ArticleBiophysical journal2015
Kinetic and vibrational isotope effects of proton transfer reactions in channelrhodopsin-2.
Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 31 citations in OpenAlex.
- Nanosecond Transient IR Spectroscopy of Halorhodopsin in Living Cells.Journal of the American Chemical Society · 2024Article
- The ωNature communications · 2022Article
- The Photoreaction of the Proton-Pumping Rhodopsin 1 From the Maize Pathogenic BasidiomyceteFrontiers in molecular biosciences · 2022Article
- The Two-Photon Reversible Reaction of the Bistable Jumping Spider Rhodopsin-1.Biophysical journal · 2019Article
- pH-sensitive vibrational probe reveals a cytoplasmic protonated cluster in bacteriorhodopsin.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Microbial Rhodopsins: Diversity, Mechanisms, and Optogenetic Applications.Annual review of biochemistry · 2017Review
- Molecular properties of a DTD channelrhodopsin fromBiophysics and physicobiology · 2017Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Channelrhodopsins (ChRs) are light-gated cation channels. After blue-light excitation, the protein undergoes a photocycle with different intermediates. Here, we have recorded transient absorbance changes of ChR2 from Chlamydomonas reinhardtii in the visible and infrared regions with nanosecond time resolution, the latter being accomplished using tunable quantum cascade lasers. Because proton transfer reactions play a key role in channel gating, we determined vibrational as well as kinetic isotope effects (VIEs and KIEs) of carboxylic groups of various key aspartic and glutamic acid residues by monitoring their C=O stretching vibrations in H2O and in D2O. D156 exhibits a substantial KIE (>2) in its deprotonation and reprotonation, which substantiates its role as the internal proton donor to the retinal Schiff base. The unusual VIE of D156, upshifted from 1736 cm(-1) to 1738 cm(-1) in D2O, was scrutinized by studying the D156E variant. The C=O stretch of E156 shifted down by 8 cm(-1) in D2O, providing evidence for the accessibility of the carboxylic group. The C=O stretching band of E90 exhibits a VIE of 9 cm(-1) and a KIE of ∼2 for the de- and the reprotonation reactions during the lifetime of the late desensitized state. The KIE of 1 determined in the time range from 20 ns to 5 ms is incompatible with early deprotonation of E90.
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