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  • 1
    Digitale Medien
    Digitale Medien
    Springer
    Archives of microbiology 147 (1987), S. 190-194 
    ISSN: 1432-072X
    Schlagwort(e): Methanobacterium thermoautotrophicum ; Methyl-CoM reductase ; Immunocytochemistry ; Colloidal gold ; Energy conservation
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Cells of Methanobacterium thermoautotrophicum were fixed with glutaraldehyde, sectioned and labeled with antibodies against the β subunit of component C (=methyl-CoM reductase) of methyl-CoM reductase system and with colloidal gold-labeled protein A. It was found that the gold particles were located predominantly in the vicinity of the cytoplasmic membrane, when the cells were grown under conditions where methyl-CoM reductase was not overproduced. This finding confirms the recent data obtained with Methanococcus voltae showing via the same immunocytochemical localization technique that in this organism methyl-CoM reductase is membrane associated.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Archives of microbiology 150 (1988), S. 447-451 
    ISSN: 1432-072X
    Schlagwort(e): Acetobacterium woodii ; Caffeate reduction ; ATP formation
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract We have addressed the question, whether the reduction of caffeate in Acetobacterium woodii strain NZva16 is coupled to ATP synthesis by electron transport phosphorylation. The following results were obtained: 1. Cultures of A. woodii with H2 and CO2, grew to greater cell densities, when caffeate was also present. Caffeate was reduced to give hydrocaffeate and less acetate was formed. The cell yield based on the amount of caffeate reduced was approximately 1 g dry cells/mol. 2. Non-growing bacterial suspensions catalyzed the reduction of caffeate by H2. The specific activity (0.2–1.0 μmol · min−1 · mg−1 bacterial protein) was as high as expected for a catabolic reaction. 3. The ATP content of bacteria incubated, with H2 increased from 〈 1 to about 7 μmol per g cellular protein on the addition of caffeate. The ATP yield was calculated as 0.06 mol ATP · mol−1 caffeate from the initial velocity of ATP formation and the activity of caffeate reduction. Valinomycin together with nigericin inhibited ATP formation and caused a 2–3-fold increase of the activity of caffeate reduction. Protonophores were without, effect. 4. Caffeate in the presence of H2 caused the uptake of tetraphenylphosphonium cation by the bacteria. The uptake was abolished by valinomycin plus nigericin, and was considerably enhanced by monensin. Protonophores were without effect, even in the presence of monensin. It is concluded that caffeate reduction by H2 is coupled to ATP formation by electron transport phosphorylation. However, the failure of protonophores to prevent phosphorylation and TPP uptake cannot be explained.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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