Thermodynamically Favourable States in the Reaction of Nitrogenase without Dissociation of any Sulfide Ligand-Reference-Cited by-同舟云学术

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Thermodynamically Favourable States in the Reaction of Nitrogenase without Dissociation of any Sulfide Ligand

Published:2022-02-02 Issue:14 Volume:28 Page:
ISSN:0947-6539
Container-title:Chemistry – A European Journal
language:en
Short-container-title:Chemistry A European J

Author:

Jiang Hao¹^ORCID,Ryde Ulf¹^ORCID

Affiliation:

1. Department of Theoretical Chemistry Lund University Chemical Centre, P. O. Box 124 221 00 Lund Sweden

Funder

Vetenskapsrådet

China Scholarship Council

Publisher

Wiley

Subject

General Chemistry,Catalysis,Organic Chemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/chem.202103933

Reference99 articles.

1. Mechanism of Nitrogen Fixation by Nitrogenase: The Next Stage

2. Nitrogenase Reveals Its Inner Secrets

3. Mechanism of Molybdenum Nitrogenase

4. Structural Models for the Metal Centers in the Nitrogenase Molybdenum-Iron Protein

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. The activating capture of N₂ at the active site of Mo–nitrogenase;Dalton Transactions;2024

2. Putative reaction mechanism of nitrogenase with a half-dissociated S2B ligand;Dalton Transactions;2024

3. How thermal fluctuations influence the function of the FeMo cofactor in nitrogenase enzymes;Chem Catalysis;2023-07

4. Understanding the Electronic Structure Basis for N₂ Binding to FeMoco: A Systematic Quantum Mechanics/Molecular Mechanics Investigation;Inorganic Chemistry;2023-03-29

5. The E3 state of FeMoco: one hydride, two hydrides or dihydrogen?;Physical Chemistry Chemical Physics;2023

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