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Electron transport chain of Zymomonas mobilis

Interaction with the membrane-bound glucose dehydrogenase and identification of ubiquinone 10

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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.

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Abbreviations

ABTS:

2,2′-Azino-di-[3-ethyl-benzthiazolinesulfonate (6)]

GDH:

glucose dehydrogenase

HQNO:

2-heptyl-4-hydroxy-quinoline-N-oxide

PQQ:

pyrroloquinoline quinone

TMPD:

N,N,N′,N′-tetramethyl-p-phenylene-diamine

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Authors and Affiliations

  1. Institut für Biotechnologie 1, Forschungszentrum Jülich GmbH, Postfach 1913, W-5170, Jülich, Federal Republic of Germany

    Michael Strohdeicher, Burkard Neuß, Stephanie Bringer-Meyer & Hermann Sahm

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  1. Michael Strohdeicher
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  2. Burkard Neuß
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  3. Stephanie Bringer-Meyer
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  4. Hermann Sahm
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Strohdeicher, M., Neuß, B., Bringer-Meyer, S. et al. Electron transport chain of Zymomonas mobilis . Arch. Microbiol. 154, 536–543 (1990). https://doi.org/10.1007/BF00248833

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  • DOI: https://doi.org/10.1007/BF00248833

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