Copper-Oxygen Dynamics in the Tyrosinase Mechanism.
Angew Chem Int Ed Engl
; 59(32): 13385-13390, 2020 08 03.
Article
em En
| MEDLINE
| ID: mdl-32356371
ABSTRACT
The dinuclear copper enzyme, tyrosinase, activates O2 to form a (µ-η2η2 -peroxido)dicopper(II) species, which hydroxylates phenols to catechols. However, the exact mechanism of phenolase reaction in the catalytic site of tyrosinase is still under debate. We herein report the near atomic resolution X-ray crystal structures of the active tyrosinases with substrate l-tyrosine. At their catalytic sites, CuA moved toward l-tyrosine (CuA1 â CuA2), whose phenol oxygen directly coordinates to CuA2, involving the movement of CuB (CuB1 â CuB2). The crystal structures and spectroscopic analyses of the dioxygen-bound tyrosinases demonstrated that the peroxide ligand rotated, spontaneously weakening its O-O bond. Thus, the copper migration induced by the substrate-binding is accompanied by rearrangement of the bound peroxide species so as to provide one of the peroxide oxygen atoms with access to the phenol substrate's ϵâ
carbon atom.
Palavras-chave
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Oxigênio
/
Tirosina
/
Monofenol Mono-Oxigenase
/
Cobre
Idioma:
En
Revista:
Angew Chem Int Ed Engl
Ano de publicação:
2020
Tipo de documento:
Article
País de afiliação:
Japão