| Literature DB >> 16366523 |
Shun Hirota1, Takumi Kawahara, Emanuela Lonardi, Ellen de Waal, Noriaki Funasaki, Gerard W Canters.
Abstract
Tyrosinases catalyze the o-hydroxylation of monophenols (monophenolase activity) and the oxidation of o-diphenols to o-quinones (diphenolase activity) and possess a dinuclear copper active site. The O2 binding kinetics of oxytyrosinase is studied by flash-photolysis measurements, and the O2 binding rate constant (kO2) is obtained as kO2 = 13 +/- 3 muM-1 s-1. Small molecules, such as carbon monoxide and p-nitrophenol (a substrate-analogue inhibitor), are demonstrated to affect O2 binding kinetics. The activation enthalpy of the rate-limiting step of O2 binding is calculated by the temperature dependence of kO2 to be 12.8 +/- 2.6 kcal/mol.Entities:
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Year: 2005 PMID: 16366523 DOI: 10.1021/ja0541128
Source DB: PubMed Journal: J Am Chem Soc ISSN: 0002-7863 Impact factor: 15.419