Trapping tyrosinase key active intermediate under turnover??

Dalton Transactions Pub Date: 2009-07-15 DOI: 10.1039/B911946A

Abstract

This paper shows for the first time that the spectral features of the ternary complex of tyrosinase/O2/phenol, trapped at low temperature using the very slow substrate 3,5-difluorophenol, are those of a μ–η2:η2-peroxidodicopper(II) species, and that this remains the only enzyme species under turnover and substrate saturation conditions.

Graphical abstract: Trapping tyrosinase key active intermediate under turnover
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