ArticleNature communications2020
Confinement in crystal lattice alters entire photocycle pathway of the Photoactive Yellow Protein.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Standard Sample Preparation for Serial Femtosecond Crystallography.Biomolecules · 2025Review
- Temporal ghost imaging for pump-probe X-ray solution scattering.Acta crystallographica. Section A, Foundations and advances · 2025Article
- Article
- TheJournal of applied crystallography · 2025Article
- Watching a signaling protein function: What has been learned over four decades of time-resolved studies of photoactive yellow protein.Structural dynamics (Melville, N.Y.) · 2024Review
- Single Amino Acid Mutation Decouples Photochemistry of the BLUF Domain from the Enzymatic Function of OaPAC and Drives the Enzyme to a Switched-on State.Journal of molecular biology · 2024Article
- From femtoseconds to minutes: time-resolved macromolecular crystallography at XFELs and synchrotrons.Acta crystallographica. Section D, Structural biology · 2024Article
- Origin of the multi-phasic quenching dynamics in the BLUF domains across the species.Nature communications · 2024Article
- The TR-icOS setup at the ESRF: time-resolved microsecond UV-Vis absorption spectroscopy on protein crystals.Acta crystallographica. Section D, Structural biology · 2024Article
- Structural Characterization of Fluorescent Proteins Using Tunable Femtosecond Stimulated Raman Spectroscopy.International journal of molecular sciences · 2023Article
- Reaction Dynamics in the Chrimson Channelrhodopsin: Observation of Product-State Evolution and Slow Diffusive Protein Motions.The journal of physical chemistry letters · 2023Article
- Photoactive Yellow Protein Represents a Distinct, Evolutionarily Novel Family of PAS Domains.Journal of bacteriology · 2022Article
- Serial femtosecond crystallography.Nature reviews. Methods primers · 2022Article
- Photoswitchable Fluorescent Proteins: Mechanisms on Ultrafast Timescales.International journal of molecular sciences · 2022Review
- Crystallographic Studies of Rhodopsins: Structure and Dynamics.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Best practices for time-resolved serial synchrotron crystallography.Acta crystallographica. Section D, Structural biology · 2022Review
- Open hardware microsecond dispersive transient absorption spectrometer for linear optical response.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022Article
- Article
- Ab Initio Quantum-Mechanical Predictions of Semiconducting Photocathode Materials.Micromachines · 2021Review
- QM calculations predict the energetics and infrared spectra of transient glutamine isomers in LOV photoreceptors.Physical chemistry chemical physics : PCCP · 2021Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Femtosecond time-resolved crystallography (TRC) on proteins enables resolving the spatial structure of short-lived photocycle intermediates. An open question is whether confinement and lower hydration of the proteins in the crystalline state affect the light-induced structural transformations. Here, we measured the full photocycle dynamics of a signal transduction protein often used as model system in TRC, Photoactive Yellow Protein (PYP), in the crystalline state and compared those to the dynamics in solution, utilizing electronic and vibrational transient absorption measurements from 100 fs over 12 decades in time. We find that the photocycle kinetics and structural dynamics of PYP in the crystalline form deviate from those in solution from the very first steps following photon absorption. This illustrates that ultrafast TRC results cannot be uncritically extrapolated to in vivo function, and that comparative spectroscopic experiments on proteins in crystalline and solution states can help identify structural intermediates under native conditions.
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