Evidence map›Paper›PMID 23509282›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Transient protonation changes in channelrhodopsin-2 and their relevance to channel gating.

Víctor A Lórenz-Fonfría, Tom Resler, Nils Krause, Melanie Nack, Michael Gossing, Gabriele Fischer von Mollard, Christian Bamann, Ernst Bamberg, Ramona Schlesinger, Joachim Heberle

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
8.0field-weighted citation impact, top 1% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

69 citing papers in PubMed, 167 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Structural Insights Into the Opening Mechanism of C1C2 Channelrhodopsin.Journal of the American Chemical Society · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Potassium-selective channelrhodopsins.Biophysics and physicobiology · 2023
    Article
  12. Article
  13. Article
  14. Time-resolved photoacoustics of channelrhodopsins: early energetics and light-driven volume changes.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023
    Article
  15. Article
  16. Article
  17. Modeling theRSC advances · 2022
    Article
  18. Article
  19. Rhodopsin-Based Optogenetics: Basics and Applications.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  20. Article

9 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 4 institutions in 2 countries.

Víctor A Lórenz-FonfríaExperimental Molecular Biophysics, Freie Universität Berlin, 14195 Berlin, Germany.
Tom Resler
Nils Krause
Melanie Nack
Michael Gossing
Gabriele Fischer von Mollard
Christian Bamann
Ernst Bamberg
Ramona Schlesinger
Joachim Heberle
Institute of Molecular Biology and Biophysics · RUBielefeld University · DEFreie Universität Berlin · DEMax Planck Institute of Biophysics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The discovery of the light-gated ion channel channelrhodopsin (ChR) set the stage for the novel field of optogenetics, where cellular processes are controlled by light. However, the underlying molecular mechanism of light-induced cation permeation in ChR2 remains unknown. Here, we have traced the structural changes of ChR2 by time-resolved FTIR spectroscopy, complemented by functional electrophysiological measurements. We have resolved the vibrational changes associated with the open states of the channel (P(2)(390) and P(3)(520)) and characterized several proton transfer events. Analysis of the amide I vibrations suggests a transient increase in hydration of transmembrane α-helices with a t(1/2) = 60 μs, which tallies with the onset of cation permeation. Aspartate 253 accepts the proton released by the Schiff base (t(1/2) = 10 μs), with the latter being reprotonated by aspartic acid 156 (t(1/2) = 2 ms). The internal proton acceptor and donor groups, corresponding to D212 and D115 in bacteriorhodopsin, are clearly different from other microbial rhodopsins, indicating that their spatial position in the protein was relocated during evolution. Previous conclusions on the involvement of glutamic acid 90 in channel opening are ruled out by demonstrating that E90 deprotonates exclusively in the nonconductive P(4)(480) state. Our results merge into a mechanistic proposal that relates the observed proton transfer reactions and the protein conformational changes to the gating of the cation channel.

Indexed as

Models, MolecularProtein ConformationProtonsChannelrhodopsinsHEK293 CellsHumansIon Channel GatingKineticsLasersModels, ChemicalPhotochemistrySpectroscopy, Fourier Transform InfraredChannelrhodopsinsProtons

Identifiers

PMID23509282
PMCPMC3619329
OpenAlexW2130015537

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.