Unique protonation states of aspartate and topaquinone in the active site of copper amine oxidase-Reference-Cited by-同舟云学术

Unique protonation states of aspartate and topaquinone in the active site of copper amine oxidase

Published:2020 Issue:63 Volume:10 Page:38631-38639
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Shoji Mitsuo¹²³⁴⁵^ORCID,Murakawa Takeshi⁶⁷⁸⁴,Boero Mauro⁹¹⁰¹¹¹²¹³^ORCID,Shigeta Yasuteru¹²³⁴^ORCID,Hayashi Hideyuki¹⁴⁷⁸⁴,Okajima Toshihide¹⁴⁷⁸⁴¹⁵

Affiliation:

1. Center for Computational Sciences

2. University of Tsukuba

3. Tsukuba

4. Japan

5. JST-PRESTO

6. Department of Biochemistry

7. Osaka Medical College

8. Takatsuki

9. University of Strasbourg

10. Institut de Physique et Chimie des Matériaux de Strasbourg

11. CNRS

12. UMR 7504

13. France

14. Department of Chemistry

15. Institute of Scientific and Industrial Research

Abstract

Copper amine oxidases catalyze the oxidative deamination of biogenic amines. We investigated the unique protonation states in the active site using first-principle calculations.

Funder

Japan Society for the Promotion of Science

Grand Équipement National De Calcul Intensif

Japan Science and Technology Agency

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2020/RA/D0RA06365G

Reference26 articles.

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