期刊
CHEMISTRY-A EUROPEAN JOURNAL
卷 19, 期 11, 页码 3655-3664出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.201202643
关键词
bioinorganic chemistry; copper; density functional calculations; enzymes; inhibitors
资金
- French Agence Nationale pour la Recherche [ANR-09-BLAN-0028-01/02]
- Agence Nationale de la Recherche (ANR) [ANR-09-BLAN-0028] Funding Source: Agence Nationale de la Recherche (ANR)
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 experimental and theoretical methods, we studied an unsymmetrical 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 unsymmetrical binding of HOPNO. Comparisons have been made with the binding modes obtained on similar symmetrical complexes. Finally, by using quantum mechanics/molecular mechanics (QM/MM) calculations, we studied the binding mode in tyrosinase from a bacterial source. A new unsymmetrical binding mode was obtained, which was linked to the second coordination sphere of the enzyme.
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