ArticleNature communications2019
Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
82 citing papers in PubMed, 168 citations in OpenAlex.
- Analysing the significance of small conformational changes and low occupancy states in serial crystallographic data.FEBS open bio · 2026Article
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- Refinement of amino-acid conformation vs. difference density maps in time-resolved serial femtosecond crystallography data analysis.FEBS open bio · 2026Article
- Quantifying optical scattering losses in pump-probe serial femtosecond crystallography experiments.IUCrJ · 2026Article
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- Assessing the problem of excitation light scattering in high-viscosity jets used in serial crystallography sample delivery.Journal of applied crystallography · 2025Article
- Sample delivery methods for protein X-ray crystallography with a special focus on sample consumption.Nature communications · 2025Review
- Ultrafast, remote-controlled protonation reaction enables structural changes in a phytochrome.Science advances · 2025Article
- Multistep 11-Journal of the American Chemical Society · 2025Article
- Ultrafast Protein Dynamics Prior to Retinal Photoisomerization in Microbial Rhodopsins.The journal of physical chemistry letters · 2025Article
- Observation of early events in the photoactivation of Myxobacterial phytochrome using time-resolved serial femtosecond crystallography.Communications chemistry · 2025Article
- TheJournal of applied crystallography · 2025Article
- Macromolecular crystallography and biology at the Linac Coherent Light Source.Journal of synchrotron radiation · 2025Article
- Structural basis for the prolonged photocycle of sensory rhodopsin II revealed by serial synchrotron crystallography.Nature communications · 2025Article
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- Filling data analysis gaps in time-resolved crystallography by machine learning.Structural dynamics (Melville, N.Y.) · 2025Article
- Structural effects of high laser power densities on an early bacteriorhodopsin photocycle intermediate.Nature communications · 2024Article
- Reversible Photochromic Reactions of Bacteriorhodopsin fromMolecules (Basel, Switzerland) · 2024Article
- Exploring the dynamics of allostery through multi-dimensional crystallography.Biophysical reviews · 2024Review
22 more citing papers are in PubMed but not listed here.
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Authors and funding
28 authors at 5 institutions in 3 countries.
Funding
Abstract
Bacteriorhodopsin (bR) is a light-driven proton pump. The primary photochemical event upon light absorption is isomerization of the retinal chromophore. Here we used time-resolved crystallography at an X-ray free-electron laser to follow the structural changes in multiphoton-excited bR from 250 femtoseconds to 10 picoseconds. Quantum chemistry and ultrafast spectroscopy were used to identify a sequential two-photon absorption process, leading to excitation of a tryptophan residue flanking the retinal chromophore, as a first manifestation of multiphoton effects. We resolve distinct stages in the structural dynamics of the all-trans retinal in photoexcited bR to a highly twisted 13-cis conformation. Other active site sub-picosecond rearrangements include correlated vibrational motions of the electronically excited retinal chromophore, the surrounding amino acids and water molecules as well as their hydrogen bonding network. These results show that this extended photo-active network forms an electronically and vibrationally coupled system in bR, and most likely in all retinal proteins.
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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.