@article{Dimroth1998Energ-8202,
  year={1998},
  doi={10.1007/s002030050616},
  title={Energy conservation in the decarboxylation of dicarboxylic acids by fermenting bacteria},
  number={2},
  volume={170},
  issn={0302-8933},
  journal={Archives of microbiology},
  pages={69--77},
  author={Dimroth, Peter and Schink, Bernhard}
}

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    <dcterms:title>Energy conservation in the decarboxylation of dicarboxylic acids by fermenting bacteria</dcterms:title>
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    <dcterms:bibliographicCitation>First publ. in: Archives of microbiology 170 (1998), pp. 69-77</dcterms:bibliographicCitation>
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    <dc:contributor>Dimroth, Peter</dc:contributor>
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    <dcterms:abstract xml:lang="eng">Decarboxylation of dicarboxylic acids (oxalate, malonate, succinate, glutarate, and malate) can serve as the sole energy source for the growth of fermenting bacteria. Since the free energy change of a decarboxylation reaction is small (around  20 kJ per mol) and equivalent to only approximately one-third of the energy required for ATP synthesis from ADP and phosphate under physiological conditions, the decarboxylation energy cannot be conserved by substrate-level phosphorylation. It is either converted (in malonate, succinate, and glutarate fermentation) by membrane-bound primary decarboxylase sodium ion pumps into an electrochemical gradient of sodium ions across the membrane; or, alternatively, an electrochemical proton gradient can be established by the combined action of a soluble decarboxylase with a dicarboxylate/monocarboxylate antiporter (in oxalate and malate fermentation). The thus generated electrochemical Na+ or H+ gradients are then exploited for ATP synthesis by Na+- or H+-coupled F1F0 ATP synthases. This new type of energy conservation has been termed decarboxylation phosphorylation and is responsible entirely for ATP synthesis in several anaerobic bacteria.</dcterms:abstract>
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    <dcterms:issued>1998</dcterms:issued>
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