ArticleBiophysical journal2019
The Two-Photon Reversible Reaction of the Bistable Jumping Spider Rhodopsin-1.
Article in Biophysical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 31 citations in OpenAlex.
- A multiscale screening platform for rapid GPCR variant profiling reveals color-tuned JSR1 mutants.Biophysical journal · 2026Article
- Retinoid dynamics in vision: from visual cycle biology to retina disease treatments.Pharmacology & therapeutics · 2025Review
- Deprotonation of retinal Schiff base and structural dynamics in the early photoreaction of primate blue cone visual pigment.Biophysical journal · 2025Article
- Active state structures of a bistable visual opsin bound to G proteins.Nature communications · 2024Article
- In-silico predicted mouse melanopsins with blue spectral shifts deliver efficient subcellular signaling.Cell communication and signaling : CCS · 2024Article
- Activating an invertebrate bistable opsin with the all-trans 6.11 retinal analog.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Fluorescence of the Retinal Chromophore in Microbial and Animal Rhodopsins.International journal of molecular sciences · 2023Review
- Functional diversity and evolution in animal rhodopsins: Report for the session 11.Biophysics and physicobiology · 2023Article
- Induction effects on the absorption maxima of photoreceptor proteins.Biophysics and physicobiology · 2023Article
- Evolution of the Automatic Rhodopsin Modeling (ARM) Protocol.Topics in current chemistry (Cham) · 2022Review
- The Impact of Retinal Configuration on the Protein-Chromophore Interactions in Bistable Jumping Spider Rhodopsin-1.Molecules (Basel, Switzerland) · 2021Article
- Optogenetic Modulation of Ion Channels by Photoreceptive Proteins.Advances in experimental medicine and biology · 2021Review
- Article
- Computational and Spectroscopic Characterization of the Photocycle of an Artificial Rhodopsin.The journal of physical chemistry letters · 2020Article
- Light-Sensitive Membrane Proteins as Tools to Generate Precision Treatments.The Journal of membrane biology · 2020Article
- Crystal structure of jumping spider rhodopsin-1 as a light sensitive GPCR.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bistable opsins are photopigments expressed in both invertebrates and vertebrates. These light-sensitive G-protein-coupled receptors undergo a reversible reaction upon illumination. A first photon initiates the cis to trans isomerization of the retinal chromophore-attached to the protein through a protonated Schiff base-and a series of transition states that eventually results in the formation of the thermally stable and active Meta state. Excitation by a second photon reverts this process to recover the original ground state. On the other hand, monostable opsins (e.g., bovine rhodopsin) lose their chromophore during the decay of the Meta II state (i.e., they bleach). Spectroscopic studies on the molecular details of the two-photon cycle in bistable opsins are limited. Here, we describe the successful expression and purification of recombinant rhodopsin-1 from the jumping spider Hasarius adansoni (JSR1). In its natural configuration, spectroscopic characterization of JSR1 is hampered by the similar absorption spectra in the visible spectrum of the inactive and active states. We solved this issue by separating their absorption spectra by replacing the endogenous 11-cis retinal chromophore with the blue-shifted 9-cis JSiR1. With this system, we used time-resolved ultraviolet-visible spectroscopy after pulsed laser excitation to obtain kinetic details of the rise and decay of the photocycle intermediates. We also used resonance Raman spectroscopy to elucidate structural changes of the retinal chromophore upon illumination. Our data clearly indicate that the protonated Schiff base is stable throughout the entire photoreaction. We additionally show that the accompanying conformational changes in the protein are different from those of monostable rhodopsin, as recorded by light-induced FTIR difference spectroscopy. Thus, we envisage JSR1 as becoming a model system for future studies on the reaction mechanisms of bistable opsins, e.g., by time-resolved x-ray crystallography.
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