Nickel–Sulfonate Mode of Substrate Binding for Forward and Reverse Reactions of Methyl-SCoM Reductase Suggest a Radical Mechanism Involving Long-Range Electron Transfer-Reference-Cited by-同舟云学术

Nickel–Sulfonate Mode of Substrate Binding for Forward and Reverse Reactions of Methyl-SCoM Reductase Suggest a Radical Mechanism Involving Long-Range Electron Transfer

Published:2021-03-24 Issue:14 Volume:143 Page:5481-5496
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Patwardhan Anjali¹,Sarangi Ritimukta²^ORCID,Ginovska Bojana³^ORCID,Raugei Simone³^ORCID,Ragsdale Stephen W.¹^ORCID

Affiliation:

1. Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan 48103, United States

2. Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, California 94025, United States

3. Pacific Northwest National Laboratory, Richland, Washington 99354, United States

Funder

National Institute of General Medical Sciences

US Department of Energy, Office of Science, Basic Energy Sciences

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.1c01086

Reference69 articles.

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

2. Methyl-coenzyme M reductase and the anaerobic oxidation of methane in methanotrophic Archaea

3. Resolving a methane mystery

4. Continuing Worldwide Increase in Tropospheric Methane, 1978 to 1987

5. Methane and related trace species on Mars: Origin, loss, implications for life, and habitability

Cited by 14 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Toward the Use of Methyl-Coenzyme M Reductase for Methane Bioconversion Applications;Accounts of Chemical Research;2024-08-27

2. Structural Dynamics of the Methyl-Coenzyme M Reductase Active Site Are Influenced by Coenzyme F₄₃₀ Modifications;Biochemistry;2024-06-24

3. Structural dynamics of the methyl-coenzyme M reductase active site are influenced by coenzyme F₄₃₀modifications;2024-01-08

4. Methyl-coenzyme M reductase;Metalloenzymes;2024

5. Trace metals as key controlling switches regulating the efficiencies of aerobic and anaerobic bioprocesses;Biochemical Engineering Journal;2023-09