ArticleBiophysical journal2005
Hydroxide and proton migration in aquaporins.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 58 citations in OpenAlex.
- Self-protecting CoFeAl-layered double hydroxides enable stable and efficient brine oxidation at 2 A cmNature communications · 2024Article
- Nuclear spin effects in biological processes.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Increasing Accessible Active Site Density of Non-Precious Metal Oxygen Reduction Reaction Catalysts through Ionic Liquid Modification.ACS applied materials & interfaces · 2023Article
- Major ceRNA regulation and key metabolic signature analysis of intervertebral disc degeneration.BMC musculoskeletal disorders · 2021Article
- Water in Nanopores and Biological Channels: A Molecular Simulation Perspective.Chemical reviews · 2020Review
- Cyclic γ-Peptides With Transmembrane Water Channel Properties.Frontiers in chemistry · 2020Article
- Transport of Reactive Oxygen and Nitrogen Species across Aquaporin: A Molecular Level Picture.Oxidative medicine and cellular longevity · 2019Article
- Review
- Human cellular retinaldehyde-binding protein has secondary thermal 9-cis-retinal isomerase activity.Journal of the American Chemical Society · 2014Article
- Aquaporins with anion/monocarboxylate permeability: mechanisms, relevance for pathogen-host interactions.Frontiers in pharmacology · 2014Review
- Molecular dynamics study of the archaeal aquaporin AqpM.BMC genomics · 2011Article
- Single-file water in nanopores.Physical chemistry chemical physics : PCCP · 2011Article
- Molecular simulations of ion channels: a quantum chemist's perspective.The Journal of general physiology · 2010Article
- Proton solvation and transport in aqueous and biomolecular systems: insights from computer simulations.The journal of physical chemistry. B · 2007Review
- Charge delocalization in proton channels, I: the aquaporin channels and proton blockage.Biophysical journal · 2007Article
- Effects of electric fields on proton transport through water chains.The Journal of chemical physics · 2006Article
- Single-channel water permeabilities of Escherichia coli aquaporins AqpZ and GlpF.Biophysical journal · 2006Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hypothetical hydroxide and proton migration along the linear water chain in Aquaporin GlpF from Escherichia coli are studied by ab initio Car-Parrinello molecular dynamics simulations. It is found that the protein stabilizes a bipolar single file of water. The single file features a contiguous set of water-water hydrogen bonds in which polarization of the water molecules vary with position along the channel axis. Deprotonation of the water chain promotes the reorientation of water molecules while the hydroxide ion rapidly migrates by sequentially accepting protons from the neighboring water molecules. The hydroxide ion is not attracted by a conserved, channel-lining arginine residue, but is immobilized at two centrally located, conserved Asparagine-Proline-Alanine motifs where fourfold coordination stabilizes the ion. Hydroxide transition from the channel vestibules into the channel lumen is strongly influenced by electrostatic coupling to two conserved oppositely aligned macrodipoles. This suggests that the macrodipole's negative poles play a role in preventing hydroxide ions from entering into the channel's inner vestibules. Water protonation within the lumen facilitates water reorientation and subsequent proton expelling occurs. In the periplasmic half-channel, expelling occurs via the Grotthuss mechanism. Protonation within the cytoplasmic half-channel implies wire-breakage at the Asn-Pro-Ala motifs. The proton is here diffusively rejected as (H(5)O(2))(+).
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.