Inhibitory effect of ammonium tetrathiotungstate on tyrosinase and its kinetic mechanism.

Kyung-Hee Park, Jae-Rin Lee, Hwa-Sun Hahn, Young-Hoon Kim, Chang-Dae Bae, Jun-Mo Yang, Sangtaek Oh, Yu-Jin Bae, Dong-Eun Kim, Myong-Joon Hahn

Index: Chem. Pharm. Bull. 54(9) , 1266-70, (2006)

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Abstract

Tyrosinase requires two copper ions at the active site, in order to oxidize phenols to catechols. In this study, the inhibitory effect of the copper-chelating compound, ammonium tetrathiotungstate (ATTT), on the tyrosinase activity was investigated. ATTT was determined to inactivate the activity of mushroom tyrosinase, in a dose-dependent manner. The kinetic substrate reaction revealed that ATTT functions as a kinetically competitive inhibitor in vitro, and that the enzyme-ATTT complex subsequently undergoes a reversible conformational change, resulting in the inactivation of tyrosinase. In human melanin-producing cells, ATTT evidenced a more profound tyrosinase-inhibitory effect than has been seen in the previously identified tyrosinase inhibitors, including kojic acid and hydroquinone. Our results may provide useful information for the development of whitening agent.