Issue 33, 2009

Trapping tyrosinase key active intermediate under turnover

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

Supplementary files

Article information

Article type
Communication
Submitted
10 Jun 2009
Accepted
26 Jun 2009
First published
15 Jul 2009

Dalton Trans., 2009, 6468-6471

Trapping tyrosinase key active intermediate under turnover

A. Spada, S. Palavicini, E. Monzani, L. Bubacco and L. Casella, Dalton Trans., 2009, 6468 DOI: 10.1039/B911946A

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