ArticleChemical science2016
Active site structure and absorption spectrum of channelrhodopsin-2 wild-type and C128T mutant.
Article in Chemical science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Neural vs Neuromorphic Interfaces: Where Are We Standing?Chemical reviews · 2025Review
- Hybrid Quantum Mechanical/Molecular Mechanical Methods For Studying Energy Transduction in Biomolecular Machines.Annual review of biophysics · 2023Review
- Modeling theRSC advances · 2022Article
- The effect on ion channel of different protonation states of E90 in channelrhodopsin-2: a molecular dynamics simulation.RSC advances · 2021Article
- NeoR, a near-infrared absorbing rhodopsin.Nature communications · 2020Article
- Modulation of Light Energy Transfer from Chromophore to Protein in the Channelrhodopsin ReaChR.Biophysical journal · 2020Article
- Gate-keeper of ion transport-a highly conserved helix-3 tryptophan in a channelrhodopsin chimera, C1C2/ChRWR.Biophysics and physicobiology · 2020Article
- Quantum Mechanical and Molecular Mechanics Modeling of Membrane-Embedded Rhodopsins.The Journal of membrane biology · 2019Review
- Retinal isomerization and water-pore formation in channelrhodopsin-2.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Mechanism by which water and protein electrostatic interactions control proton transfer at the active site of channelrhodopsin.PloS one · 2018Article
- Steady-State Linear and Non-linear Optical Spectroscopy of Organic Chromophores and Bio-macromolecules.Frontiers in chemistry · 2018Review
- Anion-conducting channelrhodopsins with tuned spectra and modified kinetics engineered for optogenetic manipulation of behavior.Scientific reports · 2017Article
- Benchmarking density functional tight binding models for barrier heights and reaction energetics of organic molecules.Journal of computational chemistry · 2017Article
- The form and function of channelrhodopsin.Science (New York, N.Y.) · 2017Review
- Molecular determinants of proton selectivity and gating in the red-light activated channelrhodopsin Chrimson.Scientific reports · 2017Article
- Proton transfer reactions in the red light-activatable channelrhodopsin variant ReaChR and their relevance for its function.The Journal of biological chemistry · 2017Article
- Reaction dynamics of the chimeric channelrhodopsin C1C2.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In spite of considerable interest, the active site of channelrhodopsin still lacks a detailed atomistic description, the understanding of which could strongly enhance the development of novel optogenetics tools. We present a computational study combining different state-of-the-art techniques, including hybrid quantum mechanics/molecular mechanics schemes and high-level quantum chemical methods, to properly describe the hydrogen-bonding pattern between the retinal chromophore and its counterions in channelrhodopsin-2 Wild-Type and C128T mutant. Especially, we show by extensive ground state dynamics that the active site, containing a glutamic acid (E123) and a water molecule, is highly dynamic, sampling three different hydrogen-bonding patterns. This results in a broad absorption spectrum that is representative of the different structural motifs found. A comparison with bacteriorhodopsin, characterized by a pentagonal hydrogen-bonded active site structure, elucidates their different absorption properties.
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