The molecular mechanism of inhibition on tyrosinase activity by luteolin was studied by enzyme kinetics experiment,fluorescence quenching experiment and molecular docking simulation.The enzyme inhibition kinetics experiment results showed that luteolin inhibited the activity of tyrosinase as a non-competitive inhibitor.The inhibition constants KI and IC50 were 86 mmol/L and 778.2 μmol/L,respectively.The fluorescence quenching experiment results showed that the interactions between luteolin and tyrosinase did not change the secondary structure of tyrosinase.As a static quenching,both hydrophobic interaction and hydrogen bonding stabilized the composite structure.Molecular docking simulation showed that the interaction between luteolin and amino acid residues in the hydrophobic pocket of tyrosinase existed.The interaction force mainly included hydrophobic interaction and hydrogen bonding.