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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Bibliografische gegevens
Gepubliceerd in:Proc Natl Acad Sci U S A
Hoofdauteurs: 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
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: National Academy of Sciences 2020
Onderwerpen:
Biological Sciences
Online toegang: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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