ArticleBiophysical journal2006
First steps of retinal photoisomerization in proteorhodopsin.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 81 citations in OpenAlex.
- Ultrafast excited-state proton transfer dynamics using linearized pair-density functional theory.Chemical science · 2026Article
- Multistep 11-Journal of the American Chemical Society · 2025Article
- Retinal to Retinal Energy Transfer in a Bistable Microbial Rhodopsin Dimer.Journal of the American Chemical Society · 2025Article
- Proteorhodopsin insights into the molecular mechanism of vectorial proton transport.Science advances · 2025Article
- A Detailed View on the (Re)isomerization Dynamics in Microbial Rhodopsins Using Complementary Near-UV and IR Readouts.Angewandte Chemie (International ed. in English) · 2025Article
- Reversible Photochromic Reactions of Bacteriorhodopsin fromMolecules (Basel, Switzerland) · 2024Article
- Fluorescence of the Retinal Chromophore in Microbial and Animal Rhodopsins.International journal of molecular sciences · 2023Review
- Effects of the Unique Chromophore-Protein Interactions on the Primary Photoreaction of Schizorhodopsin.The journal of physical chemistry letters · 2023Article
- Far-Red Absorbing Rhodopsins, Insights From Heterodimeric Rhodopsin-Cyclases.Frontiers in molecular biosciences · 2021Review
- NeoR, a near-infrared absorbing rhodopsin.Nature communications · 2020Article
- Absorption and Emission Spectroscopic Investigation of the Thermal Dynamics of the Archaerhodopsin 3 Based Fluorescent Voltage Sensor QuasAr1.International journal of molecular sciences · 2019Article
- Photoreaction Dynamics of Red-Shifting Retinal Analogues Reconstituted in Proteorhodopsin.The journal of physical chemistry. B · 2019Article
- Strong pH-Dependent Near-Infrared Fluorescence in a Microbial Rhodopsin Reconstituted with a Red-Shifting Retinal Analogue.The journal of physical chemistry letters · 2018Article
- Functionally Active Membrane Proteins Incorporated in Mesostructured Silica Films.Journal of the American Chemical Society · 2018Article
- Fluorescence spectroscopy of rhodopsins: insights and approaches.Biochimica et biophysica acta · 2014Review
- Lipid bilayer composition can influence the orientation of proteorhodopsin in artificial membranes.Biophysical journal · 2013Article
- The EF loop in green proteorhodopsin affects conformation and photocycle dynamics.Biophysical journal · 2013Article
- Aspartate-histidine interaction in the retinal schiff base counterion of the light-driven proton pump of Exiguobacterium sibiricum.Biochemistry · 2012Article
- Optical recording of action potentials in mammalian neurons using a microbial rhodopsin.Nature methods · 2011Article
- Initial reaction dynamics of proteorhodopsin observed by femtosecond infrared and visible spectroscopy.Biophysical journal · 2008Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The early steps (<1 ns) in the photocycle of the detergent solubilized proton pump proteorhodopsin are analyzed by ultrafast spectroscopic techniques. A comparison to the first primary events in reconstituted proteorhodopsin as well as to the well known archaeal proton pump bacteriorhodopsin is given. A dynamic Stokes shift observed in fs-time-resolved fluorescence experiments allows a direct observation of early motions on the excited state potential energy surface. The initial dynamics is dominated by sequentially emerging stretching (<150 fs) and torsional (approximately 300 fs) modes of the retinal. The different protonation states of the primary proton acceptor Asp-97 drastically affect the reaction rate and the overall quantum efficiencies of the isomerization reactions, mainly evidenced for time scales above 1 ps. However, no major influence on the fast time scales (approximately 150 fs) could be seen, indicating that the movement out of the Franck-Condon region is fairly robust to electrostatic changes in the retinal binding pocket. Based on fs-time-resolved absorption and fluorescence spectra, ground and exited state contributions can be disentangled and allow to construct a reaction model that consistently explains pH-dependent effects in solubilized and reconstituted proteorhodopsin.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.