論文

査読有り 国際誌
2020年5月19日

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

Proceedings of the National Academy of Sciences of the United States of America
  • Takeshi Murakawa
  • ,
  • Kazuo Kurihara
  • ,
  • Mitsuo Shoji
  • ,
  • Chie Shibazaki
  • ,
  • Tomoko Sunami
  • ,
  • Taro Tamada
  • ,
  • Naomine Yano
  • ,
  • Taro Yamada
  • ,
  • Katsuhiro Kusaka
  • ,
  • Mamoru Suzuki
  • ,
  • Yasuteru Shigeta
  • ,
  • Ryota Kuroki
  • ,
  • Hideyuki Hayashi
  • ,
  • Takato Yano
  • ,
  • Katsuyuki Tanizawa
  • ,
  • Motoyasu Adachi
  • ,
  • Toshihide Okajima

117
20
開始ページ
10818
終了ページ
10824
記述言語
英語
掲載種別
DOI
10.1073/pnas.1922538117

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-derived redox cofactor, topa quinone (TPQ). We solved hitherto unknown structures of the active site, including a keto/enolate equilibrium of the cofactor with a nonplanar quinone ring, unusual proton sharing between the cofactor and the catalytic base, and metal-induced deprotonation of a histidine residue that coordinates to the Cu. 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.

リンク情報
DOI
https://doi.org/10.1073/pnas.1922538117
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/32371483