ArticleInorganic chemistry2016
CO2 Reduction Catalyzed by Nitrogenase: Pathways to Formate, Carbon Monoxide, and Methane.
Article in Inorganic chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 54 citations in OpenAlex.
- Function, Structure, and Regulation of Nitrogen Fixation-like Metalloproteins for Nitrogen, Energy, Carbon, and Sulfur Metabolism.Chemical reviews · 2026Review
- Selective COACS catalysis · 2026Article
- Reductant- or Light-Driven ATP-Independent Reduction of COChembiochem : a European journal of chemical biology · 2025Article
- Biomimetic [MFeInorganic chemistry · 2025Article
- The iron nitrogenase reduces carbon dioxide to formate and methane under physiological conditions: A route to feedstock chemicals.Science advances · 2024Article
- Structural insights into the iron nitrogenase complex.Nature structural & molecular biology · 2024Article
- Nitrogenase beyond the Resting State: A Structural Perspective.Molecules (Basel, Switzerland) · 2023Review
- Engineering an Oxygen-Binding Protein for Photocatalytic COAngewandte Chemie (International ed. in English) · 2023Article
- Article
- The Conversion of Carbon Monoxide and Carbon Dioxide by Nitrogenases.Chembiochem : a European journal of chemical biology · 2022Review
- A Red Fluorescent Protein Reporter System Developed for Measuring Gene Expression in Photosynthetic Bacteria under Anaerobic Conditions.Microorganisms · 2022Article
- Access to Metal Centers and Fluxional Hydride Coordination Integral for COInorganic chemistry · 2021Article
- Identification of Nitrogen Fixation Genes inMicroorganisms · 2020Article
- Large Hydrogen Isotope Fractionation Distinguishes Nitrogenase-Derived Methane from Other Methane Sources.Applied and environmental microbiology · 2020Article
- Reduction of Substrates by Nitrogenases.Chemical reviews · 2020Review
- Influence of Energy and Electron Availability onApplied and environmental microbiology · 2019Article
- Carbon Dioxide Insertion into Bridging Iron Hydrides: Kinetic and Mechanistic Studies.European journal of inorganic chemistry · 2019Article
- Critical computational analysis illuminates the reductive-elimination mechanism that activates nitrogenase for NProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Interfacing nature's catalytic machinery with synthetic materials for semi-artificial photosynthesis.Nature nanotechnology · 2018Review
- Mechanism of Nitrogenase HJournal of the American Chemical Society · 2017Article
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Authors and funding
6 authors at 5 institutions in 1 country.
Funding
Abstract
The reduction of N2 to NH3 by Mo-dependent nitrogenase at its active-site metal cluster FeMo-cofactor utilizes reductive elimination of Fe-bound hydrides with obligatory loss of H2 to activate the enzyme for binding/reduction of N2. Earlier work showed that wild-type nitrogenase and a nitrogenase with amino acid substitutions in the MoFe protein near FeMo-cofactor can catalytically reduce CO2 by two or eight electrons/protons to carbon monoxide (CO) and methane (CH4) at low rates. Here, it is demonstrated that nitrogenase preferentially reduces CO2 by two electrons/protons to formate (HCOO(-)) at rates >10 times higher than rates of CO2 reduction to CO and CH4. Quantum mechanical calculations on the doubly reduced FeMo-cofactor with a Fe-bound hydride and S-bound proton (E2(2H) state) favor a direct reaction of CO2 with the hydride ("direct hydride transfer" reaction pathway), with facile hydride transfer to CO2 yielding formate. In contrast, a significant barrier is observed for reaction of Fe-bound CO2 with the hydride ("associative" reaction pathway), which leads to CO and CH4. Remarkably, in the direct hydride transfer pathway, the Fe-H behaves as a hydridic hydrogen, whereas in the associative pathway it acts as a protic hydrogen. MoFe proteins with amino acid substitutions near FeMo-cofactor (α-70(Val→Ala), α-195(His→Gln)) are found to significantly alter the distribution of products between formate and CO/CH4.
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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.