ArticleNature communications2016
Nitrogenase FeMoco investigated by spatially resolved anomalous dispersion refinement.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed.
- Classical quantum chemical solution of the FeMo-cofactor model to chemical accuracy and its implications.Science advances · 2026Article
- Function, Structure, and Regulation of Nitrogen Fixation-like Metalloproteins for Nitrogen, Energy, Carbon, and Sulfur Metabolism.Chemical reviews · 2026Review
- Unravelling Catalytic Divergence in Mo- and Fe-Only Nitrogenases: The Role of the Heterometal-Site and Protein Environment from QM/MM Insights.Journal of the American Chemical Society · 2025Article
- Synthetic models of the nitrogenase FeMo cofactor.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Occupancy Determination from Resonant X-ray Diffraction.Inorganic chemistry · 2025Article
- Electronic Desymmetrization of CuInorganic chemistry · 2024Article
- Utilizing anomalous signals for element identification in macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2024Article
- Improvement of Single-Crystal Structures of Very Heavy Element Compounds by Refining Anomalous Dispersion Parameters.Inorganic chemistry · 2024Article
- Analysis of early intermediate states of the nitrogenase reaction by regularization of EPR spectra.Nature communications · 2024Article
- A database overview of metal-coordination distances in metalloproteins.Acta crystallographica. Section D, Structural biology · 2024Article
- Molybdenum and vanadium homocitrates and their homologs - towards the local environments and protonations of FeMo/V-cofactors in nitrogenases.Coordination chemistry reviews · 2024Article
- Highly Activated Terminal Carbon Monoxide Ligand in an Iron-Sulfur Cluster Model of FeMco with Intermediate Local Spin State at Fe.Journal of the American Chemical Society · 2024Article
- Uncovering a CFAngewandte Chemie (International ed. in English) · 2023Article
- On the Shoulders of Giants-Reaching for Nitrogenase.Molecules (Basel, Switzerland) · 2023Review
- Metal Site-Specific Electrostatic Field Effects on a Tricopper(I) Cluster Probed by Resonant Diffraction Anomalous Fine Structure (DAFS).Inorganic chemistry · 2023Article
- Facing the phase problem.IUCrJ · 2023Article
- Connecting the geometric and electronic structures of the nitrogenase iron-molybdenum cofactor through site-selectiveNature chemistry · 2023Article
- Understanding the Electronic Structure Basis for NInorganic chemistry · 2023Article
- Near ambient NNature reviews. Chemistry · 2023Review
- The HD Reaction of Nitrogenase: a Detailed Mechanism.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
10 more citing papers are in PubMed but not listed here.
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8 authors.
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Abstract
The [Mo:7Fe:9S:C] iron-molybdenum cofactor (FeMoco) of nitrogenase is the largest known metal cluster and catalyses the 6-electron reduction of dinitrogen to ammonium in biological nitrogen fixation. Only recently its atomic structure was clarified, while its reactivity and electronic structure remain under debate. Here we show that for its resting S=3/2 state the common iron oxidation state assignments must be reconsidered. By a spatially resolved refinement of the anomalous scattering contributions of the 7 Fe atoms of FeMoco, we conclude that three irons (Fe1/3/7) are more reduced than the other four (Fe2/4/5/6). Our data are in agreement with the recently revised oxidation state assignment for the molybdenum ion, providing the first spatially resolved picture of the resting-state electron distribution within FeMoco. This might provide the long-sought experimental basis for a generally accepted theoretical description of the cluster that is in line with available spectroscopic and functional data.
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