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
- 巻
- 117
- 号
- 20
- 開始ページ
- 10818
- 終了ページ
- 10824
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1073/pnas.1922538117
- 出版者・発行元
- NATL ACAD SCIENCES
© 2020 National Academy of Sciences. All rights reserved. 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
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000535585100034&DestApp=WOS_CPL
- Scopus
- https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85084961941&origin=inward
- Scopus Citedby
- https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=85084961941&origin=inward
- ID情報
-
- DOI : 10.1073/pnas.1922538117
- ISSN : 0027-8424
- eISSN : 1091-6490
- PubMed ID : 32371483
- SCOPUS ID : 85084961941
- Web of Science ID : WOS:000535585100034