Binding of 2-Hydroxypyridine-N-oxide on Dicopper(II) Centers: Insights into Tyrosinase Inhibition Mechanism by Transition-State Analogs.
2-Hydroxypyridine-N-oxide (HOPNO) is described as a new and efficient transition-state analog (TS-analog) inhibitor for the mushroom tyrosinase with an IC50 = 1.16 $μ$M and a KI = 1.8 $μ$M. Using the binuclear copper(II) complex [Cu2(BPMP)($μ$-OH)](ClO4)2 (2) known as a functional model for the tyrosinase catecholase activity, a 1:1 (2)/OPNO adduct was isolated and fully characterized in which the HOPNO is deprotonated and chelates only one Cu-atom of the binuclear site in a bidentate mode. On the basis of these results, a structural model for the tyrosinase inhibition by HOPNO is proposed. [on SciFinder(R)]
Références
- Titre
- Binding of 2-Hydroxypyridine-N-oxide on Dicopper(II) Centers: Insights into Tyrosinase Inhibition Mechanism by Transition-State Analogs.
- Type de publication
- Article de revue
- Année de publication
- 2009
- Auteurs
- Peyroux, Eugenie, Ghattas Wadih, Hardre Renaud, Giorgi Michel, Faure Bruno, A Simaan Jalila, Belle Catherine, and Reglier Marius.
- Revue
- Inorg. Chem.
- Volume
- 48
- Pagination
- 10874–10876
- ISSN
- 0020-1669
Soumis le 12 avril 2018