KOPS - Das Institutionelle Repositorium der Universität Konstanz

Studies on Succinate Dehydrogenase : 8alpha-Histidyl-FAD as the Active Center of Succinate Dehydrogenase

Studies on Succinate Dehydrogenase : 8alpha-Histidyl-FAD as the Active Center of Succinate Dehydrogenase

Zitieren

Dateien zu dieser Ressource

Prüfsumme: MD5:572346865fb2cd496381f5ba69e8a0ce

WALKER, Wolfram H., Thomas P. SINGER, Sandro GHISLA, Peter HEMMERICH, 1972. Studies on Succinate Dehydrogenase : 8alpha-Histidyl-FAD as the Active Center of Succinate Dehydrogenase. In: European Journal of Biochemistry. 26(2), pp. 279-289. ISSN 0014-2956. eISSN 1432-1033. Available under: doi: 10.1111/j.1432-1033.1972.tb01766.x

@article{Walker1972Studi-8217, title={Studies on Succinate Dehydrogenase : 8alpha-Histidyl-FAD as the Active Center of Succinate Dehydrogenase}, year={1972}, doi={10.1111/j.1432-1033.1972.tb01766.x}, number={2}, volume={26}, issn={0014-2956}, journal={European Journal of Biochemistry}, pages={279--289}, author={Walker, Wolfram H. and Singer, Thomas P. and Ghisla, Sandro and Hemmerich, Peter} }

Singer, Thomas P. 2011-03-24T17:41:30Z deposit-license application/pdf Studies on Succinate Dehydrogenase : 8alpha-Histidyl-FAD as the Active Center of Succinate Dehydrogenase Hemmerich, Peter Walker, Wolfram H. 2011-03-24T17:41:30Z 1972 Walker, Wolfram H. First publ. in: European Journal of Biochemistry 26 (1972), 2, pp. 279-289 1. Succinate dehydrogenase flavocoenzyme ("SD-flavin"), previously shown to be an 8α-substituted riboflavin derivative containing a tertiary nitrogen homoconjugated to the flavin nucleus, was subjected to further hydrolysis and to reduction under acid conditions. Both conditions resulted in the liberation of 1 mole of histidine per mole of flavin. This proves histidine to be the covalent link between flavin and peptide backbone in succinate dehydrogenase and imidazole to be the tertiary nitrogen function homoconjugated to the flavin.<br />2. 8α-Histidyl-riboflavin has been synthesized starting from riboflavin chemically and shown to be completely identical with the natural product in optical, ESR and NMR spectra, pH-fluorescence curve and behavior on thin-layer and paper chromatography, as well as paper electrophoresis.<br />3. Both the natural compound isolated by acid hydrolysis of flavin peptide and the synthetic one contain two isomers, which may be separated by high voltage electrophoresis. The isomers appear to be the N(1)-and N(3)-imidazole substituted compounds. Digestion of the flavin peptide with aminopeptidase M yields only one isomer but on treatment with 6-N HC1 this is gradually converted to a mixture of the two isomers. The absolute assignment of the natural isomer is suggested as 8α-[N(3)-histidyl]-riboflavino n the basis of imidazole quaternization with CH3I, reductive cleavage of the flavin-imidazole bond and identification of the methyl-histidine liberated as 1-methyl-histidine. Ghisla, Sandro Ghisla, Sandro Singer, Thomas P. Hemmerich, Peter eng

Dateiabrufe seit 01.10.2014 (Informationen über die Zugriffsstatistik)

Eur_J_Biochem_1972_WalkerStudies_on_succinate_dehydrogenase._8.pdf 109

Das Dokument erscheint in:

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

KOPS Suche


Stöbern

Mein Benutzerkonto