title: Monooxygenation of an appended phenol in a model system of tyrosinase: implications on the enzymatic reaction mechanism.
abstract: A new tridentate N-donor ligand and its corresponding copper(i) complex have been synthesized to investigate the tyrosinase-like aromatic hydroxylation of an attached phenol. The results of the oxygenation reactions are compared to related systems having attached phenyl and catechol groups, respectively. The title complex is the first system mediating the monooxygenation of a phenol in the absence of an external base.
authors.affiliation: Christian-Albrechts-University Kiel, Max-Eyth-Straße 2, 24118 Kiel, Germany. ftuczek@ac.uni-kiel.de.
authors.forename: Jessica Nadine
authors.initials: JN
authors.lastname: Hamann
authors.forename: Malte
authors.initials: M
authors.lastname: Rolff
authors.forename: Felix
authors.initials: F
authors.lastname: Tuczek
mesh_terms: D004789:Enzyme Activation; D008956:Models, Chemical; D014442:Monophenol Monooxygenase / Q000737:chemistry* / Q000378:metabolism*; D019800:Phenol / Q000737:chemistry / Q000378:metabolism
chemical_list: D019800:Phenol; D014442:Monophenol Monooxygenase