Copper–Oxygen Dynamics in the Tyrosinase Mechanism-Reference-Cited by-同舟云学术

Copper–Oxygen Dynamics in the Tyrosinase Mechanism

Published:2020-05-26 Issue:32 Volume:59 Page:13385-13390
ISSN:1433-7851
Container-title:Angewandte Chemie International Edition
language:en
Short-container-title:Angew. Chem. Int. Ed.

Author:

Fujieda Nobutaka¹^ORCID,Umakoshi Kyohei²,Ochi Yuta¹,Nishikawa Yosuke³,Yanagisawa Sachiko⁴,Kubo Minoru⁴,Kurisu Genji³^ORCID,Itoh Shinobu²^ORCID

Affiliation:

1. 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

2. Department of Material and Life Science Graduate School of Engineering Osaka University 2-1 Yamada-oka, Suita Osaka 565-0871 Japan

3. Institute for Protein Research Osaka University 3-2 Yamada-oka, Suita Osaka 565-0871 Japan

4. Graduate School of Life Science University of Hyogo 3-2-1 Kouto, Kamigori-cho, Ako-gun Hyogo 678-1297 Japan

Funder

Japan Society for the Promotion of Science

Core Research for Evolutional Science and Technology

Publisher

Wiley

Subject

General Chemistry,Catalysis

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/anie.202004733

Reference36 articles.

1. Crystallographic Evidence That the Dinuclear Copper Center of Tyrosinase Is Flexible during Catalysis

2. Crystal structure of Manduca sexta prophenoloxidase provides insights into the mechanism of type 3 copper enzymes

3. First Structures of an Active Bacterial Tyrosinase Reveal Copper Plasticity

4. Crystal Structure of Agaricus bisporus Mushroom Tyrosinase: Identity of the Tetramer Subunits and Interaction with Tropolone

5. Crystal Structures of Copper-depleted and Copper-bound Fungal Pro-tyrosinase

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