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  • 1
    Electronic Resource
    Electronic Resource
    Energy metabolism and biosynthesis of Vibrio succinogenes growing with nitrate or nitrite as terminal electron acceptor (1983)
    Springer
    Archives of microbiology 135 (1983), S. 36-41 
    Details
    ISSN: 1432-072X
    Keywords: Phosphorylative nitrite reduction ; Nitrate reduction ; Vibrio succinogenes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract 1. Growth of Vibrio succinogenes with nitrate as terminal electron acceptor was found to be a function of the following two catabolic reactions: (a) $$HCO _2^ - + NO _3^ - + H^ + \to CO_2 + NO _2^ - + H_2 O$$ (b) $$3HCO _2^ - + NO _2^ - + 5H^ + \to 3CO_2 + NH _4^ + + 2H_2 O.$$ The latter reaction (b) was responsible for growth with nitrite. 2. Either succinate or fumarate could serve as sole carbon source during growth with nitrate or nitrite. Biosynthesis from succinate proceeded via fumarate. The ATP requirement for cell synthesis from succinate was equal to that calculated earlier for growth with fumarate as carbon source and electron acceptor (Brounder et al. 1982). 3. The cell yield at infinite dilution rate (Y max) as obtained with chemostat cultures was 8.5g dry cells/mol formate with either nitrate or nitrite as acceptor. This value amounts to 60% of that measured earlier with fumarate as acceptor (Mell et al. 1982). 4. Membrane vesicles prepared from V. succinogenes catalyzed electron transport from H2 to nitrate. The reaction was dependent on the menaquinone present in the membrane. 5. Electron transport with H2 and nitrite was coupled to the phosphorylation of ADP. The P/H2 ratio with nitrite was 40% of that measured with fumarate as acceptor using the same preparation. The phosphorylation but not the electron transport was abolished by an uncoupling agent.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00419479
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  • 2
    Electronic Resource
    Electronic Resource
    The membraneous nitrite reductase involved in the electron transport of Wolinella succinogenes (1985)
    Springer
    Archives of microbiology 140 (1985), S. 380-386 
    Details
    ISSN: 1432-072X
    Keywords: Nitrite reductase ; Electron transport ; Wolinella succinogenes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Wolinella succinogenes grown with nitrate as terminal electron acceptor contains two nitrite reductases as measured with the donor viologen radical, one in the cytoplasm and the other integrated in the cytoplasmic membrane. The fumarate-grown bacteria contain only the membraneous species. The isolated membraneous enzyme consists of a single polypeptide chain (M r 63,000) carrying 4 hemeC groups and probably an iron-sulphur cluster as prosthetic groups. The enzyme amounts to about 1% of the total membrane protein. The isolated enzyme catalyses the reduction of nitrite to ammonium without accumulation of significant amounts of intermediates or alternative products. The Michaelis constant for nitrite was 0.1 mM and the turnover number of the hemeC 1.5 · 105 electrons per min at 37°C. The viologen-reactive site of the enzyme in the membrane is oriented towards the cytoplasm. When the isolated enzyme is incorporated into liposomes, the viologen-as well as the nitrite-reactive site is exposed to thooutside. The cytoplasmic membrane contains a second hemeC protein (M r 22,000) which may represent a cytochrome c.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00446982
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  • 3
    Electronic Resource
    Electronic Resource
    Comparative analysis of genes encoding methyl coenzyme M reductase in methanogenic bacteria (1988)
    Springer
    Molecular genetics and genomics 213 (1988), S. 409-420 
    Details
    ISSN: 1617-4623
    Keywords: Methanococcus voltae ; Methylreductase genes ; Translation signals ; Comparative analysis ; Molecular evolution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The sequence of the gene cluster encoding the methyl coenzyme M reductase (MCR) in Methanococcus voltae was determined. It contains five open reading frames (ORF), three of which encode the known enzyme subunits. Putative ribosome binding sites were found in front of all ORFs. They differ in their degrees of complementarity to the 3′ end of the 16 S rRNA, which is discussed in terms of different translation efficiencies of the respective genes. The codon usage bias is different in the subunit encoding genes compared with the two other ORFs in the cluster and two other known genes of Mc. voltae. This is interpreted in terms of increased translational accuracy of the highly expressed MCR subunit genes. The derived polypeptide sequences encoded by the five ORFs of the MCR cluster were compared to those of the respective genes in Methanobacterium thermoautotrophicum Marburg and Methanosarcina barkeri. Conserved regions were detected in the enzyme subunits, which are candidates for factor binding domains. Conserved hydrophobic sequences found in the α and β subunits are discussed with respect to the membrane association of the enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00339610
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    Paper (German National Licenses)
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