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  • 1
    Electronic Resource
    Electronic Resource
    Formation and degradation of gluconate by Zymomonas mobilis (1988)
    Springer
    Applied microbiology and biotechnology 27 (1988), S. 378-382 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Zymomonas mobilis ATCC 29191 is able to degrade gluconate but cannot use it as a single carbon and energy source. Gluconate is phosphorylated by a gluconate kinase (EC 2.7.1.12) and the resulting 6-phosphogluconate is further catabolized to yield about 0.8 mol ethanol per mol of gluconate, considerable amounts of acetate and acetoin. This product spectrum agrees with the theoretical yield of only one reduction equivalent if gluconate is phosphorylated by a kinase and subsequently metabolized via the Entner-Doudoroff pathway. Furthermore, Z. mobilis contains a membrane-bound enzyme system which is able to oxidize glucose to gluconate. Cell-free extracts were active in an assay system with Wurster's blue as electron acceptor, and various aldoses as well as maltose, mannitol and sorbitol could be oxidized. The affinity for sorbitol was very low (K m =330 mM) but reasonable for glucose (K m =2.8 mM). The pH optimum for the glucose-oxidizing reaction was 6.5, while that for sorbitol oxidation was 5.5.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00251772
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Electron transport chain of Zymomonas mobilis (1990)
    Springer
    Archives of microbiology 154 (1990), S. 536-543 
    Details
    ISSN: 1432-072X
    Keywords: Zymomonas mobilis ; Glucose dehydrogenase ; Pyrroloquinoline quinone ; Ubiquinone ; Electron transport chain ; TMPD oxidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The interaction of the membrane-bound glucose dehydrogenase from the anaerobic but aerotolerant bacterium Zymomonas mobilis with components of the electron transport chain has been studied. Cytoplasmic membranes showed reduction of oxygen to water with the substrates glucose or NADH. The effects of the respiratory chain inhibitors piericidin, capsaicin, rotenone, antimycin, myxothiazol, HQNO, and stigmatellin on the oxygen comsumption rates in the presence of NADH or glucose as substrates indicated that a complete and in the most parts identical respiratory chain is participating in the glucose as well as in the NADH oxidation. Furthermore, the presence of coenzyme Q10 (ubiquinone 10) in Z. mobilis was demonstrated. Extraction from and reincorporation of the quinone into the membranes revealed that ubiquinone is essential for the respiratory activity with glucose and NADH. In addition, a membrane-associated tetramethyl-p-phenylene-diamine-oxidase activity could be detected in Z. mobilis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00248833
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    Paper (German National Licenses)
    Fulltext
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