The One-Electron Reduced Active-Site FeFe-Cofactor of Fe-Nitrogenase Contains a Hydride Bound to a Formally Oxidized Metal-Ion Core-Reference-Cited by-同舟云学术

The One-Electron Reduced Active-Site FeFe-Cofactor of Fe-Nitrogenase Contains a Hydride Bound to a Formally Oxidized Metal-Ion Core

Published:2022-03-31 Issue:14 Volume:61 Page:5459-5464
ISSN:0020-1669
Container-title:Inorganic Chemistry
language:en
Short-container-title:Inorg. Chem.

Author:

Lukoyanov Dmitriy A.¹^ORCID,Harris Derek F.²^ORCID,Yang Zhi-Yong²^ORCID,Pérez-González Ana³^ORCID,Dean Dennis R.³^ORCID,Seefeldt Lance C.²^ORCID,Hoffman Brian M.¹^ORCID

Affiliation:

1. Department of Chemistry, Northwestern University, Evanston, Illinois 60208, United States

2. Department of Chemistry and Biochemistry, Utah State University, Logan, Utah 84322, United States

3. Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg, Virginia 24061, United States

Funder

Division of Molecular and Cellular Biosciences

Basic Energy Sciences

Publisher

American Chemical Society (ACS)

Subject

Inorganic Chemistry,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.inorgchem.2c00180

Reference32 articles.

1. Mechanism of Molybdenum Nitrogenase

2. Mechanism of Mo-Dependent Nitrogenase

3. Reduction of Substrates by Nitrogenases

4. Mo-, V-, and Fe-Nitrogenases Use a Universal Eight-Electron Reductive-Elimination Mechanism To Achieve N2 Reduction

5. Kinetic Understanding of N2 Reduction versus H2 Evolution at the E4(4H) Janus State in the Three Nitrogenases

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

5. Protonation of Homocitrate and the E₁ State of Fe-Nitrogenase Studied by QM/MM Calculations;Inorganic Chemistry;2023-11-21