ArticleJournal of the American Chemical Society2019
Localized Electronic Structure of Nitrogenase FeMoco Revealed by Selenium K-Edge High Resolution X-ray Absorption Spectroscopy.
Article in Journal of the American Chemical Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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Who cites it
35 citing papers in PubMed, 76 citations in OpenAlex.
- Biosynthesis of the Selenium-Substituted [FeFe]-Hydrogenases.Journal of the American Chemical Society · 2026Article
- High energy resolution fluorescence detected X-ray absorption spectroscopy (HERFD-XAS) for studies of metals and metalloids in biology: current innovations and future perspectives.Metallomics : integrated biometal science · 2025Review
- Charge redistribution dynamics in chalcogenide-stabilized cuprous electrocatalysts unleash ampere-scale partial current toward formate production.Nature communications · 2025Article
- General Spin Restricted Open-Shell Configuration Interaction Singles (GS-ROCIS): Implementation of Spin-Orbit Coupling and Zeeman Operators for Calculation of Optical and X-ray Absorption and Magnetic Circular Dichroism Spectra of Magnetically Coupled Transition Metal Systems.The journal of physical chemistry. A · 2025Article
- Article
- Molybdenum-Iron-Sulfur Cluster with a Bridging Carbide Ligand as a Partial FeMoco Model: CO Activation, EPR Studies, and Bonding Insight.Journal of the American Chemical Society · 2025Article
- Superstoichiometric reversible and manipulable copper-ion intercalation in niobium selenide.Nature communications · 2025Article
- Investigating the Molybdenum Nitrogenase Mechanistic Cycle Using Spectroelectrochemistry.Journal of the American Chemical Society · 2025Article
- General Spin-Restricted Open-Shell Configuration Interaction Approach: Application to Metal K-Edge X-ray Absorption Spectra of Ferro- and Antiferromagnetically Coupled Dimers.The journal of physical chemistry. A · 2025Article
- Experimentally Assessing the Electronic Structure and Spin-State Energetics in MnFe Dimers Using 1s3p Resonant Inelastic X-ray Scattering.Inorganic chemistry · 2024Article
- Anaerobic cryoEM protocols for air-sensitive nitrogenase proteins.Nature protocols · 2024Review
- Analysis of early intermediate states of the nitrogenase reaction by regularization of EPR spectra.Nature communications · 2024Article
- Nitrogenase beyond the Resting State: A Structural Perspective.Molecules (Basel, Switzerland) · 2023Review
- Fe protein docking transduces conformational changes to MoFe nitrogenase active site in a nucleotide-dependent manner.Communications chemistry · 2023Article
- Peptide Selenocysteine Substitutions Reveal Direct Substrate-Enzyme Interactions at Auxiliary Clusters in RadicalJournal of the American Chemical Society · 2023Article
- Active States During the Reduction of COThe journal of physical chemistry letters · 2023Article
- Biological nitrogen fixation in theory, practice, and reality: a perspective on the molybdenum nitrogenase system.FEBS letters · 2023Review
- Article
- 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
- Selenium Valence-to-Core X-ray Emission Spectroscopy and Kβ HERFD X-ray Absorption Spectroscopy as Complementary Probes of Chemical and Electronic Structure.Inorganic chemistry · 2022Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
The size and complexity of Mo-dependent nitrogenase, a multicomponent enzyme capable of reducing dinitrogen to ammonia, have made a detailed understanding of the FeMo cofactor (FeMoco) active site electronic structure an ongoing challenge. Selective substitution of sulfur by selenium in FeMoco affords a unique probe wherein local Fe-Se interactions can be directly interrogated via high-energy resolution fluorescence detected X-ray absorption spectroscopic (HERFD XAS) and extended X-ray absorption fine structure (EXAFS) studies. These studies reveal a significant asymmetry in the electronic distribution of the FeMoco, suggesting a more localized electronic structure picture than is typically assumed for iron-sulfur clusters. Supported by experimental small molecule model data in combination with time dependent density functional theory (TDDFT) calculations, the HERFD XAS data is consistent with an assignment of Fe2/Fe6 as an antiferromagnetically coupled diferric pair. HERFD XAS and EXAFS have also been applied to Se-substituted CO-inhibited MoFe protein, demonstrating the ability of these methods to reveal electronic and structural changes that occur upon substrate binding. These results emphasize the utility of Se HERFD XAS and EXAFS for selectively probing the local electronic and geometric structure of FeMoco.
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