ArticleScientific reports2013
A molecular pathway for the egress of ammonia produced by nitrogenase.
Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 33 citations in OpenAlex.
- Function, Structure, and Regulation of Nitrogen Fixation-like Metalloproteins for Nitrogen, Energy, Carbon, and Sulfur Metabolism.Chemical reviews · 2026Review
- A Proposed Complete-Cycle Mechanism for Conversion of NChembiochem : a European journal of chemical biology · 2026Article
- Deserts, Rivers, Pools, and Billabongs: Water Features of the Nitrogenase Proteins, and their Functions.Chembiochem : a European journal of chemical biology · 2025Review
- Structural evolution of nitrogenase states under alkaline turnover.Nature communications · 2024Article
- Structural consequences of turnover-induced homocitrate loss in nitrogenase.Nature communications · 2023Article
- Biological nitrogen fixation in theory, practice, and reality: a perspective on the molybdenum nitrogenase system.FEBS letters · 2023Review
- Small-Molecule Tunnels in Metalloenzymes Viewed as Extensions of the Active Site.Accounts of chemical research · 2021Review
- Structural Enzymology of Nitrogenase Enzymes.Chemical reviews · 2020Review
- Reversible Protonated Resting State of the Nitrogenase Active Site.Journal of the American Chemical Society · 2017Article
- PockDrug-Server: a new web server for predicting pocket druggability on holo and apo proteins.Nucleic acids research · 2015Article
- Docking and migration of carbon monoxide in nitrogenase: the case for gated pockets from infrared spectroscopy and molecular dynamics.Biochemistry · 2015Article
- Substrate tunnels in enzymes: structure-function relationships and computational methodology.Proteins · 2015Review
- Substrate pathways in the nitrogenase MoFe protein by experimental identification of small molecule binding sites.Biochemistry · 2015Article
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Authors and funding
1 author at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Nitrogenase converts N2 to NH3, at one face of an Fe-Mo-S cluster (FeMo-co) buried in the protein. Through exploration of cavities in the structures of nitrogenase proteins, a pathway for the egress of ammonia from its generation site to the external medium is proposed. This pathway is conserved in the three species Azotobacter vinelandii, Klebsiella pneumoniae and Clostridium pasteurianum. A molecular mechanism for the translocation of NH3 by skipping through a sequence of hydrogen bonds involving eleven water molecules and surrounding aminoacids has been developed. The putative mechanism requires movement aside of some water molecules by up to ~ 1Å. Consistent with this, the surrounding protein is comprised of different chains and has little secondary structure: protein fluctuations are part of the mechanism. This NH3 pathway is well separated from the water chain and embedded proton wire that have been proposed for serial supply of protons to FeMo-co. Verification procedures are suggested.
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