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 mu-eta2:eta2-peroxidodicopper(II) species, and that this remains the only enzyme species under turnover and substrate saturation conditions.
Trapping tyrosinase key active intermediate under turnover
BUBACCO, LUIGI;
2009
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 mu-eta2:eta2-peroxidodicopper(II) species, and that this remains the only enzyme species under turnover and substrate saturation conditions.File in questo prodotto:
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