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  • 1
    ISSN: 1432-1440
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-072X
    Keywords: Synechococcus ; Lipopolysaccharide ; Lipid A ; O-Methyl sugars ; Chemotypes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Lipopolysaccharides have been isolated from eight strains of the unicellular cyanobacterium Synechococcus. Fucose, mannose, galactose, glucose and glucosamine were found in all of the lipopolysaccharides investigated. Additionally, strain-specific sugars are present and permit the chemotyping of lipopolysaccharide. Chemotype I, comprising three strains with a high G+C content of DNA (71-66 mol%), is characterized by a high rhamnose portion and by 3,6-dideoxy-d-arabino-hexose (tyvelose). Chemotype III, represented by three strains with a low G+C content of DNA (55-48 mol%), contains a mannose-polymer with small amounts of 3-O-methyl-mannose, 4-O-methyl-mannose, 2-keto-3-deoxyoctonate and mannosamine. Lipopolysaccharides of the two strains of chemotype II contain 2,3,4-tri-O-methyl-arabinose. Lipid A is difficult to split off from the polysaccharide moiety, but is present in all lipopolysaccharides from the Synechococcus strains. The presence of Lipid A is supported by the finding of β-hydroxy fatty acids, predominantly β-hydroxypalmitic acid. The distribution of branched β-hydroxy fatty acids, detected in small amounts, parallels chemotyping of lipopolysaccharide based on the sugar composition. The phosphorus content of the lipopolysaccharides is low. The pyrogenicity of lipopolysaccharides from two strains is low. Synechococcus lipopolysaccharides have little reactivity in antisera raised in rabbits against homologous cells. As far as tested they do not migrate in immunoelectrophoresis. This confirms the neutral character or low negative charge of Synechococcus lipopolysaccharides.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 102 (1975), S. 219-231 
    ISSN: 1432-072X
    Keywords: Respiratory Chain ; Cytochromes ; Rhodopseudomonas palustris
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The enzymatic activities and the cytochrome components of the respiratory chain were investigated with membrane fractions from chemoheterotrophically grown Rhodopseudomonas palustris. Whereas the level of electron transfer carriers was not distinctly affected by a change of the culture conditions, the potential activities of the enzymes were clearly increased when the cells were grown aerobically. Reduced-minus oxidized difference spectra of the membrane fractions prepared from dark aerobically grown cells revealed the presence of three b-type cytochromes b 561, b 560 and b 558, and at least two c-type cytochromes c 556 and c 2 as electron carriers in the electron transfer chain. Cytochrome of a-type could not be detected in these membranes. Reduced plus CO minus reduced difference spectra of the membrane fractions were indicative of cytochrome o, which may be equivalent to cytochrome b 560, appearing in substrate-reduced minus oxidized difference spectra. Cytochrome o was found to be the functional terminal oxidase. CO difference spectra of the high speed supernatant fraction indicated the presence of cytochrome c′. Succinate and NADH reduced the same types of cytochromes. However, a considerable amount of cytochrome b 561 with associated β and γ bands at 531 and 429 nm, respectively, was reducible by succinate, but not by NADH. A substantial fraction of the membrane-bound b-type cytochrome was non-substrate reducible and was found in dithionite-reduced minus substrate-reduced spectra. Cytochrome c 2 may be localized in a branch of the electron transport system, with the branch-point at the level of ubiquinone. The separate pathways rejoined at a common terminal oxidase. Two terminal oxidases with different KCN sensitivity were present in the respiratory chain, one of which was sensitive to low concentrations of KCN and was connected with the cytochrome chain. The other terminal oxidase which was inhibited only by high concentrations of cyanide was located in a branched pathway, through which the electrons could flow from ubiquinone to oxygen bypassing the cytochrome chain.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 101 (1974), S. 233-245 
    ISSN: 1432-072X
    Keywords: Lipopolysaccharides ; O-Antigens ; Chemical Composition ; Serology ; Rhodopseudomonas viridis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The present paper deals with the isolation, and chemical and serological characterization of the O-antigens (lipopolysaccharides, LPS) of the photosynthetic gram-negative bacterium Rhodopseudomonas viridis. The LPS are extractable with hot phenol/water, but unlike the phenol-soluble LPS of the closely related species Rhodopseudomonas palustris, the R. viridis O-antigens are preferentially extracted into the water phase. A mixture of phenol/chloroform/petroleum ether (PCP-method) does not extract the R. viridis LPS. All R. viridis LPS investigated belong to the same chemotype, the polysaccharide moiety of these O-antigens being composed of 3-O-methyl-l-xylose, 3-O-methyl-d-mannose, d-mannose, d-galactose, d-glucose, in addition to 2-keto-3-deoxyoctonate (KDO), glucosamine, 6-deoxyglucosamine (quinovosamine) and galactosamine uronic acid. The R. viridis O-antigens are clearly distinguishable from the l-glycero-d-mannoheptose containing O-antigens of R. palustris by the lack of this sugar (and of any other heptose) in the R. viridis LPS. The lipid moiety (lipid A) of the R. viridis O-antigen can be split off from the LPS by mild acid hydrolysis. Like lipid A from R. palustris, it differs remarkably from the well known lipid A of Enterobacteriaceae, in that d-glucosamine is replaced by a recently identified 2.3-diamino-2.3-dideoxyhexose in the R. viridis and R. palustris lipid A. Unlike enteric lipid A the R. viridis lipid A is phosphate-free and includes as the only fatty acid β-C14OH which is exclusively amide-linked. All R. viridis strains belong to the same serotype so far as investigated, as shown by passive hemagglutination with the isolated O-antigens and rabbit antisera against heat-killed cells.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 25 (1957), S. 333-351 
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Zusammefassung Im Chromatoplasma mehrerer Nostocaceen und Oscillatoriaceen liegen verstreut (Anabaena variabilis, Cylindrospermum licheniforme) oder vorwiegend an den querwänden (Oscillatoria limosa, Phormidium frigidum) angeordnet Granula, die einen Durchmesser von etwa 0,3 μ haben. Sie besitzen im submikroskopischen Bereich eine lamelläre Strukturierung. Die Granula von jungem Material speichern selektiv Janusgrün und die reduzierte Stufe, das Diäthylsafranin. Die Formazane von drei verschiedenen Tetrazoliumsalzen werden primär ebenfalls an den Granula abgelagert oder in ihnen gespeichert. Es wird aus den vorliegenden Versuchsergebnissen gefolgert, daß auf den Lamellen der Granula reduzierende Fermentsysteme lokalisiert sind. Die Granula wurden daher als “fermentaktive Granula” bezeichnet. Neben diesen “fermentaktiven Granula” sind weiterhin bei den untersuchten Arten metachromatische Körnchen anzutreffen, die kondensierte Phosphate enthalten. Außerdem sind an der Peripherie der Zelle, meist an der Wand anliegend, kleine, osmiophile Granula angeordnet. Sie haben einen Durchmesser von ungefähr 40 mμ. Im Centroplasma von Anabaena variabilis und Cylindrospermum licheniforme liegen große Einschlüsse, die RNS und kondensierte Phosphate enthalten. Die DNS ist wahrscheinlich im umliegenden Centroplasma lokalisiert.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 166 (1996), S. 151-159 
    ISSN: 1432-072X
    Keywords: Key wordsRhodobacter capsulatus ; Rhodospirillum ; rubrum ; Chaperone DnaK ; GroEL ; Light-harvesting ; complex LHI ; B870 bacteriochlorophyll protein ; B820 ; bacteriochlorophyll-protein ; Protein insertion ; Membranes ; Assembly
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The light-harvesting (LH) complex I (B870) of anoxygenic photosynthetic purple bacteria is the oligomeric form of its subunit B820 consisting of the low-molecular-weight polypeptides α, β, bacteriochlorophyll (BChl), and carotenoids in the stoichiometric ratio [α1β1 (BChl2) Crt1–2]n. LHI surrounds the photochemical reaction center (RC). The major absorption band of the LHI complex is species-specific and is found at 870–890 nm; those of the subunit and the monomeric BChl a (dissolved in methanol) absorb at 820 and 770 nm, respectively. The isolated LHI complex can be reversibly dissociated to the B820 subunit or to the polypeptides and pigments by addition of detergents. Reconstitution of the B820 or the functional B870 complex is still possible after partial truncation of the N- or C-terminal regions of the α- or β-polypeptide or of the β-polypeptide only. The minimal structural requirements for reconstitution of a spectrally wild-type form after truncation of the polypeptides and/or modifications of the BChl molecule are described. The insertion of the LHIα- and LHIβ-polypeptides into the membrane and the in vivo assembly of LHI, studied in a cell-free system and in whole cells of Rhodobacter capsulatus, depend on the primary structures of both polypeptides, BChl, the chaperones DnaK and GroEL, membrane-bound proteins, and energized membranes. Exchanges, deletions, or insertions of amino acyl residues, especially in the conserved region of the N-terminus of the LHIα-polypeptide, prevent or reduce the efficiency and stability of the LHI assembly. Therefore, reconstitution of LHI in a detergent micelle does not exactly reproduce the formation of the LHI complex in the photosynthetic membrane in vivo. The N-terminal domains play a crucial role in the formation of the oligomeric protein scaffold and of the pigment array. Facultatively phototrophic bacteria such as Rhodospirillum (Rsp.) rubrum or Rhodobacter (Rba.) capsulatus can adjust to changes in oxygen tension, light intensity, temperature, and substrates to grow under chemotrophic or phototrophic conditions. The photosynthetic apparatus (PSA), localized mainly on intracytoplasmic membranes (ICM), is usually synthesized only under low oxygen partial pressure. The cellular amount and composition of the PSA are modified upon changing light intensity in relation to cell growth (Drews and Golecki 1995). The morphogenesis of cellular structures like ICM is quite different from self-assembly. Self-assembly is a reversible process of aggregation of the constituents of a complex structure without protein synthesis and is driven by weak or strong forces in the interactions of the constituents. Morphogenesis results from the interplay of numerous gene products and the cellular organization and is always dependent upon pre-existent structures (Harold 1995). The morphogenesis of the photosynthetic membrane in purple bacteria has been studied in its different steps. The regulation at the transcriptional and post-transcriptional levels in purple bacteria, and the structure and morphogenesis of the ICM have been described recently (Armstrong 1995; Bauer 1995; Biel 1995; Drews and Golecki 1995; Klug 1995). In this mini-review, I will focus on the minimal requirements for the in vitro assembly of light-harvesting (LH) complex I (B870) from its constituents in detergent micelles and compare the results with observations on the complex process of targeting and import of LHI polypeptides into the membrane and assembly of B870.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 43 (1962), S. 152-161 
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The chromatophores of Rhodospirillum molischianum originate de novo from the cytoplasmic membrane. Their laminar membranes arise by invagination of the cytoplasmic membrane and these have a circular shape. 5–15 of these membranes are piled up to form the chromatophores. Probably, the membranes of the chromatophores remain always connected with the cytoplasmic membrane by a tubular stalk.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 53 (1966), S. 255-262 
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Description / Table of Contents: Summary Rhodopseudomonas viridis was isolated from different waters near Freiburg im Breisgau. It is a gramnegative bacterium which is motile by means of polar flagella. Cells are usually distinctly rod-shaped, occasionally the rods are lightly curved. The size is variable, the dimensions 0.6 to 0.8 by 1.5–2.5 μ. Dense suspensions of this Rhodopseudomonas species are green coloured. The colour is changed in older cultures to a dirty brown-green. The absorption-maxima of the in-vivo spectrum at 400, 606 and 1020 nm are attributed to bacteriochlorophyll b, while the peaks at 451 and 483 nm reflect the presence of carotenoids. The bacteria grow only anaerobically in the light. They are strictly photo-organotroph. Heavy growth is observed in media which contain malate, succinate, pyruvate or acetate as carbon source and ammonia as nitrogen source. p-amino-benzoic acid, biotin and vitamin B are required. Yeast extract (0.05%) and casamino acids stimulate but fatty acids with the exception of acetate inhibit growth. No development is observed with carbon dioxide as sole carbon source. Gelatine is not liquefied. Nitrate is not reduced to nitrite.
    Notes: Zusammenfassung Nach Untersuchung von Morphologie, Feinstruktur und Ernährungsphysiologie wird ein neu isoliertes grünes Bakterium in die Gattung Rhodopseudomonas eingeordnet und der Artname Rhodopseudomonas viridis vorgeschlagen.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Description / Table of Contents: Summary The growth rate (1/p; p = time for protein doubling) of Rhodospirillum rubrum in aerobic dark cultures is dependent from the oxygen partial pressure. The optimum of growth is achieved at an oxygen partial pressure of 3 to 5 mm Hg. At 150 mm Hg [O2] the growth rate will be reduced to 90% of the optimal rate. After lowering the oxygen partial pressure below 2 mm Hg the growth rate is dropped very strongly. The morphogenesis of the thylakoid-or chromatophore—membranes and the biosynthesis of bacteriochlorophyll are light independent processes. The morphogenesis is started by lowering the oxygen partial pressure. The optimum of bacteriochlorophyll synthesis in dark cultures is near the oxygen concentration of 2 mm Hg. It is possible to induce the pigment synthesis by lowering the oxygen partial pressure without changing the growth rate. But a change of the growth rate implies a change of the quotient protein/RNS and RNS/DNS. After induction of bacteriochorophyll synthesis “early” proteins are synthesized which are needed for the last part of the Mg-way of tetrapyrrol synthesis.
    Notes: Zusammenfassung Die Wachstumsrate (1/p; p = Proteinverdopplungszeit) von Rhodospirillum rubrum in aeroben Dunkelkulturen ist vom Sauerstoffpartialdruck abhängig. Das Optimum liegt bei 3–5 mm Hg [O2]. Steigt die O2-Konzentration auf 150 mm Hg [O2] an, so vermindert sich die Wachstumsrate langsam um etwa 10%. Unterhalb 2 mm Hg fällt sie dagegen steil nach 0 ab. Die Ausbildung des gesamten Systems der Photophosphorylierung (Thylakoide, Chromatophoren) ist ein lichtunabhängiger, aber vom Sauerstoffpartialdruck direkt abhängiger Prozeß. Die Morphogenese wird induziert, wenn der Sauerstoffpartialdruck auf etwa 20 mm Hg erniedrigt wird. Das Optimum der Bacteriochlorophyll-bildung unter aeroben Dunkelbedingungen liegt bei etwa 2 mm Hg [O2]. Die Pigmentsynthese kann durch Veränderung der Sauerstoffkonzentration induziert werden, ohne die Wachstumsgeschwindigkeit in der logarithmischen Wachstumsphase zu verändern. Eine Änderung der Wachstumsrate führt zu einer relativen Verschiebung der Syntheseraten für DNS, RNS und Protein.
    Type of Medium: Electronic Resource
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  • 10
    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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