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

Trapping tyrosinase key active intermediate under turnover

SPADA, ALESSIA;MONZANI, ENRICO;CASELLA, LUIGI
2009-01-01

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 l–g2:g2-peroxidodicopper(II) species, and that this remains the only enzyme species under turnover and substrate saturation conditions
File in questo prodotto:
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11571/202589
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 23
  • ???jsp.display-item.citation.isi??? 21
social impact