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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 121 (1979), S. 255-260 
    ISSN: 1432-072X
    Keywords: Purine fermentation ; Xanthine dehydrogenase ; Selenium ; Tungsten ; Molybdenum ; Clostridium acidiurici ; Clostridium cylindrosporum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The xanthine dehydrogenase of Clostridium acidiurici and C. cylindrosporum was assayed with methyl viologen as acceptor. In C. acidiurici the basal activity level was about 0.3 μmol/min x mg of protein. Cells grown on uric acid in the presence of 10-7 M selenite showed a 14-fold increase in xanthine dehydrogenase activity, which decreased with higher selenite concentrations (10-5 M). The supplementation with 10-7 M molybdate or tungstate was without effect. High concentrations of tungstate decreased the xanthine dehydrogenase if selenite was also present. In comparison, high concentrations of molybdate affected only a small decrease in activity level at the optimal concentration for selenite and relieved to some degree the inhibitory effect of 10-5 M selenite. With hypoxanthine and xanthine as substrates for growth again only the addition of selenite was necessary to show a similar increase in xanthine dehydrogenase activity. C. acidiurici could be grown in a mineral medium. Both xanthine dehydrogenase and formate dehydrogenase exhibited the highest level of activity if selenite and tungstate were present in that medium. In C. cylindrosporum the basal activity level of xanthine dehydrogenase was about 0.95 μmol/min x mg of protein. The addition of 10-7 M selenite to the growth medium increased the activity level about 3-fold, but the highest level (3.7 U/mg) was reached if 10-7 M molybdate was also added. The presence of tungstate resulted in a decreased enzyme activity.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 119 (1978), S. 7-11 
    ISSN: 1432-072X
    Keywords: Clostridium formicoaceticum ; Fumarate reductase ; Peripheral enzyme ; Membrane protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract When Clostridium formicoaceticum was grown on fumarate or l-malate crude cell extracts contained a high fumarate reductase activity. Using reduced methyl viologen as electron donor the specific activity amounted to 2–3.5 U per mg of protein. Reduced benzyl viologen, FMNH2 and NADH could also serve as electron donors but the specific activities were much lower. The NADH-dependent activity was strictly membrane-bound and rather labile. Its specific activity did not exceed 0.08 U per mg of particle protein. Fumarate reductase activity was also found in cells of C. formicoaceticum grown on fructose, gluconate, glutamate and some other substrates. The methyl viologen-dependent fumarate reductase activity could almost completely be measured with intact cells whereas only about 25% of the cytoplasmic acetate kinase activity was detected with cell suspensions. The preparation of spheroplasts from cells of C. formicoaceticum in 20 mM HEPES-KOH buffer containing 0.6 M sucrose and 1 mM dithioerythritol resulted in the specific release of 88% of the fumarate reductase activity into the spheroplast medium. Only small amounts of the cytoplasmic proteins malic enzyme and acetate kinase were released during this procedure. These results indicate a peripheral location of the fumarate reductase of C. formicoaceticum on the membrane.
    Type of Medium: Electronic Resource
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