ArticleProceedings of the National Academy of Sciences of the United States of America2011
Proton transfer via a transient linear water-molecule chain in a membrane protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.
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80 citing papers in PubMed, 203 citations in OpenAlex.
- Formation of a Proton-Conducting Hydrogen-Bond Network during the L/M Transition ofThe journal of physical chemistry letters · 2026Article
- Simulating the Photochemical Birth of the Hydrated Electron in Liquid Water.Nature communications · 2026Article
- Photoinduced proton transfer in differently structured water: an EPR approach to solving a classic problem.Scientific reports · 2026Article
- IR Spectroscopy: From Experimental Spectra to High-Resolution Structural Analysis by Integrating Simulations and Machine Learning.The journal of physical chemistry. B · 2025Article
- Role of restraints on hydrogen atoms in Hirshfeld atom refinement: the case of tri-aspartic acid trihydrate.Acta crystallographica Section B, Structural science, crystal engineering and materials · 2025Article
- Revealing the glutamate switch: Insights into proton translocation in plant HBiophysical journal · 2025Article
- Microcanonical kinetics of water-mediated proton transfer in microhydrated 4-aminobenzoic acid.Science (New York, N.Y.) · 2025Article
- A second photoactivatable state of the anion-conducting channelrhodopsin GtACR1 empowers persistent activity.Communications biology · 2025Article
- Proteorhodopsin insights into the molecular mechanism of vectorial proton transport.Science advances · 2025Article
- Unveiling polyphenol-protein interactions: a comprehensive computational analysis.Journal of cheminformatics · 2025Article
- Structural insights into light-gating of potassium-selective channelrhodopsin.Nature communications · 2025Article
- Novel Insights into the Catalytic Mechanism of Collagenolysis by Zn(II)-Dependent Matrix Metalloproteinase-1.Biochemistry · 2024Article
- Salt Effects on the Phase Behavior and Cocrystallization Kinetics of POCB-Water Mixtures.Langmuir : the ACS journal of surfaces and colloids · 2024Article
- Article
- Protonation of Asp116 and distortion of the all-trans retinal chromophore in Krokinobacter eikastus rhodopsin 2 causes a redshift in absorption maximum upon dehydration.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023Article
- Mechanisms of inward transmembrane proton translocation.Nature structural & molecular biology · 2023Article
- Transient water wires mediate selective proton transport in designed channel proteins.Nature chemistry · 2023Article
- Hybrid Quantum Mechanical/Molecular Mechanical Methods For Studying Energy Transduction in Biomolecular Machines.Annual review of biophysics · 2023Review
- Three-Dimensional Structural Insights Have Revealed the Distinct Binding Interactions of Agonists, Partial Agonists, and Antagonists with the µ Opioid Receptor.International journal of molecular sciences · 2023Review
- A Buried Water Network Modulates the Activity of theAntioxidants (Basel, Switzerland) · 2023Article
20 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
High-resolution protein ground-state structures of proton pumps and channels have revealed internal protein-bound water molecules. Their possible active involvement in protein function has recently come into focus. An illustration of the formation of a protonated protein-bound water cluster that is actively involved in proton transfer was described for the membrane protein bacteriorhodopsin (bR) [Garczarek F, Gerwert K (2006) Nature 439:109-112]. Here we show through a combination of time-resolved FTIR spectroscopy and molecular dynamics simulations that three protein-bound water molecules are rearranged by a protein conformational change that resulted in a transient Grotthuss-type proton-transfer chain extending through a hydrophobic protein region of bR. This transient linear water chain facilitates proton transfer at an intermediate conformation only, thereby directing proton transfer within the protein. The rearrangement of protein-bound water molecules that we describe, from inactive positions in the ground state to an active chain in an intermediate state, appears to be energetically favored relative to transient incorporation of water molecules from the bulk. Our discovery provides insight into proton-transfer mechanisms through hydrophobic core regions of ubiquitous membrane spanning proteins such as G-protein coupled receptors or cytochrome C oxidases.
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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.