@article{Keller2019-11-29Energ-47713,
  year={2019},
  doi={10.3389/fmicb.2019.02785},
  title={Energy-conserving enzyme systems active during syntrophic acetate oxidation in the thermophilic bacterium Thermacetogenium phaeum},
  volume={10},
  journal={Frontiers in Microbiology},
  author={Keller, Anja and Schink, Bernhard and Müller, Nicolai},
  note={Article Number: 2785}
}

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    <dc:creator>Schink, Bernhard</dc:creator>
    <dc:creator>Müller, Nicolai</dc:creator>
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    <dc:creator>Keller, Anja</dc:creator>
    <dcterms:title>Energy-conserving enzyme systems active during syntrophic acetate oxidation in the thermophilic bacterium Thermacetogenium phaeum</dcterms:title>
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    <dcterms:issued>2019-11-29</dcterms:issued>
    <dc:rights>Attribution 4.0 International</dc:rights>
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    <dc:contributor>Müller, Nicolai</dc:contributor>
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    <dc:language>eng</dc:language>
    <dcterms:abstract xml:lang="eng">The thermophilic acetogen Thermacetogenium phaeum uses the Wood-Ljungdahl pathway in both directions, either for the production of acetate from various compounds or for the oxidation of acetate in syntrophic cooperation with methanogens. In this study, energy conserving enzyme systems in Thermacetogenium phaeum were investigated in both metabolic directions. A gene cluster containing a membrane-bound periplasmically oriented formate dehydrogenase directly adjacent to putative menaquinone synthesis genes was identified in the genome. The protein products of these genes were identified by total proteome analysis, and menaquinone MK-7 had been found earlier as the dominant quinone in the membrane. Enzyme assays with membrane preparations and anthraquinone-2,6-disulfonate as electron acceptor verified the presence of a quinone-dependent formate dehydrogenase. A quinone-dependent methylene THF reductase is active in the soluble fraction and in the membrane fraction. From these results we conclude a reversed electron transport system from methyl-THF oxidation to CO2 reduction yielding formate as reduced product which is transferred to the methanogenic partner. The redox potential difference between methyl-THF (Eo’= -200 mV) and formate (Eo’= 432 mV) does not allow electron transfer through syntrophic formate removal alone. We postulate that part of the ATP conserved by substrate-level phosphorylation has to be invested into the generation of a transmembrane proton gradient by ATPase. This proton gradient could drive the endergonic oxidation of methyl-THF in an enzyme reaction similar to the membrane-bound reversed electron transport system previously observed in the syntrophically butyrate-oxidizing bacterium Syntrophomonas wolfei. To balance the overall ATP budget in acetate oxidation, we postulate that acetate is activated through an ATP-independent path via aldehyde:ferredoxin oxidoreductase (AOR) and subsequent oxidation of acetaldehyde to acetyl-CoA.</dcterms:abstract>
    <dc:contributor>Keller, Anja</dc:contributor>
    <dc:contributor>Schink, Bernhard</dc:contributor>
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