ArticleBiophysical journal2013
Exploring the pH-dependent substrate transport mechanism of FocA using molecular dynamics simulation.
Article in Biophysical journal, 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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Who cites it
13 citing papers in PubMed, 29 citations in OpenAlex.
- Molecular Dynamics Simulations and Their Novel Applications in Drug Delivery for Cancer Treatment: A Review.Annals of biomedical engineering · 2025Review
- Hydrogen production in the presence of oxygen byMicrobiology (Reading, England) · 2022Article
- A single amino acid exchange converts FocA into a unidirectional efflux channel for formate.Microbiology (Reading, England) · 2022Article
- Article
- Bioactivity of melianone against3 Biotech · 2020Article
- Transmembrane Facilitation of Lactate/HMembranes · 2020Article
- Is the E. coli Homolog of the Formate/Nitrite Transporter Family an Anion Channel? A Computational Study.Biophysical journal · 2020Article
- Formate-nitrite transporters carrying nonprotonatable amide amino acids instead of a central histidine maintain pH-dependent transport.The Journal of biological chemistry · 2019Article
- Efficient Hydrogen-Dependent Carbon Dioxide Reduction by Escherichia coli.Current biology : CB · 2018Article
- Energetics and mechanism of anion permeation across formate-nitrite transporters.Scientific reports · 2017Article
- Anion-selective Formate/nitrite transporters: taxonomic distribution, phylogenetic analysis and subfamily-specific conservation pattern in prokaryotes.BMC genomics · 2017Article
- Mechanism of formate-nitrite transporters by dielectric shift of substrate acidity.The EMBO journal · 2017Article
- Pyruvate formate-lyase interacts directly with the formate channel FocA to regulate formate translocation.Journal of molecular biology · 2014Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
FocA belongs to the formate-nitrate transporter family and plays an essential role in the export and uptake of formate in organisms. According to the available crystal structures, the N-terminal residues of FocA are structurally featureless at physiological conditions but at reduced pH form helices to harbor the cytoplasmic entrance of the substrate permeation pathway, which apparently explains the cessation of electrical signal observed in electrophysiological experiments. In this work, we found by structural analysis and molecular dynamics simulations that those N-terminal helices cannot effectively preclude the substrate permeation. Equilibrium simulations and thermodynamic calculations suggest that FocA is permeable to both formate and formic acid, the latter of which is transparent to electrophysiological studies as an electrically neutral species. Hence, the cease of electrical current at acidic pH may be caused by the change of the transported substrate from formate to formic acid. In addition, the mechanism of formate export at physiological pH is discussed.
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