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  • 1
    Electronic Resource
    Electronic Resource
    Nitrogen-limited continuous culture ofRhodopseudomonas capsulata growing photosynthetically or heterotrophically under low oxygen tensions (1974)
    Springer
    Archives of microbiology 99 (1974), S. 117-128 
    Details
    ISSN: 1432-072X
    Keywords: Continuous Culture ; Rhodopseudomonas capsulata ; Bacteriochlorophyll ; Protein ; Poly-β-Hydroxybutyrate ; Nitrogen Limitation ; Oxygen Control
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A continuous culture apparatus is described, which allows cultivation of photosynthetic bacteria anaerobically in the light and semiaerobically in the dark at constant oxygen tensions. The growth-parameters 1. substrate concentration at half maximum growth rate (K s) and 2. yield (Y) forRhodopseudomonas capsulata are calculated. An automatic control system of the oxygen partial pressure in the culture medium is elaborated. It is shown, that the discontinuous regulation with a control unit in connection with two magnetic valves, which give short pulses of either oxygen-free gas or gas mixed with oxygen, is an economic, practicable and reliable method. The yield coefficientY during growth limited by ammonium sulfate is variable due to the synthesis of nitrogen independent metabolites, such as poly-β-hydroxybutyrate. The storage of poly-β-hydroxybutyrate in continuous culture is a function of both the actual concentration of ammonia and of theC/N ratio. At very low growth rates (1/6 µ m ) the poly-β-hydroxybutyrate content increases amounting to 33% of the dry weight. In semiaerobically dark grown cells (pO2: 5 mm Hg) the protein and bacteriochlorophyll content increased definitely on dry weight basis with increasing growth rates. In contrast, in anaerobic light cultures only a small increase of the bacteriochlorophyll level but no change of the protein content per dry weight of cells was observed at increasing growth rates.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00696228
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  • 2
    Electronic Resource
    Electronic Resource
    Formation of reaction centers and light-harvesting bacteriochlorophyll-protein complexes in Rhodopseudomonas capsulata (1975)
    Springer
    Archives of microbiology 104 (1975), S. 77-82 
    Details
    ISSN: 1432-072X
    Keywords: Membrane Differentiation ; Reaction Center ; Bacteriochlorophyll ; Antenna-Pigment Complex ; Bacteriochlorophyll-Protein Association ; Photosynthetic Bacteria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Formation of the photosynthetic apparatus was induced in aerobically grown dark cultures of Rhodopseudomonas capsulata by lowering of the oxygen tension. Besides the wild type strain the carotenoid-less mutant strain A1a+ was investigated. Both strains exhibited initially a decrease of the molar ratio of total bacteriochlorophyll (Bchl) to reaction center (RC) Bchl, followed by an increase. Synthesis of RC-Bchl preceded the synthesis of light-harvesting (LH) Bchl. Activities of photophosphorylation in membrane preparations, isolated from cultures after different periods of incubation at low aeration, decreased on the basis of total Bchl from about 9 to 2 μmole ATP/μmole total Bchl·min, whereas the rate on the basis of RC-Bchl remained constant (about 500 μmole ATP/μmole RC-Bchl·min). Under the same conditions the membrane proteins were labelled with U−14C-protein hydrolysate. Corresponding to RC-Bchl the synthesis of RC-proteins dominated during the first 30 min of incubation at pO2 below 3 mmHg. After 45–60 min of membrane formation at low aeration the synthesis of LH-complex proteins exceeded the synthesis of RC proteins. The correlations between protein and Bchl synthesis in the sequential formation of RC- and LH-complexes are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00447303
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  • 3
    Electronic Resource
    Electronic Resource
    Oxygen tension regulated expression of the hemA gene of Rhodobacter capsulatus (1991)
    Springer
    Archives of microbiology 156 (1991), S. 129-134 
    Details
    ISSN: 1432-072X
    Keywords: δ-Aminolevulinic acid synthase ; Bacteriochlorophyll ; Promoter activity ; Oxygen regulation ; Rhodobacter capsulatus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The promoter of the Rhodobacter capsulatus hemA gene, coding for the enzyme δ-aminolevulinic acid synthase (ALAS), was identified by trans-complementation of a δ-aminolevulinic acid (ALA)-dependent mutant and found to be located within a 170 bp region proximal to the hemA gene. The activity of the hemA promoter was demonstrated by lacZ fusion and in vitro transcription-translation. An open reading frame (ORFX) was found downstream of hemA. The activity of the hemA promoter, but not that of the ORFX promoter, increased when oxygen tension was lowered in the culture. Deletions upstream of the hemA promoter region did not affect ALAS activity and formation of pigment-protein complexes in R. capsulatus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00290985
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  • 4
    Electronic Resource
    Electronic Resource
    Differentiation of the intracytoplasmic membrane of Rhodopseudomonas palustris induced by variations of oxygen partial pressure or light intensity (1977)
    Springer
    Archives of microbiology 115 (1977), S. 299-306 
    Details
    ISSN: 1432-072X
    Keywords: Rhodopseudomonas palustris ; Intracytoplasmic membrane ; Bacteriochlorophyll ; Antenna pigments ; Pigment-protein complexes ; Membrane differentiation ; Influence of light intensity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The photosynthetic apparatus of Rhodopseudomonas palustris contains, in addition to reaction center bacteriochlorophyll (Bchl) two spectral forms of light harvesting (LH) Bchl, i.e. LH Bchl I, characterized by an infrared absorption maximum at 880 nm (890 nm at 77°K) and LH Bchl II absorbing at 805 and 855 nm (805 and 870 nm at 77°K). LH Bchl I seems to be associated with a single protein species of an apparent mol. wt. of 13000 whereas LH Bchl II is apparently associated with two proteins of mol. wts. of 9000 and 11000. Cells in anaerobic cultures adapt to changes of light intensity 1. by variation of the size of the photosynthetic unit, i.e. the molar ratio of LH Bchl II to reaction center Bchl, 2. by variation of the number of photosynthetic units per unit of membrane area, 3. by regulation of the size of the intracytoplasmic membrane system. During adaptation of changes of oxygen partial pressure cells are able to synthesize reaction center Bchl, LH Bchl and intracytoplasmic membranes at different rates. The synthesis of reaction center Bchl and LH Bchl I are, however, coordinated with each other, while the syntheses of LH Bchl II and reaction center Bchl proceed independently.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00446456
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  • 5
    Electronic Resource
    Electronic Resource
    The regulation of cytochrome c oxidase of Rhodobacter capsulatus by light and oxygen (1987)
    Springer
    Archives of microbiology 149 (1987), S. 12-18 
    Details
    ISSN: 1432-072X
    Keywords: Oxidase regulation ; Cytochrome c oxidase ; Cytochrome c 2 ; Regulatory DNA sequence ; Rhodobacter capsulatus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In order to distinguish between the regulatory effects of oxygen tension and light intensity on cytochrome c oxidase protein and enzymatic activity cells of Rhodobacter capsulatus were shifted from phototrophic (anaerobic, light) growth to aerobic-light, aerobic-dark and to anaerobic-dark conditions, respectively. During shift-experiments the formation of oxidase protein and regulation of oxidase activity was followed by immunological and enzymatic means. The results support the idea, that the formation of oxidase protein is regulated by oxygen tension and light intensity changes, whereas the regulation of oxidase activity seems only to be correlated to the oxygen tension. A DNA sequence involved in the oxygen-dependent regulation of cytochrome oxidase could be identified in the regulation-deficient oxidase mutant H41 of R. capsulatus. Immunological investigations of cytochrome c 2 from mutant H41 demonstrated at the same time the participation of the c 2-polypeptide in the regulation of cytochrome c oxidase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00423129
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  • 6
    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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  • 7
    Electronic Resource
    Electronic Resource
    Recommendations for the naming of photochemical reaction centres and light-harvesting pigment-protein complexes from purple photosynthetic bacteria
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Bioenergetics 806 (1985), S. 185-186 
    Details
    ISSN: 0005-2728
    Keywords: Bacteriochlorophyll ; Light-harvesting pigment-protein complex ; Photosynthetic bacterium ; Reaction center
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0005-2728(85)90095-7
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  • 8
    Electronic Resource
    Electronic Resource
    Bacteriochlorophyll-protein interaction in the light-harvesting complex B800-850 from Rhodobacter sulfidophilus: A Fourier-transform Raman spectroscopic investigation
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Bioenergetics 1057 (1991), S. 367-372 
    Details
    ISSN: 0005-2728
    Keywords: (Rb. sulfidophilus) ; BCh1; bacteriochlorophyll ; Bacteriochlorophyll ; FT; Fourier transform ; Fourier transform Raman spectroscopy ; LH; light-harvesting ; Light-harvesting complex ; Photosynthesis ; Pigment-protein interaction ; Rb.; Rhodobacter
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0005-2728(05)80149-5
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  • 9
    Electronic Resource
    Electronic Resource
    Fluorescence emission by wild-type- and mutant-strains of Rhodopseudomonas capsulata
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Bioenergetics 593 (1980), S. 241-253 
    Details
    ISSN: 0005-2728
    Keywords: (Rps. capsulata) ; Bacterial photosynthesis ; Bacteriochlorophyll ; Energy transfer ; Fluorescence emission ; Pigment complex
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0005-2728(80)90062-6
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  • 10
    Electronic Resource
    Electronic Resource
    Effects of light intensity on membrane differentiation in Rhodopseudomonas capsulata
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Bioenergetics 547 (1979), S. 417-428 
    Details
    ISSN: 0005-2728
    Keywords: Bacteriochlorophyll ; Light effect (Rhodopseudomonas capsulata) ; Light-harvesting complex ; Membrane differentiation ; Photosynthetic apparatus ; Reaction center
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0005-2728(79)90022-7
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