ArticleJournal of the American Chemical Society2015
Identification of a key catalytic intermediate demonstrates that nitrogenase is activated by the reversible exchange of N₂ for H₂.
Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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35 citing papers in PubMed, 105 citations in OpenAlex.
- A Proposed Complete-Cycle Mechanism for Conversion of NChembiochem : a European journal of chemical biology · 2026Article
- Mechanistic Insights into Dinitrogen Reduction to Ammonia in Light-Controlled Nanocrystal:Nitrogenase Complexes.Accounts of chemical research · 2026Review
- Final EThe journal of physical chemistry. B · 2024Article
- Computational Model Study of the Experimentally Suggested Mechanism for Nitrogenase.The journal of physical chemistry. B · 2024Article
- Nitrogenase beyond the Resting State: A Structural Perspective.Molecules (Basel, Switzerland) · 2023Review
- Cryo-annealing of Photoreduced CdS Quantum Dot-Nitrogenase MoFe Protein Complexes Reveals the Kinetic Stability of the EJournal of the American Chemical Society · 2023Article
- Understanding the Electronic Structure Basis for NInorganic chemistry · 2023Article
- Biological nitrogen fixation in theory, practice, and reality: a perspective on the molybdenum nitrogenase system.FEBS letters · 2023Review
- A Mechanism for Nitrogenase Including Loss of a Sulfide.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Comparing Molecular Mechanisms in Solar NHInternational journal of molecular sciences · 2020Review
- Reduction of Substrates by Nitrogenases.Chemical reviews · 2020Review
- Structural Enzymology of Nitrogenase Enzymes.Chemical reviews · 2020Review
- The Spectroscopy of Nitrogenases.Chemical reviews · 2020Review
- Carbon substrate re-orders relative growth of a bacterium using Mo-, V-, or Fe-nitrogenase for nitrogen fixation.Environmental microbiology · 2020Article
- A model for dinitrogen binding in the EChemical science · 2019Article
- Light Enhanced Fe-Mediated Nitrogen Fixation: Mechanistic Insights Regarding HACS catalysis · 2019Article
- Dinitrogen Activation and Functionalization using β-Diketiminate Iron Complexes.European journal of inorganic chemistry · 2019Article
- Control of electron transfer in nitrogenase.Current opinion in chemical biology · 2018Review
- Kinetic Understanding of NBiochemistry · 2018Article
- ENDOR Characterization of (NInorganic chemistry · 2018Article
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6 authors at 3 institutions in 1 country.
Funding
Abstract
Freeze-quenching nitrogenase during turnover with N2 traps an S = ½ intermediate that was shown by ENDOR and EPR spectroscopy to contain N2 or a reduction product bound to the active-site molybdenum-iron cofactor (FeMo-co). To identify this intermediate (termed here EG), we turned to a quench-cryoannealing relaxation protocol. The trapped state is allowed to relax to the resting E0 state in frozen medium at a temperature below the melting temperature; relaxation is monitored by periodically cooling the sample to cryogenic temperature for EPR analysis. During -50 °C cryoannealing of EG prepared under turnover conditions in which the concentrations of N2 and H2 ([H2], [N2]) are systematically and independently varied, the rate of decay of EG is accelerated by increasing [H2] and slowed by increasing [N2] in the frozen reaction mixture; correspondingly, the accumulation of EG is greater with low [H2] and/or high [N2]. The influence of these diatomics identifies EG as the key catalytic intermediate formed by reductive elimination of H2 with concomitant N2 binding, a state in which FeMo-co binds the components of diazene (an N-N moiety, perhaps N2 and two [e(-)/H(+)] or diazene itself). This identification combines with an earlier study to demonstrate that nitrogenase is activated for N2 binding and reduction through the thermodynamically and kinetically reversible reductive-elimination/oxidative-addition exchange of N2 and H2, with an implied limiting stoichiometry of eight electrons/protons for the reduction of N2 to two NH3.
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