltd  (6)
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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 75 (1989), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The mechanism for uptake of glycolate in the cyanobacterium Anabaena 7120 and its capacity to metabolize glycolate were examined. The uptake of [14C]-glycolate in light, at pH 7, consisted of an initial rapid phase (≤60s) and a second slower phase. The latter obviously represents metabolism as the glycolate dehydrogenase inhibitor 2-pyridylhydroxymethanesulfonic acid (HPMS) did not affect the initial uptake phase while the second phase was strongly reduced. The sulfhydryl reagent N-ethylmaleimide (NEM) inhibited uptake of glycolate and the uptake was reduced by lactate, glycerate and glyoxylate, Treatment with triphenylmethylphosphonium (TPMP+), a lipophilic cation collapsing ΔΨ only slightly reduced the uptake of glycolate. At pH 7.0, the F0F1-ATPase inhibitor N, N′-dicyclohexylcarbodiimide (DCCD) and the uncoupler carbonylcyanide m-chlorophenylhydrazone (CCCP) abolished the uptake. Inhibition of photophosphorylation by dark-treatment and presence of 3-(3′,4′-dichlorophenyl)-1, 1-dimethylurea (DCMU) also reduced the uptake. Decreasing the pH in the range of 10 to 5.5 increased the uptake. In contrast to the situation at pH 7. CCCP did not affect the initial glycolate uptake at pH 5.5. We conclude that the uptake of glycolate is a carrier-mediated process which, at pH 7, is dependent on a H+-ATPase to create the ΔpH across the membranes needed for uptake, while at pH 5.5 the uptake of glycolate is not ATP-dependent. The capacity to metabolize glycolate was at least 50 μmol (mg chl a)−1 h−1 in young cultures. In older cultures the rate was nearly 50% lower.
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  • 2
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Nitrogen regulation of nitrate uptake and nitrate reductase (EC 1.7.99.4) was studied in the cyanobacterium Anabaena cycadeae Reinke and its glutamine auxotroph. Development of the nitrate uptake system preceded, and was independent of, the development of the nitrate reductase system. The levels of both systems were several-fold higher in the glutamine auxotroph lacking glutamine synthetase (EC 6.3.1.2) than in the wild type strain having normal glutamine synthetase activity. The nitrate uptake system was found to be NH4-repressible and the nitrate reductase system NO3−-inducible. NH4+ was the initial repressor signal for the uptake process which was involved in the control of the NO3−inducible reductase system.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 57 (1983), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Acetylene reduction (nitrogenase activity) by excised cephalodia of Peltigera aphthosa Willd. slowly declined on transfer of the cephalodia from light to darkness. The decline was more rapid in the absence of CO2 or when phosphoenolpyruvate carboxylase activity was inhibited by adding maleic acid or malonic acid. When glutamine synthetase (GS) activity was totally inhibited by adding l-methionine-dl-sulphoximine (MSX) the decline in nitrogenase activity in the absence of CO2 still occurred. However, this loss of activity did not occur when the mycobiont was disrupted using digitonin (0.01 % w/v) and the fixed NH4+ was released into the medium. The data suggest that dark CO2 fixation by the fungus supplies carbon skeletons which remove newly fixed NH4+ produced by the cyanobacterium. When such carbon skeletons are not available MH4+ accumulates and inhibits nitrogenase activity even in the absence of GS activity. It is probable that NH4+ and a product of GS exert independent inhibitory effects on nitrogenase activity.
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 80 (1990), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Distribution pattern and levels of nitrogenase (EC 1.7.99.2) and glutamine synthetase (GS, EC 6.3.1.2) were studied in N2-, NO3− and NH4+ grown Anabaena cylindrica (CCAP 1403/2a) using immunogold electron microscopy. In N2- and NO3− grown cultures, heterocysts were formed and nitrogenase activity was present. The nitrogenase antigen appeared within the heterocysts only and showed an even distribution. The level of nitrogenase protein in the heterocysts was identical with both nitrogen sources. In NO3− grown cells the 30% reduction in the nitrogenase activity was due to a corresponding decrease in the heterocyst frequency and not to a repressed nitrogenase synthesis. In NH4− grown cells, the nitrogenase activity was almost zero and new heterocysts were formed to a very low extent. The heterocysts found showed practically no nitrogenase protein throughout the cytoplasm, although some label occurred at the periphery of the heterocyst. This demonstrates that heterocyst differentiation and nitrogenase expression are not necessarily correlated and that while NH4+ caused repression of both heterocyst and nitrogenase synthesis, NO3− caused inhibition of heterocyst differentiation only. The glutamine synthetase protein label was found throughout the vegetative cells and the heterocysts of all three cultures. The relative level of the GS antigen varied in the heterocysts depending on the nitrogen source, whereas the GS level was similar in all vegetative cells. In N2- and NO3+ grown cells, where nitrogenase was expressed, the GS level was ca 100% higher in the heterocysts compared to vegetative cells. In NH4+ grown cells, where nitrogenase was repressed, the GS level was similar in the two cell types. The enhanced level of GS expressed in heterocysts of N2 and NO3− grown cultures apparently is related to nitrogenase expression and has a role in assimilation of N2derived ammonia.
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 36 (1986), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The utilization of NO−3, NO−2 and NH+4 was studied in whole filaments and isolated heterocysts of Anabaena 7120 (ATCC27893). NO−3- and NO−2-uptake were detectable in whole filaments but not in heterocysts, whereas NH+4-uptake was detectable in both. Activity of NO−3-reductase was present in cell-free extracts of whole filaments but not of heterocysts, whereas activities of NO−2-reductase and glutamine synthetase were present in both. NO−3-uptake and reductase activities could not be induced in heterocysts even after prolonged incubation in NO−3 medium. It is suggested that NO−3-metabolism in heterocysts is impaired due to a selective and irreversible loss of NO−3-uptake and reductase systems resulting in the abolition of competition for molybdenum cofactor (Mo-Co) and reductant between nitrogenase and NO−3-reductase, and an increase in glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase levels.
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 35 (1986), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Nitrogenase (Fe-protein) was localized in the free-living cyanobacterium Anabaena cylindrica and in the cyanobionts of Cycas revoluta and Peltigera aphthosa, using colloidal gold as an immunocytochemical marker. The Fe-protein was found to be evenly distributed throughout the heterocyst cytoplasma in A. cylindrica and in both the cyanobionts, including multiple heterocysts of the C. revoluta cyanobiont. No label was observed in the vegetative cells of free-living A. cylindrica or of the cyanobionts, although the cyanobionts apparently live under microaerobic conditions.
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