ReviewJournal of the American Chemical Society2016
Insight into the Iron-Molybdenum Cofactor of Nitrogenase from Synthetic Iron Complexes with Sulfur, Carbon, and Hydride Ligands.
Review in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 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
45 citing papers in PubMed, 174 citations in OpenAlex.
- Enhancing Plant Growth and Yield Quality Through Molybdenum Application: Trends, Future and Directions.Plants (Basel, Switzerland) · 2026Review
- Single-Step Insertion of Organic Sulfur Into a FeAngewandte Chemie (International ed. in English) · 2025Article
- What you C is what you get.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Synthetic models of the nitrogenase FeMo cofactor.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Substrate-Dependent Hydridic and Radical Reactivity of Triiron Hydride Clusters.Inorganic chemistry · 2025Article
- Water-catalyzed iron-molybdenum carbyne formation in bimetallic acetylene transformation.Nature communications · 2024Article
- PuClChemical science · 2024Article
- Mössbauer and Nuclear Resonance Vibrational Spectroscopy Studies of Iron Species Involved in N-N Bond Cleavage.Inorganic chemistry · 2023Article
- Bioinspired Framework Catalysts: From Enzyme Immobilization to Biomimetic Catalysis.Chemical reviews · 2023Review
- Sulfur-Ligated [2Fe-2C] Clusters as Synthetic Model Systems for Nitrogenase.Inorganic chemistry · 2023Article
- Terminal NChemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
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- Statistical analysis of PRSC advances · 2022Article
- Bonding and stability of dinitrogen-bonded donor base-stabilized Si(0)/Ge(0) species [(cAACRSC advances · 2022Article
- Iron Complexes of a Proton-Responsive SCS Pincer Ligand with a Sensitive Electronic Structure.Inorganic chemistry · 2022Article
- Estimations of FeRSC advances · 2022Article
- Estimations of Fe-NACS omega · 2021Article
- EDA-NOCV Calculation for Efficient NACS omega · 2021Article
- Partial synthetic models of FeMoco with sulfide and carbyne ligands: Effect of interstitial atom in nitrogenase active site.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Heterojunction-based photocatalytic nitrogen fixation: principles and current progress.Nanoscale advances · 2021Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Nitrogenase enzymes are used by microorganisms for converting atmospheric N2 to ammonia, which provides an essential source of N atoms for higher organisms. The active site of the molybdenum-dependent nitrogenase is the unique carbide-containing iron-sulfur cluster called the iron-molybdenum cofactor (FeMoco). On the FeMoco, N2 binding is suggested to occur at one or more iron atoms, but the structures of the catalytic intermediates are not clear. In order to establish the feasibility of different potential mechanistic steps during biological N2 reduction, chemists have prepared iron complexes that mimic various structural aspects of the iron sites in the FeMoco. This reductionist approach gives mechanistic insight, and also uncovers fundamental principles that could be used more broadly for small-molecule activation. Here, we discuss recent results and highlight directions for future research. In one direction, synthetic iron complexes have now been shown to bind N2, break the N-N triple bond, and produce ammonia catalytically. Carbon- and sulfur-based donors have been incorporated into the ligand spheres of Fe-N2 complexes to show how these atoms may influence the structure and reactivity of the FeMoco. Hydrides have been incorporated into synthetic systems, which can bind N2, reduce some nitrogenase substrates, and/or reductively eliminate H2 to generate reduced iron centers. Though some carbide-containing iron clusters are known, none yet have sulfide bridges or high-spin iron atoms like the FeMoco.
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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.