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Ultrafast Backbone Protonation in Channelrhodopsin-1 Captured by Polarization Resolved Fs Vis-pump—IR-Probe Spectroscopy and Computational Methods

1
Institut für Experimentalphysik, Freie Universität Berlin, Arnimallee 14, 1495 Berlin, Germany
2
Fritz Haber Center for Molecular Dynamics Research, Institute of Chemistry, The Hebrew University of Jerusalem, Givat Ram, Jerusalem 9190401, Israel
*
Author to whom correspondence should be addressed.
Academic Editor: Martial Boggio-Pasqua
Molecules 2020, 25(4), 848; https://doi.org/10.3390/molecules25040848 (registering DOI)
Received: 7 January 2020 / Revised: 3 February 2020 / Accepted: 12 February 2020 / Published: 14 February 2020
(This article belongs to the Special Issue New Studies of Photoisomerization)
Channelrhodopsins (ChR) are light-gated ion-channels heavily used in optogenetics. Upon light excitation an ultrafast all-trans to 13-cis isomerization of the retinal chromophore takes place. It is still uncertain by what means this reaction leads to further protein changes and channel conductivity. Channelrhodopsin-1 in Chlamydomonas augustae exhibits a 100 fs photoisomerization and a protonated counterion complex. By polarization resolved ultrafast spectroscopy in the mid-IR we show that the initial reaction of the retinal is accompanied by changes in the protein backbone and ultrafast protonation changes at the counterion complex comprising Asp299 and Glu169. In combination with homology modelling and quantum mechanics/molecular mechanics (QM/MM) geometry optimization we assign the protonation dynamics to ultrafast deprotonation of Glu169, and transient protonation of the Glu169 backbone, followed by a proton transfer from the backbone to the carboxylate group of Asp299 on a timescale of tens of picoseconds. The second proton transfer is not related to retinal dynamics and reflects pure protein changes in the first photoproduct. We assume these protein dynamics to be the first steps in a cascade of protein-wide changes resulting in channel conductivity. View Full-Text
Keywords: photoisomerization; retinal; optogenetics; vibrational spectroscopy; QM/MM calculations; protein dynamics; counter-ion; proton transfer; proton back-transfer; channelrhodopsin photoisomerization; retinal; optogenetics; vibrational spectroscopy; QM/MM calculations; protein dynamics; counter-ion; proton transfer; proton back-transfer; channelrhodopsin
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Stensitzki, T.; Adam, S.; Schlesinger, R.; Schapiro, I.; Heyne, K. Ultrafast Backbone Protonation in Channelrhodopsin-1 Captured by Polarization Resolved Fs Vis-pump—IR-Probe Spectroscopy and Computational Methods. Molecules 2020, 25, 848.

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