Neutron crystallography of copper amine oxidase reveals keto/enolate interconversion of the quinone cofactor and unusual proton sharing

Recent advances in neutron crystallographic studies have provided structural bases for quantum behaviors of protons observed in enzymatic reactions. Thus, we resolved the neutron crystal structure of a bacterial copper (Cu) amine oxidase (CAO), which contains a prosthetic Cu ion and a protein-derive...

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Detalles Bibliográficos
Publicado en:Proc Natl Acad Sci U S A
Main Authors: Murakawa, Takeshi, Kurihara, Kazuo, Shoji, Mitsuo, Shibazaki, Chie, Sunami, Tomoko, Tamada, Taro, Yano, Naomine, Yamada, Taro, Kusaka, Katsuhiro, Suzuki, Mamoru, Shigeta, Yasuteru, Kuroki, Ryota, Hayashi, Hideyuki, Yano, Takato, Tanizawa, Katsuyuki, Adachi, Motoyasu, Okajima, Toshihide
Formato: Artigo
Idioma:Inglês
Publicado: National Academy of Sciences 2020
Assuntos:
Biological Sciences
Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC7245091/
https://ncbi.nlm.nih.gov/pubmed/32371483
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1922538117
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