Trapping tyrosinase key active intermediate under turnover

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 l–g2:g2-peroxidodicopper(II) species, and that
this remains the only enzyme species under turnover and
substrate saturation conditions