Binding of 2-Hydroxypyridine-N-oxide on Dicopper(II) Centers: Insights into Tyrosinase Inhibition Mechanism by Transition-State Analogs

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• 作者：Eugnie Peyroux ; Wadih Ghattas ; Renaud Hardr ; Michel Giorgi ; Bruno Faure ; A. Jalila Simaan ; Catherine Belle ; Marius Rglier
• 刊名：Inorganic Chemistry
• 出版年：2009
• 出版时间：December 7, 2009
• 年：2009
• 卷：48
• 期：23
• 页码：10874-10876
• 全文大小：691K
• 年卷期：v.48,no.23(December 7, 2009)
• ISSN：1520-510X

文摘

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 μM and a K_I = 1.8 μM. Using the binuclear copper(II) complex [Cu₂(BPMP)(μ−OH)](ClO₄)₂ (2) known as a functional model for the tyrosinase catecholase activity, we isolated and fully characterized a 1:1 (2)/OPNO adduct 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.