Molecular mechanism of a large conformational change of the quinone cofactor in the semiquinone intermediate of bacterial copper amine oxidase-Reference-Cited by-同舟云学术

Molecular mechanism of a large conformational change of the quinone cofactor in the semiquinone intermediate of bacterial copper amine oxidase

Published:2022 Issue:36 Volume:13 Page:10923-10938
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Shoji Mitsuo¹²^ORCID,Murakawa Takeshi³^ORCID,Nakanishi Shota⁴,Boero Mauro⁵^ORCID,Shigeta Yasuteru¹^ORCID,Hayashi Hideyuki⁶^ORCID,Okajima Toshihide⁴⁶^ORCID

Affiliation:

1. Center for Computational Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba 305-8577, Ibaraki, Japan

2. JST-PRESTO, 4-1-8 Honcho, Kawaguchi 332-0012, Saitama, Japan

3. Department of Biochemistry, Osaka Medical and Pharmaceutical University, 2-7 Daigakumachi, Takatsuki 569-8686, Osaka, Japan

4. Institute of Scientific and Industrial Research, Osaka University, 8-1 Mihogaoka, Ibaraki 567-0047, Osaka, Japan

5. University of Strasbourg, Institut de Physique et Chimie des Matériaux de Strasbourg, CNRS, UMR 7504, 23 rue du Loess, F-67034, France

6. Department of Chemistry, Osaka Medical and Pharmaceutical University, 2-7 Daigakumachi, Takatsuki 569-8686, Osaka, Japan

Abstract

The large conformational change of topaquinone in bacterial copper amine oxidase occurs through the TPQ ring rotation and slide, which are essential to stabilize the semiquinone form.

Funder

Precursory Research for Embryonic Science and Technology

Ministry of Education, Culture, Sports, Science and Technology

Japan Society for the Promotion of Science

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2022/SC/D2SC01356H

Reference60 articles.

1. Swinging Arms and Swinging Domains in Multifunctional Enzymes: Catalytic Machines for Multistep Reactions