ArticleInorganic chemistry2020
Quantum Mechanics/Molecular Mechanics Study of Resting-State Vanadium Nitrogenase: Molecular and Electronic Structure of the Iron-Vanadium Cofactor.
Article in Inorganic chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 32 citations in OpenAlex.
- Periodic Trends in M-Fe Interactions across an Isostructural and Isoelectronic Series of [MFeJournal of the American Chemical Society · 2025Article
- Biomimetic [MFeInorganic chemistry · 2025Article
- Article
- Accelerating reliable multiscale quantum refinement of protein-drug systems enabled by machine learning.Nature communications · 2024Article
- On the Shoulders of Giants-Reaching for Nitrogenase.Molecules (Basel, Switzerland) · 2023Review
- Computational Study on the Influence of Mo/V Centers on the Electronic Structure and Hydrazine Reduction Capability of [MFeInorganic chemistry · 2023Article
- Computational Description of Alkylated Iron-Sulfur Organometallic Clusters.Journal of the American Chemical Society · 2023Article
- Understanding the Electronic Structure Basis for NInorganic chemistry · 2023Article
- Facile and dynamic cleavage of every iron-sulfide bond in cuboidal iron-sulfur clusters.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- An FeAngewandte Chemie (International ed. in English) · 2022Article
- Analysis of the Geometric and Electronic Structure of Spin-Coupled Iron-Sulfur Dimers with Broken-Symmetry DFT: Implications for FeMoco.Journal of chemical theory and computation · 2022Article
- Carbon Monoxide Binding to the Iron-Molybdenum Cofactor of Nitrogenase: a Detailed Quantum Mechanics/Molecular Mechanics Investigation.Inorganic chemistry · 2021Article
- The electronic structure of FeV-cofactor in vanadium-dependent nitrogenase.Chemical science · 2021Article
- The influences of carbon donor ligands on biomimetic multi-iron complexes for NChemical science · 2020Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nitrogenase enzymes are responsible for all biological nitrogen reduction. How this is accomplished at the atomic level, however, has still not been established. The molybdenum-dependent nitrogenase has been extensively studied and is the most active catalyst for dinitrogen reduction of the nitrogenase enzymes. The vanadium-dependent form, on the other hand, displays different reactivity, being capable of CO and CO
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