Myoglobin Reconstituted with Ni Tetradehydrocorrin as a Methane‐Generating Model of Methyl‐coenzyme M Reductase-Reference-Cited by-同舟云学术

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Myoglobin Reconstituted with Ni Tetradehydrocorrin as a Methane‐Generating Model of Methyl‐coenzyme M Reductase

Published:2019-08-23 Issue:39 Volume:58 Page:13813-13817
ISSN:1433-7851
Container-title:Angewandte Chemie International Edition
language:en
Short-container-title:Angew. Chem. Int. Ed.

Author:

Oohora Koji¹²^ORCID,Miyazaki Yuta¹,Hayashi Takashi¹^ORCID

Affiliation:

1. Department of Applied Chemistry Graduate School of Engineering Osaka University 2-1 Yamadaoka Suita 565-0871 Japan

2. Frontier Research Base for Global Young Researchers Graduate School of Engineering Osaka University 2-1 Yamadaoka Suita 565-0871 Japan

Funder

Japan Society for the Promotion of Science

Precursory Research for Embryonic Science and Technology

Publisher

Wiley

Subject

General Chemistry,Catalysis

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/anie.201907584

Reference35 articles.

1. Biosynthesis of dimethylarsine by methanobacterium

2. Methane formation from methyl-coenzyme M in a system containing methyl-coenzyme M reductase, component B and reduced cobalamin

3. The key nickel enzyme of methanogenesis catalyses the anaerobic oxidation of methane

4. A conspicuous nickel protein in microbial mats that oxidize methane anaerobically

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1. Redox Engineering of Myoglobin by Cofactor Substitution to Enhance Cyclopropanation Reactivity;Angewandte Chemie International Edition;2024-07-04

2. Redox Engineering of Myoglobin by Cofactor Substitution to Enhance Cyclopropanation Reactivity;Angewandte Chemie;2024-07-04

3. Intramolecular C-H bond amination catalyzed by myoglobin reconstituted with iron porphycene;Journal of Inorganic Biochemistry;2024-03

4. Electronic isomerism in a heterometallic nickel–iron–sulfur cluster models substrate binding and cyanide inhibition of carbon monoxide dehydrogenase;Chemical Science;2024

5. Diversifying the functions of heme proteins with non-porphyrin cofactors;Journal of Inorganic Biochemistry;2023-09

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