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 mu-eta2:eta2-peroxidodicopper(II) species, and that this remains the only enzyme species under turnover and substrate saturation conditions.
Spada
Alessia
A
Dipartimento di Chimica Generale, Università di Pavia, viale Taramelli 12, 27100, Pavia, Italy.
Palavicini
Sara
S
Monzani
Enrico
E
Bubacco
Luigi
L
Casella
Luigi
L
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
D010636:Phenols; D003300:Copper; D014442:Monophenol Monooxygenase