@article{oai:repo.qst.go.jp:00079969,
 author = {Murakawa, Takeshi and Kurihara, Kazuo and Shoji, Mitsuo and Shibazaki, Chie and Sunami, Tomoko and Tamada, Taro and Yano, Naomine and Yamada, Taro and Kusaka, Katsuhiro and Suzuki, Mamoru and Shigeta, Yasuteru and Kuroki, Ryota and Hayashi, Hideyuki and Yano, Takato and Tanizawa, Katsuyuki and Adachi, Motoyasu and Okajima, Toshihide and Kurihara, Kazuo and Shibazaki, Chie and Sunami, Tomoko and Tamada, Taro and Adachi, Motoyasu},
 issue = {20},
 journal = {Proceedings of the National Academy of Sciences of United States of America},
 month = {May},
 note = {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 amine oxidase, which contains a prosthetic copper ion and a protein-derived redox cofactor, topa quinone. We solved hitherto unknown structures of the active site, including a keto/enolate equilibrium of the cofactor with a non-planar quinone ring, unusual proton sharing between the cofactor and the catalytic base, and metal-induced deprotonation of a histidine residue that coordinates to the copper. Our findings show a refined active-site structure that gives detailed information on the protonation state of dissociable groups, such as the quinone cofactor, which are critical for catalytic reactions.},
 pages = {10818--10824},
 title = {Neutron crystallography of copper amine oxidase reveals keto/enolate interconversion of the quinone cofactor and unusual proton sharing},
 volume = {117},
 year = {2020}
}