@article{ref1,
title="Indirect inactivation of tyrosinase in its action on 4-tert-butylphenol",
journal="Journal of enzyme inhibition and medicinal chemistry",
year="2014",
author="Muñoz-Muñoz, J.L. and García-Molina, M.D.M. and García-Molina, F. and Varon, R. and García-Ruiz, P.A. and Rodríguez-López, J.N. and García-Cánovas, F.",
volume="29",
number="3",
pages="344-352",
abstract="Under anaerobic conditions, the o-diphenol 4-tert-butylcatechol (TBC) irreversibly inactivates met and deoxytyrosinase enzymatic forms of tyrosinase. However, the monophenol 4-tert-butylphenol (TBF) protects the enzyme from this inactivation. Under aerobic conditions, the enzyme suffers suicide inactivation when it acts on TBC. We suggest that TBF does not directly cause the suicide inactivation of the enzyme in the hydroxylase activity, but that the o-diphenol, which is necessary for the system to reach the steady state, is responsible for the process. Therefore, monophenols do not induce the suicide inactivation of tyrosinase in its hydroxylase activity, and there is a great difference between the monophenols that give rise to unstable o-quinones such as L-tyrosine, which rapidly accumulate L-dopa in the medium and those like TBF, after oxidation, give rise to a very stable o-quinone. © 2014 Informa UK Ltd.<p /><p>Language: en</p>",
language="en",
issn="1475-6366",
doi="10.3109/14756366.2013.782298",
url="http://dx.doi.org/10.3109/14756366.2013.782298"
}