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  Molecular mechanism of channelrhodopsin

Heberle, J., Lorenz-Fonfria, V., Resler, T., Schultz, B., Schlesinger, R., Bamann, C., et al. (2018). Molecular mechanism of channelrhodopsin. Biochimica et Biophysica Acta, Bioenergetics, 1859: e27. doi:10.1016/j.bbabio.2018.09.084.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0002-DEAD-2 Version Permalink: http://hdl.handle.net/21.11116/0000-0002-E34A-B
Genre: Conference Paper

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 Creators:
Heberle, Joachim1, Author
Lorenz-Fonfria, Victor1, Author
Resler, Tom1, Author
Schultz, Bernd1, Author
Schlesinger, Ramona2, Author
Bamann, Christian3, Author              
Bamberg, Ernst3, Author              
Affiliations:
1Freie Universität Berlin, Department of Physics, Experimental Molecular Biophysics, Berlin, Germany, ou_persistent22              
2Genetic Biophysics, Arnimallee Berlin, Germany, ou_persistent22              
3Emeritusgruppe Biophysikalische Chemie, Max Planck Institute of Biophysics, Max Planck Society, ou_2253652              

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 Abstract: The discovery of channelrhodopsins introduced a new class of ion channels whose conductance can be remotely controlled by light, the feature that founded optogenetics. To explore the connection between the gating mechanism and the influx and efflux of water molecules in channelrhodopsin-2 (ChR2), we have integrated light-induced time-resolved infrared spectroscopy and electrophysiology. Cross-correlation analysis revealed that ion conductance tallies with peptide backbone amide I vibrational changes that report on the hydration of transmembrane α-helices. We show that D253 accepts the proton released by the Schiff base (τ1/2= 10 μs), the latter being reprotonated by D156 (τ1/2= 2 ms) which is part of the DC gate. Previous conclusions on the involvement of E90 in channel opening are ruled out by demonstrating that E90 deprotonates exclusively in the non-conductive P4480 state. Our results merge into a mechanistic proposal that relates the observed proton transfer reactions, protein conformational changes and backbone hydration to the gating of the cation channel. Our results will not only contribute to improve the properties of this optogenetic tool but will also help in elucidating the temporal sequences of ion channeling across the cellular membrane

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Language(s): eng - English
 Dates: 20182018-112018-09
 Publication Status: Published in print
 Pages: 1
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.bbabio.2018.09.084
 Degree: -

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Title: 20th European Bioenergetics Conference
Place of Event: Budapest, Hungary
Start-/End Date: 2018-08-25 - 2018-08-30
Invited: Yes

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Title: Biochimica et Biophysica Acta, Bioenergetics
  Abbreviation : Biochim. Biophys. Acta, Bioenerg.
Source Genre: Journal
 Creator(s):
Zimányi, László1, Editor
Tretter, László1, Editor
Affiliations:
1 20th European Bioenergetics Conference, ou_persistent22            
Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 1859 Sequence Number: e27 Start / End Page: - Identifier: ISSN: 0005-2728
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702_6