ArticleJournal of chemical information and modeling2023
Anion Pathways in the NarK Nitrate/Nitrite Exchanger.
Article in Journal of chemical information and modeling, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 9 citations in OpenAlex.
- Protonation States of Proton-Sensing Glutamate Residues in Transporter Sialin.International journal of molecular sciences · 2026Article
- Characterization of a thermotolerant strain inhibiting tobacco-specific nitrosamines in cigar fermentation.World journal of microbiology & biotechnology · 2026Article
- Comparative genomic analysis of hydrogen peroxide and nitric oxide metabolic pathways in Limosilactobacillus fermentum.Scientific reports · 2025Article
- How minor sequence changes enable mechanistic diversity in MFS transporters? An atomic-level rationale for symport emergence in NarU.bioRxiv : the preprint server for biology · 2025Article
- Article
- Investigation on the aerobic methanotrophic community and the dominant taxon Methylomarinum in seagrass ecosystem.Environmental microbiome · 2025Article
- Substrate binding plasticity revealed by Cryo-EM structures of SLC26A2.Nature communications · 2024Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
NarK nitrate/nitrite antiporter imports nitrate (a mineral form of the essential element nitrogen) into the cell and exports nitrite (a metabolite that can be toxic in high concentrations) out of the cell. However, many details about its operational mechanism remain poorly understood. In this work, we performed steered molecular dynamics simulations of anion translocations and quantum-chemistry model calculations of the binding sites to study the wild-type NarK protein and its R89K mutant. Our results shed light on the importance of the two strictly conserved binding-site arginine residues (R89 and R305) and two glycine-rich signature motifs (G164-M176 and G408-F419) in anion movement through the pore. We also observe conformational changes of the protein during anion migration. For the R89K mutant, our quantum calculations reveal a competition for a proton between the anion (especially nitrite) and lysine, which can potentially slow down or even trap the anion in the pore. Our findings provide a possible explanation for the striking experimental finding that the arginine-to-lysine mutation, despite preserving the charge, impedes or abolishes anion transport in such mutants of NarK and other similar nitrate/nitrite exchangers.
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Registered trials
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