ArticleeLife2015
Catalysis-dependent selenium incorporation and migration in the nitrogenase active site iron-molybdenum cofactor.
Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
73 citing papers in PubMed, 155 citations in OpenAlex.
- 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
- Molybdenum doping enhances backbonding at neighboring iron centers in iron-sulfur clusters.Chem · 2026Article
- A Proposed Complete-Cycle Mechanism for Conversion of NChembiochem : a European journal of chemical biology · 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
- EPR andInorganic chemistry · 2025Article
- Article
- Belt-Sulfur Mobilization as a Crucial Mechanistic Feature Shared between the Vanadium and Molybdenum Nitrogenases.Chem catalysis · 2025Article
- The nitrogenase mechanism: new roles for the dangler?Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Review
- Methylthio-alkane reductases use nitrogenase metalloclusters for carbon-sulfur bond cleavage.Nature catalysis · 2025Article
- Structural evolution of nitrogenase states under alkaline turnover.Nature communications · 2024Article
- Anaerobic cryoEM protocols for air-sensitive nitrogenase proteins.Nature protocols · 2024Review
- ATP-Independent Turnover of Dinitrogen Intermediates Captured on the Nitrogenase Cofactor.Angewandte Chemie (International ed. in English) · 2024Article
- 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
- An Iron-Sulfur Cluster with a Highly Pyramidalized Three-Coordinate Iron Center and a Negligible Affinity for Dinitrogen.Journal of the American Chemical Society · 2023Article
- Enzymatic Fischer-Tropsch-Type Reactions.Chemical reviews · 2023Review
- Connecting the geometric and electronic structures of the nitrogenase iron-molybdenum cofactor through site-selectiveNature chemistry · 2023Article
- Structural consequences of turnover-induced homocitrate loss in nitrogenase.Nature communications · 2023Article
13 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Dinitrogen reduction in the biological nitrogen cycle is catalyzed by nitrogenase, a two-component metalloenzyme. Understanding of the transformation of the inert resting state of the active site FeMo-cofactor into an activated state capable of reducing dinitrogen remains elusive. Here we report the catalysis dependent, site-selective incorporation of selenium into the FeMo-cofactor from selenocyanate as a newly identified substrate and inhibitor. The 1.60 Å resolution structure reveals selenium occupying the S2B site of FeMo-cofactor in the Azotobacter vinelandii MoFe-protein, a position that was recently identified as the CO-binding site. The Se2B-labeled enzyme retains substrate reduction activity and marks the starting point for a crystallographic pulse-chase experiment of the active site during turnover. Through a series of crystal structures obtained at resolutions of 1.32-1.66 Å, including the CO-inhibited form of Av1-Se2B, the exchangeability of all three belt-sulfur sites is demonstrated, providing direct insights into unforeseen rearrangements of the metal center during catalysis.
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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.