ReviewJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2014
Nitrogenase FeMo cofactor: an atomic structure in three simple steps.
Review in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 74 citations in OpenAlex.
- Recent Advances and Perspectives of Metal Clusters for Electrochemical Nitrogen Reduction.ChemPlusChem · 2026Review
- Iron-molybdenum cofactor synthesis by a thermophilic nitrogenase devoid of the scaffold NifEN.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Scalar Relativistic All-Electron and PseudopotentialThe journal of physical chemistry. A · 2024Article
- Protonation of Homocitrate and the EInorganic chemistry · 2023Article
- Two local minima for structures of [4Fe-4S] clusters obtained with density functional theory methods.Scientific reports · 2023Article
- Quantum Mechanical Calculations of Redox Potentials of the Metal Clusters in Nitrogenase.Molecules (Basel, Switzerland) · 2022Article
- QM/MM Study of Partial Dissociation of S2B for the EInorganic chemistry · 2022Article
- Proton Transfer Pathways in Nitrogenase with and without Dissociated S2B.Angewandte Chemie (International ed. in English) · 2022Article
- Benchmark Study of Redox Potential Calculations for Iron-Sulfur Clusters in Proteins.Inorganic chemistry · 2022Article
- Thermodynamically Favourable States in the Reaction of Nitrogenase without Dissociation of any Sulfide Ligand.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Biophysical Characterization of Iron-Sulfur Proteins.Bio-protocol · 2021Article
- Two ligand-binding sites in CO-reducing V nitrogenase reveal a general mechanistic principle.Science advances · 2021Article
- Plant expression of NifD protein variants resistant to mitochondrial degradation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Does the crystal structure of vanadium nitrogenase contain a reaction intermediate? Evidence from quantum refinement.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Article
- Structural Enzymology of Nitrogenase Enzymes.Chemical reviews · 2020Review
- NJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Article
- What Is the Structure of the EJournal of chemical theory and computation · 2020Article
- Crystal structure of VnfH, the iron protein component of vanadium nitrogenase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Another twist on nitrogenases.Nature microbiology · 2018Article
- The structure of vanadium nitrogenase reveals an unusual bridging ligand.Nature chemical biology · 2017Article
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Abstract
The enzyme nitrogenase catalyzes the six-electron reduction of molecular dinitrogen to ammonium, concomitant with the reduction of protons to yield hydrogen gas. In the MoFe protein component of the nitrogenase system, the unique FeMo cofactor is the active site of catalysis, but its exact mechanism remains under debate. This review focuses on the history of the structure determination of FeMo cofactor, a process that extended over two decades and involved several iterations and corrections that are unusual and unexpected within the established field of X-ray crystallography. However, FeMo cofactor has defied expectations on several occasions, and besides being the largest single iron-sulfur cluster known to bioinorganic chemistry, this [Mo:7Fe:9S:C]:homocitrate moiety is unique in some aspects that have misled researchers several times. We have now arrived at a final and complete description of the atomic structure of FeMo cofactor, and yet many questions regarding various aspects of the catalytic mechanism of this enzyme remain to be answered.
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