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Initial steps in the fermentation of 3-hydroxybenzoate by Sporotomaculum hydroxybenzoicum

Initial steps in the fermentation of 3-hydroxybenzoate by Sporotomaculum hydroxybenzoicum

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MÜLLER, Jochen A., Bernhard SCHINK, 2000. Initial steps in the fermentation of 3-hydroxybenzoate by Sporotomaculum hydroxybenzoicum. In: Archives of Microbiology. 173(4), pp. 288-295. ISSN 0302-8933. eISSN 1432-072X

@article{Muller2000Initi-8173, title={Initial steps in the fermentation of 3-hydroxybenzoate by Sporotomaculum hydroxybenzoicum}, year={2000}, doi={10.1007/s002030000148}, number={4}, volume={173}, issn={0302-8933}, journal={Archives of Microbiology}, pages={288--295}, author={Müller, Jochen A. 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/123456789/8173"> <dc:creator>Schink, Bernhard</dc:creator> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:41:09Z</dc:date> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/8173"/> <dc:contributor>Müller, Jochen A.</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:41:09Z</dcterms:available> <dcterms:title>Initial steps in the fermentation of 3-hydroxybenzoate by Sporotomaculum hydroxybenzoicum</dcterms:title> <dc:rights>deposit-license</dc:rights> <dc:language>eng</dc:language> <dcterms:abstract xml:lang="eng">The anaerobic bacterium Sporotomaculum hydroxybenzoicum ferments 3-hydroxybenzoate to acetate, butyrate, and CO2. 3-Hydroxybenzoate was activated to 3-hydroxybenzoyl-CoA in a CoA-transferase reaction with acetyl-CoA or butyryl-CoA as CoA donors. 3-Hydroxybenzoyl-CoA was reductively dehydroxylated, forming benzoyl-CoA. This reaction was measured in cell-free extracts with cob(I)alamin as low-potential electron donor. No evidence was obtained that cob(I)alamin is the physiological electron donor; however, inhibitor studies indicated involvement of a strong nucleophile in the reaction. Benzoate was degraded by dense cell suspensions without a lag phase until an in situ DG¢ value</dcterms:abstract> <dc:creator>Müller, Jochen A.</dc:creator> <dcterms:issued>2000</dcterms:issued> <dc:format>application/pdf</dc:format> <dcterms:bibliographicCitation>First publ. in: Archives of Microbiology 173 (2000), 4, pp. 288-295</dcterms:bibliographicCitation> <dc:contributor>Schink, Bernhard</dc:contributor> </rdf:Description> </rdf:RDF>

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