@article{ref1,
title="Studies of the competing rates of catechol oxidation and suicide inactivation of tyrosinase",
journal="Arkivoc",
year="2010",
author="Ramsden, C.A. and Riley, P.A.",
volume="2010",
number="10",
pages="248-254",
abstract="Tyrosinase oxidation of catechols to ortho-quinones is accompanied by suicide inactivation of the enzyme. The rates of these competing processes vary and depend on the nature of ring substituents. For a series of 4-substituted catechols the relationships between structure and reaction rates have been examined using multiple regression. Significant but different structure-rate relationships were found for each process. The oxidation rate (k1) is greatest for short hydrophobic substituents; there is an optimum substituent hydrophobicity (π ̃ 0.7) for the rate of inactivation (k2). © ARKAT USA, Inc.<p /><p>Language: en</p>",
language="en",
issn="1551-7012",
doi="10.3998/ark.5550190.0011.a20",
url="http://dx.doi.org/10.3998/ark.5550190.0011.a20"
}