Resolving the structure of the E1state of Mo nitrogenase through Mo and Fe K-edge EXAFS and QM/MM calculations-Reference-Cited by-同舟云学术

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Resolving the structure of the E1state of Mo nitrogenase through Mo and Fe K-edge EXAFS and QM/MM calculations

Published:2019 Issue:42 Volume:10 Page:9807-9821
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Van Stappen Casey¹²³^ORCID,Thorhallsson Albert Thor¹²³,Decamps Laure¹²³^ORCID,Bjornsson Ragnar¹²³^ORCID,DeBeer Serena¹²³^ORCID

Affiliation:

1. Max-Planck Institute for Chemical Energy Conversion

2. 45470 Mülheim an der Ruhr

3. Germany

Abstract

The FeMoco cluster of Mo nitrogenase undergoes minor distortions upon reduction to E₁, supporting iron-based reduction and belt sulfide protonation.

Funder

FP7 Ideas: European Research Council

Deutsche Forschungsgemeinschaft

Max-Planck-Gesellschaft

Icelandic Centre for Research

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2019/SC/C9SC02187F

Reference85 articles.

1. Mechanism of Molybdenum Nitrogenase

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

3. Electron Transfer within Nitrogenase: Evidence for a Deficit-Spending Mechanism

4. Conformational Gating of Electron Transfer from the Nitrogenase Fe Protein to MoFe Protein

5. Evidence That the Pi Release Event Is the Rate-Limiting Step in the Nitrogenase Catalytic Cycle

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1. Sulfide release and rebinding in the mechanism for nitrogenase;Journal of Computational Chemistry;2024-08-27

2. H₂ formation from the E₂–E₄ states of nitrogenase;Physical Chemistry Chemical Physics;2024

3. The energetics of N₂ reduction by vanadium containing nitrogenase;Physical Chemistry Chemical Physics;2024

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

5. On the Shoulders of Giants—Reaching for Nitrogenase;Molecules;2023-12-05

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