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Issue 6, 2003
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Theoretical study of phenol and 2-aminophenol docking at a model of the tyrosinase active site

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Abstract

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.

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Article information


Submitted
21 Oct 2002
Accepted
18 Feb 2003
First published
15 May 2003

New J. Chem., 2003,27, 909-913
Article type
Paper

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

J. Piquemal, J. Maddaluno, B. Silvi and C. Giessner-Prettre, New J. Chem., 2003, 27, 909
DOI: 10.1039/B210307A

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