[Mechanism of action of D-amino acid oxidase. II. Evidence for the free radical mechanism of the reaction catalysed by the monomer form of the enzyme].
D-Amino acid oxidase was shown to dissociate into subunits in 2 M urea retaining the catalytic activity. This makes possible the direct observation of ESR spectra of the intermediate radical state of the enzyme when interacting with the substrate. We have shown that these radicals are really observable. Using the reversibility of the reaction and an equilibrium shift the amount of radicals can be increased up to 10% of all flavin groups present. The dependence of the radicals concentration on the amount of substrate and product can be predicted. The theory is confirmed by experimental data.
D003605:D-Amino-Acid Oxidase / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D005182:Flavin-Adenine Dinucleotide; D005609:Free Radicals; D007700:Kinetics; D046911:Macromolecular Substances; D008433:Mathematics
D005609:Free Radicals; D046911:Macromolecular Substances; D005182:Flavin-Adenine Dinucleotide; D003605:D-Amino-Acid Oxidase
Izuchenie mekhanizma deĭstviia oksidazy D-aminokislot. II. Dokazatel'stvo svobodno-radikal'nogo mekhanizma reaktsii monomernoĭ formy fermenta.