Oxidation of baicalein by tyrosinase and by o-quinones.

Baicalein (5,6,7-trihydroxyflavone) has been previously described as an inhibitor of tyrosinase (Guo et al. Int. J. Biol. Macromol. 118 (2018) 57-68). However, long before this article was published this flavonoid had been shown to be a substrate of this enzyme and a catecholic cofactor partially abolishing the lag-phase during oxidation of l-tyrosine. Other compounds with a 1,2,3-triphenol moiety, such as pyrogallol, gallic acid and its esters are also oxidized by tyrosinase. Gallic acid was also shown to reduce tyrosinase-generated o-quinones. We have demonstrated that baicalein is also rapidly oxidized by o-quinones generated from catechols by tyrosinase or by treatment with sodium periodate. Smaller changes of absorbance at 475 nm during oxidation of l-dopa by tyrosinase in the presence of baicalein do not result from enzyme inhibition but from reduction of dopaquinone by baicalein. This reaction prevents formation of dopachrome giving an effect of inhibition, which is only apparent. The actual reaction rates did not decrease but increased in the presence of baicalein, which we demonstrated by measurements of oxygen consumption.