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Copper-Oxygen Dynamics in the Tyrosinase Mechanism.
Fujieda, Nobutaka; Umakoshi, Kyohei; Ochi, Yuta; Nishikawa, Yosuke; Yanagisawa, Sachiko; Kubo, Minoru; Kurisu, Genji; Itoh, Shinobu.
Afiliação
  • Fujieda N; Department of Applied Life Sciences, Graduate School of Life and Environmental Sciences, Osaka Prefecture University, 1-1 Gakuen-cho, Naka-ku, Sakai-shi, Osaka, 599-8531, Japan.
  • Umakoshi K; Department of Material and Life Science, Graduate School of Engineering, Osaka University, 2-1 Yamada-oka, Suita, Osaka, 565-0871, Japan.
  • Ochi Y; Department of Applied Life Sciences, Graduate School of Life and Environmental Sciences, Osaka Prefecture University, 1-1 Gakuen-cho, Naka-ku, Sakai-shi, Osaka, 599-8531, Japan.
  • Nishikawa Y; Institute for Protein Research, Osaka University, 3-2 Yamada-oka, Suita, Osaka, 565-0871, Japan.
  • Yanagisawa S; Graduate School of Life Science, University of Hyogo, 3-2-1 Kouto, Kamigori-cho, Ako-gun, Hyogo, 678-1297, Japan.
  • Kubo M; Graduate School of Life Science, University of Hyogo, 3-2-1 Kouto, Kamigori-cho, Ako-gun, Hyogo, 678-1297, Japan.
  • Kurisu G; Institute for Protein Research, Osaka University, 3-2 Yamada-oka, Suita, Osaka, 565-0871, Japan.
  • Itoh S; Department of Material and Life Science, Graduate School of Engineering, Osaka University, 2-1 Yamada-oka, Suita, Osaka, 565-0871, Japan.
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 → CuA2), whose phenol oxygen directly coordinates to CuA2, involving the movement of CuB (CuB1 → 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 ϵ carbon atom.
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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

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