Unsymmetrical Binding Modes of the HOPNO Inhibitor of Tyrosinase: From Model Complexes to the Enzyme.
The deciphering of the binding mode of tyrosinase (Ty) inhibitors is essential to understand how to regulate the tyrosinase activity. In this paper, by combining exptl. and theor. methods, we studied an unsym. tyrosinase functional model and its interaction with 2-hydroxypyridine-N-oxide (HOPNO), a new and efficient competitive inhibitor for bacterial Ty. The tyrosinase model was a dinuclear copper complex bridged by a chelated ring with two different complexing arms (namely (bis(2-ethylpyridyl)amino)methyl and (bis(2-methylpyridyl)amino)methyl). The geometrical asymmetry of the complex induces an unsym. binding of HOPNO. Comparisons have been made with the binding modes obtained on similar sym. complexes. Finally, by using quantum mechanics/mol. mechanics (QM/MM) calcns., we studied the binding mode in tyrosinase from a bacterial source. A new unsym. binding mode was obtained, which was linked to the second coordination sphere of the enzyme. [on SciFinder(R)]
Références
- Titre
- Unsymmetrical Binding Modes of the HOPNO Inhibitor of Tyrosinase: From Model Complexes to the Enzyme.
- Type de publication
- Article de revue
- Année de publication
- 2013
- Auteurs
- Bochot, Constance, Favre Elisabeth, Dubois Carole, Baptiste Benoit, Bubacco Luigi, Carrupt Pierre-Alain, Gellon Gisèle, Hardre Renaud, Luneau Dominique, Moreau Yohann, Nurisso Alessandra, Reglier Marius, Serratrice Guy, Belle Catherine, and Jamet Hélène
- Revue
- Chem. - A Eur. J.
- Volume
- 19
- Pagination
- 3655–3664
- ISSN
- 0947-6539
Soumis le 12 avril 2018