KOPS - Das Institutionelle Repositorium der Universität Konstanz

Studies on succinate dehydrogenase : site of attachment of the covalently-bound flavin to the peptide chain

Studies on succinate dehydrogenase : site of attachment of the covalently-bound flavin to the peptide chain

Zitieren

Dateien zu dieser Ressource

Prüfsumme: MD5:984e4fc8c6d8f3931f3b2b971eaec2be

SALACH, Jim, Wolfram H. WALKER, Thomas P. SINGER, Anders EHRENBERG, Peter HEMMERICH, Sandro GHISLA, Ursula HARTMANN, 1972. Studies on succinate dehydrogenase : site of attachment of the covalently-bound flavin to the peptide chain. In: European Journal of Biochemistry. 26(2), pp. 267-278. ISSN 0014-2956. eISSN 1432-1033

@article{Salach1972Studi-6563, title={Studies on succinate dehydrogenase : site of attachment of the covalently-bound flavin to the peptide chain}, year={1972}, doi={10.1111/j.1432-1033.1972.tb01765.x}, number={2}, volume={26}, issn={0014-2956}, journal={European Journal of Biochemistry}, pages={267--278}, author={Salach, Jim and Walker, Wolfram H. and Singer, Thomas P. and Ehrenberg, Anders and Hemmerich, Peter and Ghisla, Sandro and Hartmann, Ursula} }

<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/123456789/6563"> <dc:contributor>Ghisla, Sandro</dc:contributor> <dc:creator>Hemmerich, Peter</dc:creator> <dc:creator>Ehrenberg, Anders</dc:creator> <dc:format>application/pdf</dc:format> <dc:creator>Ghisla, Sandro</dc:creator> <dc:contributor>Walker, Wolfram H.</dc:contributor> <dc:contributor>Hemmerich, Peter</dc:contributor> <dc:contributor>Salach, Jim</dc:contributor> <dcterms:abstract xml:lang="eng">Improved methods have been devised for the isolation in pmole quantities of a pure flavin pentapeptide and its acid-hydrolysis product (SD-flavin) from inner-membrane preparations of heart mitochondria and from soluble, purified succinate dehydrogenase. SD-flavin differs from riboflavin in still having an amino acid covalently linked to the isoalloxazine ring system. SDflavin may be compared with riboflavin and with various 8n-substituted synthetic flavins by optical spectrophotometry in the neutral and cationic states and by ESR and ENDOR spectrometry in the cationic radical state. On the basis of these experiments is was concluded that the FAD prosthetic group of mitochondria1 succinate dehydrogenase is covalently linked through the 8n-position to the peptide backbone of the protein. This conclusion is in accord with the acid stability of the natural product and its tendency to yield riboflavin under reductive conditions. The unusual pH-fluorescence spectrum of the flavin strongly suggests that the 8n-methylene group is linked to an amino acid through a tertiary nitrogen group.</dcterms:abstract> <dc:language>eng</dc:language> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dcterms:title>Studies on succinate dehydrogenase : site of attachment of the covalently-bound flavin to the peptide chain</dcterms:title> <dc:contributor>Hartmann, Ursula</dc:contributor> <dc:creator>Singer, Thomas P.</dc:creator> <dcterms:issued>1972</dcterms:issued> <dc:rights>deposit-license</dc:rights> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:27:26Z</dcterms:available> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:27:26Z</dc:date> <dc:contributor>Ehrenberg, Anders</dc:contributor> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/6563"/> <dcterms:bibliographicCitation>First publ. in: European Journal of Biochemistry 26 (1972), pp. 267-278</dcterms:bibliographicCitation> <dc:creator>Hartmann, Ursula</dc:creator> <dc:creator>Walker, Wolfram H.</dc:creator> <dc:creator>Salach, Jim</dc:creator> <dc:contributor>Singer, Thomas P.</dc:contributor> </rdf:Description> </rdf:RDF>

Dateiabrufe seit 01.10.2014 (Informationen über die Zugriffsstatistik)

Studies_on_succinate_dehydrogenase.pdf 97

Das Dokument erscheint in:

deposit-license Solange nicht anders angezeigt, wird die Lizenz wie folgt beschrieben: deposit-license

KOPS Suche


Stöbern

Mein Benutzerkonto