Quercetin as a tyrosinase inhibitor: Inhibitory activity, conformational change and mechanism

- Quercetin could inhibit both monophenolase and diphenolase activities of tyrosinase.
- Hydrophobic interaction dominated the binding of quercetin to tyrosinase.
- The binding of quercetin to tyrosinase induced conformational changes of tyrosinase.
- Catechol structure of quercetin chelated the copper in the active site of tyrosinase.

Quercetin, a flavonoid compound, was found to inhibit both monophenolase and diphenolase activities of tyrosinase, and its inhibition against diphenolase activity was in a reversible and competitive manner with an IC50 value of (3.08 ± 0.74) × 10− 5 mol L− 1. Quercetin bound to tyrosinase driven by hydrophobic interaction, thereby resulted in a conformational change of tyrosinase and its intrinsic fluorescence quenching. Tyrosinase had one binding site for quercetin with the binding constant in the order of magnitude of 104 L mol− 1. The molecular docking revealed that quercetin bound to the active site of tyrosinase and chelated a copper with the 3′, 4′-dihydroxy groups. It can be deduced that the chelation may prevent the entrance of substrate and then inhibit the catalytic activity of tyrosinase. These findings may be helpful to understand the inhibition mechanism of quercetin on tyrosinase and functional research of quercetin in the treatment of pigmentation disorders.

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