ArticleProceedings of the National Academy of Sciences of the United States of America2015
Enlightening the photoactive site of channelrhodopsin-2 by DNP-enhanced solid-state NMR spectroscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed.
- High-frequency dynamic nuclear polarization in rotating solids.Science advances · 2026Review
- Optogenetics meets automated patch clamp.iScience · 2026Article
- Operando Magic Angle Spinning Solid-State NMR Spectroscopy of Methanol Photoreforming Over Titania-Coated Silica Monoliths.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- DNP enhanced solid-state NMR of lattice-like microcrystalline protein assemblies facilitated by co-assembly with dinitroxide-tagged proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2026Article
- Solid-State NMR Approaches to Study Protein Structure and Protein-Lipid Interactions.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Dipolar Recoupling in Rotating Solids.Chemical reviews · 2024Review
- Resonant Mixing Dynamic Nuclear Polarization.The journal of physical chemistry letters · 2023Article
- Structural and functional consequences of the H180A mutation of the light-driven sodium pump KR2.Biophysical journal · 2023Article
- Photoreaction Pathways of Bacteriorhodopsin and Its D96N Mutant as Revealed by in Situ Photoirradiation Solid-State NMR.Membranes · 2022Article
- Solid-State NMR Spectroscopy on Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering.Frontiers in chemistry · 2022Review
- The Desensitized Channelrhodopsin-2 Photointermediate Contains 13 -cis, 15 -syn Retinal Schiff Base.Angewandte Chemie (International ed. in English) · 2021Article
- Probing the photointermediates of light-driven sodium ion pump KR2 by DNP-enhanced solid-state NMR.Science advances · 2021Article
- Real-time nuclear magnetic resonance spectroscopy in the study of biomolecular kinetics and dynamics.Magnetic resonance (Gottingen, Germany) · 2021Review
- Structure of a retinal chromophore of dark-adapted middle rhodopsin as studied by solid-state nuclear magnetic resonance spectroscopy.Biophysics and physicobiology · 2021Article
- Solid-state NMR spectroscopy.Nature reviews. Methods primers · 2021Article
- Membrane Protein Structure Determination and Characterisation by Solution and Solid-State NMR.Biology · 2020Review
- Unifying photocycle model for light adaptation and temporal evolution of cation conductance in channelrhodopsin-2.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Photocycle-dependent conformational changes in the proteorhodopsin cross-protomer Asp-His-Trp triad revealed by DNP-enhanced MAS-NMR.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Photoreaction pathways and photointermediates of retinal-binding photoreceptor proteins as revealed by in situ photoirradiation solid-state NMR spectroscopy.Biophysical reviews · 2019Review
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11 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Channelrhodopsin-2 from Chlamydomonas reinhardtii is a light-gated ion channel. Over recent years, this ion channel has attracted considerable interest because of its unparalleled role in optogenetic applications. However, despite considerable efforts, an understanding of how molecular events during the photocycle, including the retinal trans-cis isomerization and the deprotonation/reprotonation of the Schiff base, are coupled to the channel-opening mechanism remains elusive. To elucidate this question, changes of conformation and configuration of several photocycle and conducting/nonconducting states need to be determined at atomic resolution. Here, we show that such data can be obtained by solid-state NMR enhanced by dynamic nuclear polarization applied to (15)N-labeled channelrhodopsin-2 carrying 14,15-(13)C2 retinal reconstituted into lipid bilayers. In its dark state, a pure all-trans retinal conformation with a stretched C14-C15 bond and a significant out-of-plane twist of the H-C14-C15-H dihedral angle could be observed. Using a combination of illumination, freezing, and thermal relaxation procedures, a number of intermediate states was generated and analyzed by DNP-enhanced solid-state NMR. Three distinct intermediates could be analyzed with high structural resolution: the early [Formula: see text] K-like state, the slowly decaying late intermediate [Formula: see text], and a third intermediate populated only under continuous illumination conditions. Our data provide novel insight into the photoactive site of channelrhodopsin-2 during the photocycle. They further show that DNP-enhanced solid-state NMR fills the gap for challenging membrane proteins between functional studies and X-ray-based structure analysis, which is required for resolving molecular mechanisms.
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