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• W2123457980 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." @default.
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• W2123457980 date "2003-01-01" @default.
• W2123457980 modified "2023-10-14" @default.
• W2123457980 title "Theoretical study of phenol and 2-aminophenol docking at a model of the tyrosinase active site" @default.
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• W2123457980 doi "https://doi.org/10.1039/b210307a" @default.
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