Theoretical study of phenol and 2-aminophenol docking at a model of the tyrosinase active site

被引：15
作者：
Piquemal, JP
Maddaluno, J
Silvi, B
Giessner-Prettre, C
机构：
[1] Univ Paris 06, Chim Theor Lab, F-75252 Paris 05, France
[2] Univ Rouen, IRCOF, Lab Fonct Azotees & Oxygenees Complexes, F-76821 Mont St Aignan, France
来源：
NEW JOURNAL OF CHEMISTRY | 2003年 / 27卷 / 06期
关键词：
D O I：
10.1039/b210307a
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
DFT calculations using the B3LYP functional are reported for a model of the (oxy) tyrosinase active site including the two copper cations, six imidazoles and dioxygen (in the oxy form), plus either phenol (taken as a model of tyrosine, the enzyme's natural substrate) or 2-aminophenol, a very efficient inhibitor. The results obtained suggest that (i) both the substrate and the inhibitor have to be deprotonated to form a stable complex with the model of the "native'' form of the enzyme; (ii) only phenol binds to the oxy form; (iii) the complex formed between our oxy model and 2-aminophenate is more stable than that with phenate, suggesting a competitive inhibition mechanism between the deprotonated forms of the substrate and of the inhibitor.
引用
收藏
页码：909 / 913
页数：5
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