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  • 1
    Electronic Resource
    Electronic Resource
    Differentiation of the membrane system in cells of Rhodopseudomonas capsulata after transition from chemotrophic to phototrophic growth conditions (1982)
    Springer
    Archives of microbiology 131 (1982), S. 313-322 
    Details
    ISSN: 1432-072X
    Keywords: Membrane differentiation ; Buoyant density ; Photosynthetic units ; Bacteriochlorophyll, emission, absorption ; Phospholipids
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Aerobically in the dark grown cultures of Rhodopseudomonas capsulata were shifted to low oxygen partial pressure for 30 min and afterwards to phototrophic conditions (anaerobic, light). During 210 min of adaptation to a phototrophic mode of life the bacteriochlorophyll (BChl) concentration increased 53-fold (doubling time 40 min) and the carotenoid content six fold. Growth was delayed. The light membrane fraction from chemotrophic and induced phototrophic cells contained low concentrations of small photosynthetic units (reaction center+light harvesting BChl B870), and low respiratory activities, especially of succinatecytochrome c oxidase. The heavy membrane fraction, i.e. the intracytoplasmic chromatophore fraction, increased during adaptation approximately 9-fold in surface area per cell, 42-fold in BChl content, 7-fold in reaction center content and 6-fold in the size of the photosynthetic unit. Phospholipid and fatty acid content and patterns changed slightly during adaptation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00411178
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  • 2
    Electronic Resource
    Electronic Resource
    Occurrence of oscillations in ATP synthesis and hydrolysis in chromatophores of Rhodospirillum rubrum (1985)
    Springer
    Archives of microbiology 143 (1985), S. 192-195 
    Details
    ISSN: 1432-072X
    Keywords: Oscillations ; Photophosphorylation ; ATPase ; Cooperative behaviour ; Chromatophores ; Rhodospirillum rubrum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The conditions under which an oscillatory behaviour is observed during net hydrolysis or synthesis of ATP in chromatophores of Rhodospirillum rubrum FR1 are described. In the case of ATPase the oscillations are observed at low temperature (ca. 11°C) in the dark after an initial transient behaviour. These oscillations are attenuated or disappear by the addition of an uncoupler. Oscillations are also observed during ATP synthesis. At 3°C the oscillations appear spontaneously if photophosphorylation is measured during a sufficiently long time. At 30°C the mere intercalation of a dark period also at 30°C is sufficient to trigger the oscillations in the following light period.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00411046
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  • 3
    Electronic Resource
    Electronic Resource
    Fusion of proteoliposomes containing the B800-850 light-harvesting complex with membranes of the mutant strain NK3 of Rhodopseudomonas capsulata lacking B800-850 (1985)
    Springer
    Archives of microbiology 141 (1985), S. 239-243 
    Details
    ISSN: 1432-072X
    Keywords: Absorption spectra ; Fluorescence emission spectra ; Carotenoid band shift ; Excition transfer ; Light-harvesting complexes ; Rhodopseudomonas capsulata
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Intracytoplasmic membranes of the mutant strain NK3 of Rhodopseudomonas capsulata lacking the lightharvesting complex B800-850 were fused with proteoliposomes containing the B800-850 complex. Fluorescence emission spectroscopy at 77K showed that after fusion the fluorescence of the B850 bacteriochlorophyll disappeared nearly completely and the B870 fluorescence became prominent. This result and control experiments with proteoliposome-chromatophore mixture and with chromatophore and solubilized B800-850 complexes, respectively, indicate that in fused membranes a reorientation of membrane particles took place and excitons migrated from B850 to B870 bacteriochlorophyll. In fused proteoliposome-chromatophore vesicles a light-induced carotenoid band shift was observed, reflecting the building of an electrical membrane potential due to chargeseparation. Carotenoid band shift was not observed in separated proteoliposomes and NK3 chromatophores. It is concluded that by membrane fusion and lateral diffusion of membrane particles reaction center-light-harvesting B870 complexes came in functional contact with B800-850 antenna complexes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00408065
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  • 4
    Electronic Resource
    Electronic Resource
    Isolation and purification of reaction center from Rhodopseudomonas viridis NHTC 133 by means of LDAO (1976)
    Springer
    Archives of microbiology 109 (1976), S. 301-305 
    Details
    ISSN: 1432-072X
    Keywords: Photosynthetic membrane ; Reaction center ; Quinones ; Cytochromes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two different procedures are described to isolate and purify the reaction center complex from Rhodopseudomonas viridis NHTC 133 by means of the non-ionic detergent dodecyldimethylamine oxide. Both reaction center particles thus obtained were active, as shown by a photobleaching centered at 975 nm. The reaction center also contained, in addition to bacteriochlorophyll, bacteriopheophytin. Other components were also found in this particle: cytochromes C553 and C558 and a menaquinone-like substance. The SDS gel electrophoresis of reaction centers is shown. The molecular weights of the subunits forming the reaction center in 0.5% sodium dodecyl sulfate and 1% mercaptoethanol were calculated as being: 45±1.5 and 37±1.5 kdalton, 29±1.5 and 23±1.5 kdalton. The molecular weight of the complex determined by means of gel filtration (Sepharose 6-B and Bio-Gel P-300) gives a value of approximately 240 kdalton. The minimum molecular weight of the complex calculated by disc gel electrophoresis was 231 kdalton.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00446642
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  • 5
    Electronic Resource
    Electronic Resource
    The reconstitution of photophosphorylation and the effect of inorganic phosphate at different pH's on the phenazine methosulfate photoinhibition of Rhodospirillum rubrum chromatophores (1979)
    Springer
    Archives of microbiology 120 (1979), S. 283-287 
    Details
    ISSN: 1432-072X
    Keywords: PMS photoinhibition ; Photophosphorylation ; Chromatophores ; Bacteriochlorophyll ; Coupling factor ; Structural changes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Preillumination of R. rubrum membranes in the presence of 50μM phenazine methosulfate produces an inhibition of their photophosphorylating capacity. At low pH's phosphate protects against this photo-inhibition, whereas increasing the pH eliminates this protective effect. The inhibition can be produced not only by preillumination at high pH in the presence of phenazine methosulfate, but also by preillumination at low pH (5.0) and then shifting the pH to 8.0 in the dark. We have also measured the effect of preillumination in the presence of an uncoupler such as carbonylcyanide p-trifluoromethoxyphenylhydrazone, and found that at normal pH's while photophosphorylation was protected, the uncoupler activated ATPase was inhibited pointing to a clear difference for both reactions and perhaps different structural requirements for their activities. The purified coupling factor protein isolated from either normal or photoinactivated membrane will reconstitute normal photophosphorylation in previously uncoupled membranes but not in uncoupled membranes which were inactivated by preillumination with phenazine methosulfate prior to uncoupling.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00423077
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  • 6
    Electronic Resource
    Electronic Resource
    Characterization of three membrane fractions isolated from cells of Rhodopseudomonas capsulata adapting from chemotrophic to phototrophic conditions (1980)
    Springer
    Archives of microbiology 127 (1980), S. 157-161 
    Details
    ISSN: 1432-072X
    Keywords: Rhodopseudomonas capsulata ; Membrane differentiation ; Photophosphorylation ; Succinate dehydrogenase ; NADH dehydrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract By means of sucrose density centrifugation three membrane fractions, named “light, medium and heavy” have been isolated from cells of Rhodopseudomonas capsulata strain 37b4, adapting from chemotrophic to phototrophic growth conditions. Succinate dehydrogenase activity of aerobically grown cells was mainly confined to the heavy (chromatophore) fraction. Upon changing to phototrophic conditions the activity of the succinate dehydrogenase increased in the medium and light fraction. All fractions contain bacteriochlorophyll. NADH dehydrogenase of chemotrophically grown cells was enriched in the light and medium fraction but is increased in the heavy fraction under phototrophic growth conditions. The capacity of photophosphorylation is high in the light and heavy fraction. The results indicate a differentially incorporation of functional subunits into specific parts of the membrane system during membrane differentiation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00428019
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  • 7
    Electronic Resource
    Electronic Resource
    Comparative studies on membranes isolated from Rhodopseudomonas viridis grown in the presence and in the absence of yeast extract (1974)
    Springer
    Archives of microbiology 101 (1974), S. 259-272 
    Details
    ISSN: 1432-072X
    Keywords: Photosynthetic Membrane ; Lipid and Protein Composition ; Reaction Center
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Rhodopseudomonas viridis was grown in the presence and in the absence of yeast extract. The cells grown under this latter condition present a ten fold diminished bacteriochlorophyll (bchl) content. This decrease was paralleled by a similar increase in the ratio lipid phosphorous/bchl, whereas the ornithine lipid/bchl ratio remains constant. Some quantitative differences in the fatty acid composition are also reported. The protein composition of both membranes was also studied, only indicating quantitative differences. An active reaction center preparation was obtained from both types of cells. When isolated from cells grown in the presence of yeast extract, this reaction center preparation shows the presence of proteins a, b, c and d. Further treatment of this active reaction center results, in cells grown under either condition, in the isolation of green (oxidized behl) and brown (inactive reaction center) bchl containing fractions. The protein composition and absorption spectrum of the inactive reaction centers obtained from both types of cells were identical (proteins a, c and d). On the other hand the green complexes differ in their protein composition as well as in their absorption spectrum.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00455943
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  • 8
    Electronic Resource
    Electronic Resource
    Heterogeneity of the coupling factor isolated from Rhodospirillum rubrum chromatophores by means of lithium chloride (1980)
    Springer
    Archives of microbiology 125 (1980), S. 149-152 
    Details
    ISSN: 1432-072X
    Keywords: ATPase ; Coupling factor ; Photophosphorylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract By means of 2.0 M lithium chloride we have been able to extract a coupling factor protein complex from membranes of Rhodospirillum rubrum strain W. The subunit composition analyzed by SDS-gel electrophoresis showed the presence of both the α and β subunits. The coupling factor protein analyzed by nondissociating gel electrophoresis indicated the presence of two protein bands (Protein I and II), of which only one showed Ca-ATPase activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00403212
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  • 9
    Electronic Resource
    Electronic Resource
    Growth and photosynthetic activities of wild-type and antenna-deficient mutant strains of Rhodobacter capsulatus (1991)
    Springer
    Archives of microbiology 155 (1991), S. 205-209 
    Details
    ISSN: 1432-072X
    Keywords: Turbidostat ; Light-intensity ; Growth ; Photophosphorylation ; Reaction center bleaching ; Absorption spectra ; Rhodobacter capsulatus mutants ; Antenna deficiency
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cells of Rhodobacter capsulatus wild-type strains (37b4, B 10) and mutant strains, lacking lightharvesting (LH) complex II (B800–850) and defective in formation of LH I (B870) complex [U 43 (pTXB 87), U43 (pTXA6-10)] were grown photosynthetically at high and low light intensities in a turbidostate. The mutant strain U43 (pTXA6-10), lacking any LH system, was able to grow at high and low light intensities with doubling times of 4.6 and 9.8 h, respectively. In this mutant the concentration of photochemical reaction centers (RC) per cell and per membrane protein was several times higher than in wild type cells, but the bacteriochlorophyll content, the size of the photosynthetic unit and the rate of photophosphorylation were lower than in wild type cells. Reversible bleaching of reaction center and photophosphorylation were measured under different excitation light intensities. The charge recombination in the RC between the primary donor and QB was very slow in the mutant strains. Two membrane fractions differing in absorption spectra and light saturation behaviour of reversible bleaching and photophosphorylation were isolated from the mutant strains. The experimental data indicate that photosynthetic units of different composition and/or organization are present in the mutant cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00252201
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  • 10
    Electronic Resource
    Electronic Resource
    Redox-controlled, in vivo and in vitro phosphorylation of the α subunit of the light-harvesting complex I in Rhodobacter capsulatus (1992)
    Springer
    Archives of microbiology 158 (1992), S. 315-319 
    Details
    ISSN: 1432-072X
    Keywords: Protein phosphorylation ; Antenna protein ; Rhodobacter capsulatus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Labelling of Rhodobacter capsulatus cells with (32P)Pi in a phototrophic culture results in phosphorylation of a membrane-bound polypeptide identified as the α subunit of the LHI antenna complex of the photosynthetic apparatus. Phosphorylation of the same polypeptide was also observed by incubation of chromatophores with (32P)ATP or under conditions of photophosphorylation with ADP and (32P)Pi. The identity of the phosphorylated LHI-α subunit was demonstrated by N-terminal protein sequencing of the phosphorylated polypeptide and by failure of labelling in LHI-defective mutants. Pre-aeration of the samples or addition of the oxidant potassium ferrcyanide stimulated the kinase activity whereas the presence of soluble cytoplasmic proteins impaired phosphorylation in an in vitro assay. No effect resulted from addition of reductants to the assay medium. The results indicate the presence of a membrane-bound protein kinase in R. capsulatus that phosphorylates the α subunit of the LHI antenna complex under redox control.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00245359
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