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Studies on the reaction mechanism of general acyl-CoA dehydrogenase : determination of selective isotope effects in the dehydrogenation of butyryl-CoA

Studies on the reaction mechanism of general acyl-CoA dehydrogenase : determination of selective isotope effects in the dehydrogenation of butyryl-CoA

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POHL, Brigitte, Thomas RAICHLE, Sandro GHISLA, 1986. Studies on the reaction mechanism of general acyl-CoA dehydrogenase : determination of selective isotope effects in the dehydrogenation of butyryl-CoA. In: European Journal of Biochemistry. 160(1), pp. 109-115. ISSN 0014-2956. eISSN 1432-1033

@article{Pohl1986Studi-7325, title={Studies on the reaction mechanism of general acyl-CoA dehydrogenase : determination of selective isotope effects in the dehydrogenation of butyryl-CoA}, year={1986}, doi={10.1111/j.1432-1033.1986.tb09946.x}, number={1}, volume={160}, issn={0014-2956}, journal={European Journal of Biochemistry}, pages={109--115}, author={Pohl, Brigitte and Raichle, Thomas and Ghisla, Sandro} }

<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/123456789/7325"> <dc:contributor>Pohl, Brigitte</dc:contributor> <dc:creator>Ghisla, Sandro</dc:creator> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/7325"/> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dcterms:title>Studies on the reaction mechanism of general acyl-CoA dehydrogenase : determination of selective isotope effects in the dehydrogenation of butyryl-CoA</dcterms:title> <dc:rights>deposit-license</dc:rights> <dc:format>application/pdf</dc:format> <dc:creator>Pohl, Brigitte</dc:creator> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:33:33Z</dc:date> <dcterms:issued>1986</dcterms:issued> <dc:language>eng</dc:language> <dcterms:bibliographicCitation>First publ. in: European Journal of Biochemistry 160 (1986), 1, pp. 109-115</dcterms:bibliographicCitation> <dcterms:abstract xml:lang="eng">The kinetic properties of general acyl-CoA dehydrogenase from pig kidney have been investigated using normal butyryl-CoA as well as a α-deutero, β-deutero-and perdeutero-butyryl-CoA. In turnover catalysis, isotope effects of 2, 3.6, and 9 were found respectively. In the reductive half reaction the isotope effects were 2.5, 14, and 28 for the same substrates, and 21 for (2R,3R)-(2,3-D2)butyryl-CoA. No intermediates are apparent during the reduction of oxidized enzyme to the presumed complex of reduced enzyme and crotonyl-CoA. The results are interpreted as indicating a high degree of concertedness during the rupture of the α and β C-H bonds. They are compatible with a mechanism in which simultaneously the α-hydrogen is abstracted as a proton, while the β-hydrogen is transferred to the oxidized flavin as a hydride.</dcterms:abstract> <dc:contributor>Raichle, Thomas</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:33:33Z</dcterms:available> <dc:creator>Raichle, Thomas</dc:creator> <dc:contributor>Ghisla, Sandro</dc:contributor> </rdf:Description> </rdf:RDF>

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