ArticleScience (New York, N.Y.)2022
Structures of the nitrogenase complex prepared under catalytic turnover conditions.
Article in Science (New York, N.Y.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 84 citations in OpenAlex.
- Article
- Structural Characterization of Four Redox States of the P-cluster in Molybdenum Nitrogenase via Electrochemical Control of Crystals.Journal of the American Chemical Society · 2026Article
- Molecular basis of NNature communications · 2026Article
- Function, Structure, and Regulation of Nitrogen Fixation-like Metalloproteins for Nitrogen, Energy, Carbon, and Sulfur Metabolism.Chemical reviews · 2026Review
- Minimal ATP-Independent NAngewandte Chemie (International ed. in English) · 2026Article
- Mechanistic Insights into Dinitrogen Reduction to Ammonia in Light-Controlled Nanocrystal:Nitrogenase Complexes.Accounts of chemical research · 2026Review
- Trafficking of a nitrogenase FeMo-cofactor assembly intermediate.Nature chemical biology · 2026Article
- A Surfactant Cocktail Overcomes Air-Water Interface Artifacts in Single-Particle CryoEM.bioRxiv : the preprint server for biology · 2026Article
- Structural insights into metallocluster trafficking in the nitrogenase assembly scaffold NifEN.Nature catalysis · 2026Article
- Design of a protein scaffold with a selective, Bi-containing heterodinuclear metal coordination motif.Journal of inorganic biochemistry · 2026Article
- Deserts, Rivers, Pools, and Billabongs: Water Features of the Nitrogenase Proteins, and their Functions.Chembiochem : a European journal of chemical biology · 2025Review
- ANTIDOTE: A Metadata-Driven Neural Network for Improving CryoEM 3-D Particle Sorting.bioRxiv : the preprint server for biology · 2025Article
- Enzyme-Substrate Complex Formation and Electron Transfer in Nitrogenase-Like Dark-Operative Protochlorophyllide Oxidoreductase (DPOR).ChemistryOpen · 2025Article
- Reductant- or Light-Driven ATP-Independent Reduction of COChembiochem : a European journal of chemical biology · 2025Article
- Article
- Belt-Sulfur Mobilization as a Crucial Mechanistic Feature Shared between the Vanadium and Molybdenum Nitrogenases.Chem catalysis · 2025Article
- Article
- Heterologous synthesis of a simplified nitrogenase analog inScience advances · 2025Article
- Cryo-EM captures the coordination of asymmetric electron transfer through a di-copper site in DPOR.Nature communications · 2025Article
- Preparation of oxygen-sensitive proteins for high-resolution cryoEM structure determination using blot-free vitrification.Nature communications · 2025Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The enzyme nitrogenase couples adenosine triphosphate (ATP) hydrolysis to the multielectron reduction of atmospheric dinitrogen into ammonia. Despite extensive research, the mechanistic details of ATP-dependent energy transduction and dinitrogen reduction by nitrogenase are not well understood, requiring new strategies to monitor its structural dynamics during catalytic action. Here, we report cryo-electron microscopy structures of the nitrogenase complex prepared under enzymatic turnover conditions. We observe that asymmetry governs all aspects of the nitrogenase mechanism, including ATP hydrolysis, protein-protein interactions, and catalysis. Conformational changes near the catalytic iron-molybdenum cofactor are correlated with the nucleotide-hydrolysis state of the enzyme.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.