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  • 1
    Electronic Resource
    Electronic Resource
    Biochemical and Spectroscopic Characterization of the B800-850 Light-Harvesting Complex from Rhodobacter sulfidophilus and Its B800-830 Spectral Form (1995)
    s.l. : American Chemical Society
    Biochemistry 34 (1995), S. 10519-10524 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00033a025
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  • 2
    Electronic Resource
    Electronic Resource
    Phosphorylation of the α and β polypeptides of the light-harvesting complex I (B870) of Rhodobacter capsulatus in an in vitro translation system (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 124 (1994), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Synthesis and phosphorylation of the proteins α and β of the light-harvesting (LH) complex I (B870) were investigated in a cell-free translation system of Rhodobacter capsulatus. Both proteins were incorporated into the membrane fraction; LHIβ was inserted in the absence of LHIα was phosphorylated in the presence of [γ-32P]ATP only when membranes were present. Phosphorylated LHIβ was found only in the absence of membranes. The phosphate group bound to LHIβ was not transferred to LHIα during insertion. The results indicate that a membrane-bound and a soluble protein kinase are involved. Strong light reduced the amount of phosphorylated LHIα. The results are discussed with respect to the assembly and function of LHI.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1994.tb07266.x
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  • 3
    Electronic Resource
    Electronic Resource
    The light-harvesting complex II (B800-850) of Rhodobacter sulfidophilus: Characterization and formation under different growth conditions (1995)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 126 (1995), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The photosynthetic bacterium Rhodobacter sulfidophilus is able to grow chemotrophically and phototrophically at a broad range of light intensities. In contrast to other facultative phototrophs, R. sulfidophilus synthesizes reaction center and light-harvesting (LH) complexes, B870 (LHI) and B800–850 (LHII) even under full aerobic conditions in the dark. The content of bacteriochlorophyll (BChl) varied from 3.8 μg Bchl per mg cell protein when grown at high light intensity (20 000 lux) to 60 μg Bchl per mg cell protein when grown at low light intensities (6 lux). After a shift from high light to low light conditions, the size of the photosynthetic unit increased by a factor of 4. Chromatographie analysis of the LHII complex, isolated and purified from cells grown phototrophically (at high and low light intensities) and chemotrophically, could resolve only one type of a and one type of β polypeptide in the purified complex, of which the N-terminal sequences have been determined.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1995.tb07382.x
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  • 4
    Electronic Resource
    Electronic Resource
    Isolation and characterisation of porin from the outer membrane of Synechococcus PCC 6301 (1994)
    Springer
    Archives of microbiology 161 (1994), S. 163-167 
    Details
    ISSN: 1432-072X
    Keywords: Key words: Cyanobacteria – Outer membrane – Peptidoglycan-associated protein – Pore-forming protein – Porin –Synechococcus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. Pore-forming protein (porin) was isolated from N,N-dimethyl-dodecylaminoxid (LDAO)-extracted outer membranes of Synechococcus PCC 6301 and purified by ion exchange chromatography on DEAE-Sephacel column. The apparent molecular mass on SDS-PAGE was determined to be about 52 000. The native porin was reconstituted into black lipid bilayer membranes and showed a single-channel conductance of 5.5 nS in 1 M KCl. The porin was found to be N-terminally blocked. The C-terminal amino acid sequence was identified as Phe-Thr-Phe. Amino acid analysis suggested that the porin protein consists of about 420 amino acid residues, yielding a polarity of 43.6% and a molecular mass of 45 000 in contrast to the mobility on SDS-PAGE.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00276478
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  • 5
    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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  • 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
    Isolation and characterisation of porin from the outer membrane of Synechococcus PCC 6301 (1994)
    Springer
    Archives of microbiology 161 (1994), S. 163-167 
    Details
    ISSN: 1432-072X
    Keywords: Cyanobacteria ; Outer membrane ; Peptidoglycan ; associated protein ; Pore-forming protein ; Porin ; Synechococcus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Pore-forming protein (porin) was isolated from N,N-dimethyl-dodecylaminoxid (LDAO)-extracted outer membranes of Synechococcus PCC 6301 and purified by ion exchange chromatography on DEAE-Sephacel column. The apparent molecular mass on SDS-PAGE was determined to be about 52000. The native porin was reconstituted into black lipid bilayer membranes and showed a single-channel conductance of 5.5 nS in 1 M KCl. The porin was found to be N-terminally blocked. The C-terminal amino acid sequence was identified as Phe-Thr-Phe. Amino acid analysis suggested that the porin protein consists of about 420 amino acid residues, yielding a polarity of 43.6% and a molecular mass of 45000 in contrast to the mobility on SDS-PAGE.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00276478
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  • 8
    Electronic Resource
    Electronic Resource
    Characterization of Two Pore-Forming Proteins Isolated from the Outer Membrane of Synechococcus PCC 6301 (1998)
    Springer
    Current microbiology 36 (1998), S. 321-326 
    Details
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Two major proteins, A and B, were isolated and purified from outer membranes of the unicellular cyanobacterium Synechococcus PCC 6301 by gel filtration, anion-exchange chromatography, and preparative SDS-PAGE. Protein A revealed a single-channel conductance of 0.4 nanoSiemens (nS) in 1 M KCl, whereas preparations containing both proteins showed two different conductance maxima of 0.4 and 0.9 nS, suggesting that B also forms pores. The apparent molecular mass of the two closely migrating proteins was determined as 52 kDa, whereas native porin extracts revealed a relative molecular mass of ca. 140 kDa, indicating trimeric pore-forming units. Partial sequences of both proteins were obtained by N-terminal sequencing of tryptic peptides, and the C-terminal amino acid sequences were derived from the complete proteins. These sequences were aligned to protein sequences available in the databases. The results are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002849900316
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