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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 118 (1978), S. 109-114 
    ISSN: 1432-072X
    Keywords: Chromatium ; Near infrared absorption spectra ; Physiological and artificial spectral changes ; Triton X-100 ; Subchromatophore fractions ; Fluorescence emission spectra
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Spectral changes in the near infrared absorption region of chromatophores of Chromatium vinosum, strain D, were analyzed. Spectral changes dependent in growing cultures on temperature (33° C and 39° C, respectively) were compared to artificial changes which take place under the influence of the detergent Triton X-100. Like addition of Triton X-100 to chromatophores, transfer of cells from 39° C to 33° C leads to the reversible formation of an absorption band at 820 nm at the expense of a band at 850 nm. But in contrast to the influence of Triton X-100, chromatophores isolated from cells grown at 39° C (39° C chromatophores), contain on an identical bacteriochlorophyll basis, higher amounts of pigment absorbing at 880 nm and lower amounts of pigment absorbing at 800 nm than found in 33° C chromatophores. Triton X-100 treatment does not influence the production of light induced absorbance changes characteristic of photochemical reaction centers; it does, however, change absorption spectra of a subchromatophore fraction which does not exhibit the known light dependent reaction center responses. The spectral properties of this fraction are altered with Triton X-100 in a manner comparable to whole chromatophores, i.e. translocation of the 850 nm band to 820 nm. Subchromatophore fractions isolated from 33° C chromatophores, which display an absorption band at 820 nm show in the presence of menadione a light induced absorbance change at 835 nm. Subchromatophore fractions from 39° C chromatophores, which display no absorbance at 820 nm show a light induced adsorbance change at 835 nm only after addition of Triton X-100. Spectral changes in growing cultures are accompanied by changes in the fluorescence emission spectra of isolated chromatophores. While 33° C chromatophores exhibit a major fluorescence emission band at 929 nm plus a minor band at 890 nm 39° C chromatophores exhibit only one band at 937 nm.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 118 (1978), S. 99-108 
    ISSN: 1432-072X
    Keywords: Chromatium vinosum ; Membrane differentiation ; Subchromatophore fractions ; Protein patterns ; Reaction center and light harvesting bacteriochlorophyll complexes ; Photophosphorylation ; Sulfide oxidation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Chromatium vinosum, strain D, exhibits two extreme modifications of near infra-red absorption spectra when growing heterotrophically at temperatures either above or below 36.5° C. Chromatophores isolated from cells grown either at 33° C (33° C chromatophores) or 39° C (39° C chromatophores) were analyzed for structural and functional parameters. For this the following chromatophore subunits were solubilized and characterized; (i) a fraction absorbing maximally at 800 nm with shoulders at 820 and 850 nm when derived from 33° C chromatophores or absorbing at 800 nm and 850 nm when derived from 39° C chromatophores; (ii) reaction center-light harvesting bacteriochlorophyll complexes with identical spectra and ratios of reaction center to light harvesting bacteriochlorophyll (1:45); (iii) complexes containing cytochromes, (IV) reaction center bacteriochlorophyll complexes. Irrespective of their origins the fractions exhibited qualitatively identical protein patterns as analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Protein patterns of 33° C and 39° C chromatophores revealed an identical ratio of proteins of reaction centers to proteins of cytochrome preparations. But the ratio of proteins of reaction centers to proteins of light harvesting moieties was 1.9 times higher in 39° C chromatophores than in 33° C chromatophores. Correspondingly, the ratio of reaction center per total bacteriochlorophyll was 1.7 times higher in 39° C chromatophores (1:110) then in 33° C chromatophores (1:190). Activities of photophosphorylation were 0.73 and 0.56 μmoles of ATP per μmoles of total bacteriochlorophyll per min for 33° C and 39° C chromatophores, respectively. Activities of sulfide oxidation in the light by whole cells were 2.37 and 1.96 μmoles of sulfide per μmole of total bacteriochlorophyll per min for 33° C and 39° C cells. Accordingly, on a reaction center basis activities are significantly lower after growth of the organisms at 39° C than at 33° C. The data indicate that spectral changes in Chromatium vinosum represent changes in the ratio of reaction center to light harvesting bacteriochlorophyll accompanied by a variation of the absorption spectra of the latter bacteriochlorophyll moiety. Concomitantly, activities coupled to the photochemical apparatus were subjected to variations.
    Type of Medium: Electronic Resource
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