Inhibitory effect of Bis(2-chlorobenzaldehyde)phenyl disulphide diimine on mushroom polyphenol oxidase

ABSTRACT: The inhibitory effect of Bis(2-chlorobenzaldehyde)phenyldisulphide diimine on both activities of mushroom polyphenol oxidase at (20)°C in a 10 mM phosphate buffer solution (pH 6.8), was studied. L-Dopa and L-Tyrosine were used as substrates of catecholase and cresolase activities, respectively. The results showed that ligand competitively inhibits both activities of the enzyme with inhibition constants (Ki) of 0.5 ± 0.01 and 0.4 ± 0.02?M for catecholase and cresolase respectively, which are good valuses comparing with the reported values for other inhibitors. For further insight a docking study between polyphenol oxidase and ligand was performed. The docking simulation showed that ligand binds in the active site of the enzyme near the Cu atoms.