Biocatalytic oxidation of flavone analogues mediated by general biocatalysts: horseradish peroxidase and laccase.

Horseradish peroxidase (HRP) and laccase are well known oxidases, which have been widely applied for the biosynthesis of organic compounds. In the present work, flavone analogues as an important type of bioactive natural product could be oxidized by HRP or laccase, which afforded dimeric and oxidative flavones. All of the flavone analogues usually possessing phenolic groups could be transformed using HRP. However, only flavonols, isoflavones and chalcones with phenolic groups and dihydroxylflavones were effective substrates of laccase. The radical reaction mechanism with the B-ring of flavone analogues as the radical reaction trigger was proposed for the oxidation of flavones. molecular docking analyses for assaying the interaction between flavone analogues and oxidases indicated that the phenolic groups at the B rings of flavones docked into the HEME active pocket of HRP well. Kinetic behaviors of the oxidation for various flavone analogues mediated by HRP or laccase displayed Hill and substrate inhibition kinetic models. Therefore, in the present work, the oxidation of various flavone analogues mediated by HRP or laccase has been successfully characterized, which would be helpful for the preparation of flavone derivatives.