ArticleRSC chemical biology2021
Environment and coordination of FeMo-co in the nitrogenase metallochaperone NafY.
Article in RSC chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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Who cites it
4 citing papers in PubMed.
- Dynamics driving the precursor in NifEN scaffold during nitrogenase FeMo-cofactor assembly.Nature chemical biology · 2026Article
- Understanding the P-Cluster of Vanadium Nitrogenase: an EPR and XAS Study of the Holo vs. Apo Forms of the Enzyme.Chembiochem : a European journal of chemical biology · 2025Article
- Molecular sorting of nitrogenase catalytic cofactors.bioRxiv : the preprint server for biology · 2025Article
- The role of nucleoside triphosphate hydrolase metallochaperones in making metalloenzymes.Metallomics : integrated biometal science · 2022Review
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In nitrogenase biosynthesis, the iron-molybdenum cofactor (FeMo-co) is externally assembled at scaffold proteins and delivered to the NifDK nitrogenase component by the NafY metallochaperone. Here we have used nuclear magnetic resonance, molecular dynamics, and functional analysis to elucidate the environment and coordination of FeMo-co in NafY. H
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Registered trials
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