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Issue 33, 2009
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Trapping tyrosinase key active intermediate under turnover

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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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Publication details

The article was received on 10 Jun 2009, accepted on 26 Jun 2009 and first published on 15 Jul 2009


Article type: Communication
DOI: 10.1039/B911946A
Citation: Dalton Trans., 2009, 6468-6471
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    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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