[Kinetic regulations of dihydroquercetin oxidation with horseradish peroxide].
The steady-state kinetics of horseradish peroxidase-catalyzed dihydroquercetin oxidation was studied. Dihydroquercetin was shown to be a slowly oxidized substrate of horseradish peroxidase. Two dihydroquercetin isoforms (cis and trans forms) that were selectively involved in peroxidase-induced oxidation were found in water-alcohol and buffer solutions. The k(cat) and K(m) were determined in the pH range of 4.5-8.0.
Rogozhin
V V
VV
Yakutsk State Agricultural Academy, Yakutsk, Russia. vrogozhin@mail.ru
Peretolchin
D V
DV
D006735:Horseradish Peroxidase / Q000737:chemistry*; D007700:Kinetics; D010084:Oxidation-Reduction; D011794:Quercetin / Q000031:analogs & derivatives* / Q000737:chemistry
D011794:Quercetin; C003377:taxifolin; D006735:Horseradish Peroxidase