期刊
INORGANICA CHIMICA ACTA
卷 361, 期 4, 页码 1202-1206出版社
ELSEVIER SCIENCE SA
DOI: 10.1016/j.ica.2007.05.029
关键词
laccase; Trametes versicolor; TEMPO; MHQ
Laccase from Trametes versicolor reduces dioxygen to water. The enzyme is used in green chemistry applications such as the selective oxidation of alcohols in the presence of a suitable mediator (TEMPO) or in biofuel cells. We studied the catalytic mechanism of the enzyme by the stopped-flow and our newly developed rapid-mixing rapid sampling method, which has an experimental dead time of 75 +/- 15 mu s. Equilibrium and kinetic analyses yielded a reduction potential of 717 +/- 5 mV for Type 1 copper center. EPR and low-temperature UV-Vis spectroscopy indicate that oxidation of the blue copper center and O=O bond splitting occur within 100 mu s, without detectable formation of a peroxide intermediate. These results indicate a rapid internal electron transfer between the various copper centers (> 25.000/s) and rapid binding of O-2 (k(on) > 5 x 10(7) M-1 s(-1)). Mechanistic aspects of the catalytic cycle are shortly discussed. (C) 2007 Elsevier B.V. All rights reserved.
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