ArticlePloS one2018
Mechanism by which water and protein electrostatic interactions control proton transfer at the active site of channelrhodopsin.
Article in PloS one, 2018. 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, 26 citations in OpenAlex.
- Structural insights into light-gating of potassium-selective channelrhodopsin.Nature communications · 2025Article
- The biophysics of water in cell biology: perspectives on a keystone for both marine sciences and cancer research.Frontiers in cell and developmental biology · 2024Article
- Embedding Nonrigid Solutes in an Averaged Environment: A Case Study on Rhodopsins.Journal of chemical theory and computation · 2023Article
- Leveraging intrinsic flexibility to engineer enhanced enzyme catalytic activity.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Deciphering the Spectral Tuning Mechanism in Proteorhodopsin: The Dominant Role of Electrostatics Instead of Chromophore Geometry.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- The Impact of Retinal Configuration on the Protein-Chromophore Interactions in Bistable Jumping Spider Rhodopsin-1.Molecules (Basel, Switzerland) · 2021Article
- The effect on ion channel of different protonation states of E90 in channelrhodopsin-2: a molecular dynamics simulation.RSC advances · 2021Article
- Structures of the archaerhodopsin-3 transporter reveal that disordering of internal water networks underpins receptor sensitization.Nature communications · 2021Article
- Phosphatidylglyerol Lipid Binding at the Active Site of an Intramembrane Protease.The Journal of membrane biology · 2020Review
- Modulation of Light Energy Transfer from Chromophore to Protein in the Channelrhodopsin ReaChR.Biophysical journal · 2020Article
- Ultrafast Backbone Protonation in Channelrhodopsin-1 Captured by Polarization Resolved Fs Vis-pump-IR-Probe Spectroscopy and Computational Methods.Molecules (Basel, Switzerland) · 2020Article
- Role of Computational Methods in Going beyond X-ray Crystallography to Explore Protein Structure and Dynamics.International journal of molecular sciences · 2018Review
- An Atomistic Model of a Precursor State of Light-Induced Channel Opening of Channelrhodopsin.Biophysical journal · 2018Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Channelrhodopsins are light-sensitive ion channels whose reaction cycles involve conformation-coupled transfer of protons. Understanding how channelrhodopsins work is important for applications in optogenetics, where light activation of these proteins triggers changes in the transmembrane potential across excitable membranes. A fundamental open question is how the protein environment ensures that unproductive proton transfer from the retinal Schiff base to the nearby carboxylate counterion is avoided in the resting state of the channel. To address this question, we performed combined quantum mechanical/molecular mechanical proton transfer calculations with explicit treatment of the surrounding lipid membrane. The free energy profiles computed for proton transfer to the counterion, either via a direct jump or mediated by a water molecule, demonstrate that, when retinal is all-trans, water and protein electrostatic interactions largely favour the protonated retinal Schiff base state. We identified a conserved lysine group as an essential structural element for the proton transfer energetics in channelrhodopsins.
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