Walker 1970 J Biol Chem
| Walker WH, Singer TP (1970) Identification of the covalently bound flavin of succinate dehydrogenase as 8-alpha-(histidyl) flavin adenine dinucleotide. J Biol Chem 245:4224-5 |
Walker WH, Singer TP (1970) J Biol Chem
Abstract: Acid hydrolysis of flavin peptides from the active center of mammalian succinate dehydrogenase yields a substituted riboflavin which was isolated in pure form. It contains a substituent attached to position 8a of riboflavin. Drastic acid hydrolysis of this compound and catalytic hydrogenation yield nearly 1 mole of free histidine. Histidine is also liberated on neutral photolysis. The presence of histidine is confirmed by behavior on high voltage electrophoresis at various pH values and by acid titration curves. Linkage of the 8cr-CHs group of riboflavin is to one of the imidazole ring nitrogens since neither the flavin peptide nor its acid derivative give a Pauly reaction. This assignment is in full accord with the characteristic pH-fluorescence curve of covalently bound flavin. The pK of the fluorescence quenching agrees with that expected for the imidazole nitrogen in histidyl flavin.
• Bioblast editor: Gnaiger E
Selected quotes
- It has been known for many years that succinate dehydrogenase from aerobic cells contains FAD covalently linked to the protein (1).
Labels:
Organism: Bovines
Tissue;cell: Heart
Preparation: Enzyme
Enzyme: Complex II;succinate dehydrogenase
