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  • 1985-1989  (3)
  • 1
    Electronic Resource
    Electronic Resource
    The three classes of hydrogenases from sulfate-reducing bacteria of the genus Desulfovibrio (1988)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 54 (1988), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Three types of hydrogenases have been isolated from the sulfate-reducing bacteria of the genus Desulfobibrio. They differ in their subunit and metal compositions, physico-chemical characteristics, amino acid sequences, immunological ractivities, gene structures and their catalytic properties. Broadly, the hydrogenases can be considered as ‘iron only’ hydrogenases and nickel-containing hydrogenases. The iron-sulfur-containg hydrogenase ([Fe] hydrogenase) contains two ferredoxin-type (4Fe-4S) clusters and an atypical iron-sulfur center belived to be involved in the activation of H2. The [Fe] hydrogenase has the highest specific activity in the evolution and consumption of hydrogen and in the proton-deuterium exchange reaction and this enzyme is the most sensitive to CO and NO2−. It is not present in all species of DesulfovibrioThe nickel-(iron-sulfur)-containing hydrogenases ([NiFe] hydrogenase) posses two (4Fe-4S) centers and one (3Fe-xS) cluster in addition to nickel and have been found in all species of Desulfovibrio so far investigated. The redox active nickel is ligated by at least two cysteinyl thiolate residues and the [NiFe] hydrogenases are particularly resistant to inhibitors such as CO and NO2−. The genes encoding the large and small subunits of a periplasmic and a membrane-bound species of the [NiFe] hydrogenase have been cloned in Eschierichia (E.) coli and sequenced. Their derived amino acid sequences exhibit a high degree of homology (70%); however, they show no obvious metal-binding sites or homology with the derived amino acid sequence of the [Fe] hydrogenase. The third class is represented by the nickel-iron-sulfur)-selenium-containing hydrogenases ([NiFe-Se] hydrohenases) which contain nickel and selenium in equimoleular amounts plus (4Fe-4S) centers and are only found in some species of Desulfovibrio. The genes encoding the large and small subunits of the periplasmic hydrogenase from Desulfrovibio (D) baculatus (DSM 1743) (for abbrviations see appendix) have been cloned
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1988.tb02748.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Trypanosoma cruzi: Histochemical Characterization of Parasitized Skeletal Muscle Fibers (1985)
    Oxford, UK : Blackwell Publishing Ltd
    The @journal of eukaryotic microbiology 32 (1985), S. 0 
    Details
    ISSN: 1550-7408
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: C57B1/6 mice were infected with Brasil strain Trypanosoma cruzi trypomastigotes. The leg muscles of the mice were serial-sectioned with a cryostat, and individual fibers were classified histochemically as type I or type II on the basis of succinic dehydrogenase or adenosine triphosphatase activity. Although markedly more type II fibers were present in the leg muscles, the percentage of infected type I fibers was nearly five-fold higher than type II. This is the first demonstration of a preferential in vivo distribution of T. cruzi in muscle fibers based upon muscle type.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1550-7408.1985.tb03062.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Nuclear magnetic resonance study of the configurational equilibria of ranitidine in solution (1987)
    Chichester : Wiley-Blackwell
    Organic Magnetic Resonance 25 (1987), S. 203-207 
    Details
    ISSN: 0749-1581
    Keywords: 13C NMR ; 1H NMR ; Ranitidine ; E/Z isomerization ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The E/Z configurational equilibrium of the nitroethylenic moiety of the antiulcer agent ranitidine was studied in aqueous solution and in DMSO-d6 and CDCl3 using 1H and 13C NMR spectroscopy. In aqueous solution the room temperature E/Z isomerization of the unprotonated nitroketenediamine moiety is fast on the NMR time scale, but becomes slow for the species protonated at this moiety owing to intramolecular hydrogen bonding between the nitro group and a neighbouring NH2R+ group. In DMSO-d6 a free energy of activation of the order of 70 kJ mol-1 was estimated for the E/Z isomerization of the unprotonated moiety of ranitidine, in good agreement with values previously found for 2,2-disubstituted nitroethylene model compounds.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrc.1260250305
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    Paper (German National Licenses)
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