ArticleProceedings of the National Academy of Sciences of the United States of America2012
Structural and functional characterization of the nitrite channel NirC from Salmonella typhimurium.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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32 citing papers in PubMed, 66 citations in OpenAlex.
- Kinetic plasticity of nitrite-oxidizing bacteria containing cytoplasmic nitrite oxidoreductase.The ISME journal · 2026Article
- Intrinsic Asymmetry in Weak Acid Transmembrane Transporters.Biomolecules · 2026Review
- Structure of Chlamydomonas reinhardtii LciA guided the engineering of FNT family proteins to gain bicarbonate transport activity.Nature plants · 2026Article
- Conserved hydrophilic checkpoints tune FocA-mediated formate:HNature communications · 2025Article
- How FocA facilitates fermentation and respiration of formate byJournal of bacteriology · 2025Review
- Function Investigations and Applications of Membrane Proteins on Artificial Lipid Membranes.International journal of molecular sciences · 2023Review
- Comparison of ion selectivities of nitrite channel NirC and water channel aquaporin.World journal of microbiology & biotechnology · 2023Article
- Distinguishing functional from structural roles of conserved pore residues during formate translocation by the FocA anion channel.MicrobiologyOpen · 2022Article
- A single amino acid exchange converts FocA into a unidirectional efflux channel for formate.Microbiology (Reading, England) · 2022Article
- Unchanged nitrate and nitrite isotope fractionation during heterotrophic and Fe(II)-mixotrophic denitrification suggest a non-enzymatic link between denitrification and Fe(II) oxidation.Frontiers in microbiology · 2022Article
- Article
- Structural basis of transport and inhibition of the Plasmodium falciparum transporter PfFNT.EMBO reports · 2021Article
- 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
- 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
- The Paracoccus denitrificans NarK-like nitrate and nitrite transporters-probing nitrate uptake and nitrate/nitrite exchange mechanisms.Molecular microbiology · 2017Article
- The C-terminal Six Amino Acids of the FNT Channel FocA Are Required for Formate Translocation But Not Homopentamer Integrity.Frontiers in microbiology · 2017Article
- Article
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6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nitrite (NO(2)(-)) is a central intermediate in the nitrogen metabolism of microorganisms and plants, and is used as a cytotoxin by macrophages as part of the innate immune response. The bacterial membrane protein NirC acts as a specific channel to facilitate the transport of nitrite anions across lipid bilayers for cytoplasmic detoxification. Despite NirC's importance in nitrogen metabolism and in the pathogenicity of enteric bacteria, available biochemical data are scarce. Here we present a functional and structural characterization of NirC from Salmonella typhimurium by lipid bilayer electrophysiology and X-ray crystallography. NirC is a pentameric member of the formate/nitrite transporter family of membrane proteins that operates as a channel with high conductance. Single-channel measurements reveal fast and slow gating events but, in contrast to the related FocA formate channel, no pH-dependent gating. A 2.4Å crystal structure of NirC at pH 5 shows similarity to FocA and aquaporins, but lacks the structural asymmetry observed in the formate channel at similarly low pH. Resolved water molecules in the protomers suggest a transport mechanism that also permits a facultative NO(2)(-)/H(+) symport.
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