Rogozhin V V, Peretolchin D V
Yakutsk State Agricultural Academy, Yakutsk, Russia.
Bioorg Khim. 2009 Sep-Oct;35(5):640-5. doi: 10.1134/s1068162009050069.
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.
研究了辣根过氧化物酶催化二氢槲皮素氧化的稳态动力学。结果表明，二氢槲皮素是辣根过氧化物酶的一种缓慢氧化底物。在水 - 醇溶液和缓冲溶液中发现了两种选择性参与过氧化物酶诱导氧化的二氢槲皮素异构体（顺式和反式）。在4.5 - 8.0的pH范围内测定了催化常数（k(cat)）和米氏常数（K(m)）。
