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Energetics and biochemistry of fermentative benzoate degradation by Syntrophus gentianae

Energetics and biochemistry of fermentative benzoate degradation by Syntrophus gentianae

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SCHÖCKE, Ludger, Bernhard SCHINK, 1999. Energetics and biochemistry of fermentative benzoate degradation by Syntrophus gentianae. In: Archives of Microbiology. 171(5), pp. 331-337. ISSN 0302-8933. eISSN 1432-072X

@article{Schocke1999Energ-6564, title={Energetics and biochemistry of fermentative benzoate degradation by Syntrophus gentianae}, year={1999}, doi={10.1007/s002030050718}, number={5}, volume={171}, issn={0302-8933}, journal={Archives of Microbiology}, pages={331--337}, author={Schöcke, Ludger and Schink, Bernhard} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/6564"> <dc:contributor>Schöcke, Ludger</dc:contributor> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dc:rights>deposit-license</dc:rights> <dcterms:title>Energetics and biochemistry of fermentative benzoate degradation by Syntrophus gentianae</dcterms:title> <dcterms:abstract xml:lang="eng">The pathway of fermentative benzoate degradation by the syntrophically fermenting bacterium Syntrophus gentianae was studied by measurement of enzyme activities in cell-free extracts. Benzoate was activated by a benzoate-CoA ligase reaction, forming AMP and pyrophosphate, which was subsequently cleaved by a membrane-bound proton-translocating pyrophosphatase. Glutaconyl-CoA (formed from hypothetical pimelyl-CoA and glutaryl-CoA intermediates) was decarboxylated to crotonyl-CoA by a sodium-ion-dependent membrane-bound glutaconyl-CoA decarboxylase, a biotin enzyme that could be inhibited by avidin. The overall energy budget of this fermentation could be balanced only if the dearomatizing reduction of benzoyl-CoA is assumed to produce cyclohexene carboxyl-CoA rather than cyclohexadiene carboxyl-CoA, although experimental evidence of this reaction is still insufficient. With this assumption, benzoate degradation by S. gentianae can be balanced to yield onethird to two-thirds of an ATP unit per benzoate degraded, in accordance with earlier measurements of whole-cell energetics.</dcterms:abstract> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/6564"/> <dcterms:bibliographicCitation>First publ. in: Archives of Microbiology 171 (1999), pp. 331-337</dcterms:bibliographicCitation> <dc:creator>Schink, Bernhard</dc:creator> <dc:language>eng</dc:language> <dc:contributor>Schink, Bernhard</dc:contributor> <dcterms:issued>1999</dcterms:issued> <dc:creator>Schöcke, Ludger</dc:creator> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:27:26Z</dcterms:available> <dc:format>application/pdf</dc:format> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:27:26Z</dc:date> </rdf:Description> </rdf:RDF>

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