title: 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 mu-eta2:eta2-peroxidodicopper(II) species, and that this remains the only enzyme species under turnover and substrate saturation conditions.
authors: Dipartimento di Chimica Generale, Università di Pavia, viale Taramelli 12, 27100, Pavia, Italy.
authors: Alessia
authors: A
authors: Spada
authors: Sara
authors: S
authors: Palavicini
authors: Enrico
authors: E
authors: Monzani
authors: Luigi
authors: L
authors: Bubacco
authors: Luigi
authors: L
authors: Casella
mesh_terms: D002384:Catalysis; D003300:Copper / Q000737:chemistry; D014442:Monophenol Monooxygenase / Q000737:chemistry / Q000378:metabolism*; D010636:Phenols / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet; D013303:Streptomyces antibioticus / Q000201:enzymology; D013696:Temperature
chemical_list: D010636:Phenols; D003300:Copper; D014442:Monophenol Monooxygenase