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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 126 (1980), S. 187-194 
    ISSN: 1432-072X
    Keywords: Temperature coefficients ; Cell protein production ; Specific growth rate ; Rate of bacteriochlorophyll synthesis ; Arrhenius plots ; Regulation of cellular bacteriochlorophyll levels ; Rhodospirillum rubrum ; Rhodopseudomonas sphaeroides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The influence of temperature on yields of cell protein and bacteriochlorophyll as well as on the rates of growth and bacteriochlorophyll synthesis was studied with Rhodospirillum rubrum and Rhodopseudomonas sphaeroides. Under chemotrophic conditions net cell-protein production increased in cultures of both species along with temperature from 14°C up to the optimum at 33°C. Under phototrophic conditions cell-protein yields were largely constant within the range from 21°C to 33°C. At temperatures below 21°C and above 33°C yields decreased. These results are interpreted in terms of coupling between energy yielding or redox equivalent providing metabolisms and cell biosynthesis. Upon adaptation from chemotrophic to phototrophic conditions a direct relationship between temperature increase and bacteriochlorophyll level was observed. Arrhenius plots of both, specific growth rates and rates of bacteriochlorophyll synthesis, revealed discontinuities at about 20°C. Temperature coefficients either above or below those discontinuities were similar in both species. In R. rubrum temperature coefficients of the synthesis of total bacteriochlorophyll were also representative of the synthesis of photochemical reaction center and light harvesting bacteriochlorophylls. But in R. sphaeroides significant differences were observed between temperature coefficients of the syntheses of bacteriochlorophylls of the costantly composed reaction centerlight harvesting complex on one hand and of both, total and the quantitatively variable light harvesting bacteriochlorophylls on the other. The results are interpreted in light of hypotheses on the regulation (a) of cellular bacteriochlorophyll levels as well as (b) of the ratio of functionally different bacteriochlorophylls in the photosynthetic apparatus.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-072X
    Keywords: Azotobacter vinelandii ; Nitrogenase ; Glutamine synthetase ; Glutamate synthase ; Intracellular localization of enzymes ; Chemostat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Azotobacter vinelandii was grown in oxygen-controlled continuous cultures under conditions of dinitrogen fixation. Different oxygen concentrations were adjusted with air. Cell-free extracts were employed to study the oxygen dependency of the intracellular distribution and activity of the following enzymes: nitrogenase, glutamine synthetase and glutamate synthase. Nitrogenase was localized exclusively in the soluble fraction. Its activity increased steeply when the oxygen concentration employed in growing the organism decreased from about 30% close to 0% air saturation. Glutamine synthetase was identified exclusively as a soluble enzyme. The degree of adenylylation of the enzyme increased from about one to about four parallel to nitrogenase activity when the oxygen concentration in the culture was lowered. Glutamate synthase was detected in both a soluble and a membrane-bound form. The sum of specific activities of both forms stayed constant irrespective of changes in the oxygen concentration. However, with increasing oxygen concentration, the proportion of the membrane-bound form increased up to two-thirds of the total activity.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 102 (1975), S. 59-64 
    ISSN: 1432-072X
    Keywords: Membrane Proteins ; Electron Microscopy ; Rhodospirillum rubrum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Intracytoplasmic membranes isolated from Rhodospirillum rubrum, mutant strain VI, were extracted with the detergent lauryl dimethyl amine oxide. Subsequently two fractions were isolated, one of which contained reaction centers and the other contained light-harvesting bacteriochlorophyll of the photosynthetic apparatus. The two fractions are compared with unextracted membranes on the basis of protein patterns obtained by different methods of polyacrylamide gelelectrophoresis. Electron micrographs of the light-harvesting bacteriochlorophyll fraction reveal the presence of vesicular membrane structures. The only difference between such membranes and unextracted membranes is identified after freeze etching. While unextracted membrane surfaces are studded with particles extracted membranes exhibit a smooth surface.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 102 (1975), S. 65-69 
    ISSN: 1432-072X
    Keywords: Ubiquinone 10 ; Bacteriochlorophyll ; Phototrophy ; Chemotrophy ; Rhodospirillum rubrum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The formation of ubiquinone 10 and bacteriochlorophyll (bchl) was determined in Rhodospirillum rubrum grown under different culture conditions. Transfer of chemotrophically grown cultures to photosynthetic conditions leads to the formation of the pigments until cells reach the stationary phase of growth. Bchl-synthesis initially exceeds quinone synthesis. On a cellular protein basis quinone levels first decrease by about a factor of two and subsequently increase by a factor of four. Bchl levels per protein increase until cells reach the stationary phase of growth. Quinone levels per bchl decrease rather rapidly and become constant in the growing culture. When cells were transferred under continuous phototrophic conditions to new culture medium, both pigments are formed concomitantly. While protein synthesis starts immediately, bchl and ubiquinone formation is slightly delayed. This causes a short time decrease in the amount of both pigments per cellular protein followed by an increase to a constant level. Ratios of ubiquinone per bchl are constant. The transfer of phototrophically grown cultures to chemotrophic conditions results in a complete inhibition of bchl formation while quinone synthesis resumes. Quinone cellular levels decrease slightly and then remain constant. Quinone values increase per bchl which is eventually diluted out of the cells.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1432-072X
    Keywords: Azotobacter vinelandii ; Ammonium assimilation ; Dinitrogen fixation ; Nitrogenase proteins ; Continuous culture
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Azotobacter vinelandii was grown at constant growth rate in a chemostat with different molar ratios of sucrose to ammonium (C/N) in the influent media. Both compounds were consumed at essentially the same ratios as were present in the influent media. At low (C/N)-ratios, the cultures were ammonium-limited. At increased (C/N)-ratio ammonium-assimilating cultures additionally began to fix dinitrogen. The (C/N)-ratio at which nitrogenase activity became measurable, increased when the ambient oxygen concentration was increased. Immunoblotting revealed the appearance of nitrogenase proteins when the activity became detectable. Nitrogenase activity as determined either by acetylene reduction or by total nitrogen fixation gave constant relative activities of 1:3.8 (mol of N2 fixed per mol of acetylene reduced) under all sets of conditions used in this investigation. In spite of the oxygen dependent variation of the (C/N)-ratio, nitrogenase became active when the ammonium supply was less than about 14 nmol of ammonium per g of protein. This suggests that oxygen was not directly involved in the onset of dinitrogen fixation.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 157 (1992), S. 141-147 
    ISSN: 1432-072X
    Keywords: Chloroflexus aurantiacus ; Amino acid utilization ; Bacteriochlorophyll synthesis ; Photosynthetic apparatus ; Chemostat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The phototrophic green bacterium Chloroflexus aurantiacus was grown anaerobically in batch culture with different amino acids at 56°C and constant illumination of 25 klx. The composition of the photosynthetic apparatus was measured by quantitation of the bacteriochlorophylls (Bchl) a and c (representing the membrane-bound and the chlorosomal moieties, respectively). Ser added at concentrations up to 15 mM stimulated protein formation and Bchl a and c syntheses. A comparable stimulation was found with Glu and Ala. Coproporphyrin accumulation approached saturation at 5 mM of Ala, Asp, Orn, and Ser, while with Glu and Arg saturating concentrations were above 5 mM. Protein and tetrapyrrole syntheses became saturated at 2.5 to 5 mM of Asp, Ile, and Val. However, with Arg and Orn Bchl c synthesis was stimulated up to 2.5 mM, growth and Bchl a synthesis up to 5 mM. At higher Arg or Orn concentrations these activities were inhibited. Coproporphyrin accumulation was highest with Arg or Orn, at concentrations which inhibited growth and Bchl formation. Stimulation of Bchl synthesis took place preferentially at the level of Bchl c, while Bchl a was more sensitive toward inhibition. In both cases however, the ratio of Bchl c to Bchl a increased with higher amino acid concentrations. Nevertheless, each amino acid induced a typical effect. To understand different effects exerted by different amino acids, chemostat cultures were grown limited by either Ser or Glu. With Ser, steady state protein levels and specific Bchl a contents decreased slightly when increasing the dilution rate (D). Concomitantly Bchl c and coproporphyrin levels as well as the ratio of Bchl a/Bchl c increased. With Glu as the limiting substrate, all of the above mentioned parameters decreased. Since all of the Ser was consumed and increasing amounts of Glu remained unutilized in the spent medium, it is concluded that differences in the formation of the three pyrrole derivatives tested are due to differences in the affinities of uptake systems for Ser and Glu.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 160 (1993), S. 406-410 
    ISSN: 1432-072X
    Keywords: Rhodobacter capsulatus ; Adenine nucleotides ; Chemostat ; Dinitrogen fixation ; Energy charge ; T/D ratios ; d,l-Malate utilization ; Control of nitrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Rhodobacter capsulatus strain 37b4 was grown diazotrophically in phototrophic chemostat culture with 30 mM of d,l-malate and 2 mM of ammonium. Illumination was varied at constant dilution rate (D) and vice versa, respectively. When D was raised from 0.035 to 0.165 h-1 at 30 klx, the steady state cell protein level as well as malate consumption decreased. d-malate was utilized only at D=0.035 h-1. Specific cellular activities of nitrogenase, as determined by acetylene reduction as well as by dinitrogen (N2) fixation, increased and approached constancy at D〉0.075 h-1. Specific ATP contents of cells increased with increasing D, while specific ADP and AMP contents exhibited no significant variations. Consequently, energy charge values as well as molar ratios of ATP/ADP (T/D) increased. Raising illumination from 6 to 30 klx at D=0.075 h-1 resulted in an increase of the steady state protein level as well as of l-malate consumption. d-malate was not utilized under these conditions. Specific nitrogenase activity of cells increased at the lower and levelled off at the higher illuminations. Specific ATP contents of cells stayed constant but specific ADP contents increased with increasing illumination. The energy charge did not vary significantly, while the T/C ratio decreased between 6 and 18 klx and stayed constant at the higher illuminations. The results do not reveal any relationship between nitrogenase activity and the cellular levels or relative proportions of different adenine nucleotides. However, when steady state amounts of fixed N2 were plotted versus steady state T/D ratios, an inverse proportion became apparent, irrespective of the growth conditions employed. On the other hand, specific nitrogenase activity increased linearly when the rate of malate consumption increased. The results suggest that under steady state conditions the T/D ratio reflects the amount of ATP required to keep the amount of fixed N2 at a given level, while the rate at which nitrogenase functions depends on the rate at which the carbon and electron source, malate, is utilized by the organisms.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 72 (1970), S. 361-370 
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The activity of NADH oxidase in cell fractions of R. rubrum was measured. In cells grown photosynthetically (anaerobic in the light) and semiaerobically in the dark, the highest activity was found to be in the 19,000xg pellet. This consisted preponderantly of cytoplasmic membrane and cell wall material. Bchl was more enriched in the purified thylakoids than the NADH oxidase activity. In extracts of cells grown aerobically the oxidase activity was higher than in cells grown anaerobically or semiaerobically. The highest activity was recovered in the 220,000xg pellet. The data suggest that NADH oxidase as well as bacteri ochlorophyll can be localized in the total intracellular membrane system. However, the distribution is inhomogeneous. Most of the NADH oxidase activity is localized in the c. m. region and most of bchl in the thylakoids.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 93 (1973), S. 219-228 
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The effects of 2-hydroxybiphenyl upon intracytoplasmic membranes of Rhodospirillum rubrum were investigated. At concentrations of 110 and 165 μM of 2-hydroxybiphenyl growth was delayed, it stopped completely at a concentration of 330 μM. In the latter case, instead of vesicular intracytoplasmic membranes concentric membraneous layers were found in electronmicrographs of whole cells. Inhibitor concentrations which still permit growth do not change the general appearance of intracytoplasmic membranes either in situ or in the isolated form. However, the formation of intracytoplasmic membranes was more affected by the presence of the inhibitor than was growth. Although by electron microscopy no effect of 2-hydroxybiphenyl on intracytoplasmic membranes could be revealed there were considerable influences on membrane composition. This concerned the formation of colored carotenoids and specifically the patterns of membrane proteins.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 79 (1971), S. 108-121 
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The growth of photosynthetically precultured cells of Rhodospirillum rubrum under aerobic condition in light is investigated. Special emphasis is given to the question of whether the photosynthetic electron transport chain is influenced under these conditions. Light-induced absorbance changes under anaerobic conditions show that although in whole cells a variation can be noted, the reactions of isolated membranes decrease only very slowly and parallel to each other. The photophosphorylation activity remains constant on a bacteriochlorophyll basis. On a cell mass basis this activity decreases parallel to the decreasing bacteriochlorophyll content. Light-dependent NAD+ reduction by ascorbate-DCPI remains constant on a bacteriochlorophyll basis, whereas succinate supported NAD+ reduction in light increases. On a cell mass basis the activity of succinate supported NAD+ reduction stays nearly constant, thus showing similar responses to the presence of oxygen in light as the NADH oxidase system. NADH oxidase activity increases on a bacteriochlorophyll basis and does not change on a cell mass basis. Parallel to the NADH-oxidase system, oxygen uptake in the dark by whole cells does not change after aerobiosis in light. Light inhibits respiration even after several generations of growth in the presence of oxygen; however, the inhibition decreases slowly. Light inhibition of respiration can be totally overcome by the addition of the uncoupler CCCP. These results indicate that light-dependent electron transport is not influenced significantly by the presence of oxygen. Although the respiratory system is formed, cells preferentially grow photosynthetically. Respiration takes over when the amount of bacteriochlorophyll reaches very low values.
    Type of Medium: Electronic Resource
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