ArticleBiophysical journal2006
Influence of the crystalline state on photoinduced dynamics of photoactive yellow protein studied by ultraviolet-visible transient absorption spectroscopy.
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 26 papers.
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Who cites it
26 citing papers in PubMed.
- Blue and red in the protein world: Photoactive yellow protein and phytochromes as revealed by time-resolved crystallography.Structural dynamics (Melville, N.Y.) · 2024Article
- Protein Nucleation and Crystallization Process with Process Analytical Technologies in a Batch Crystallizer.Crystal growth & design · 2023Article
- Reversible molecular motional switch based on circular photoactive protein oligomers exhibits unexpected photo-induced contraction.Cell reports. Physical science · 2021Article
- Effect of Hydrated Ionic Liquid on Photocycle and Dynamics of Photoactive Yellow Protein.Molecules (Basel, Switzerland) · 2021Article
- Confinement in crystal lattice alters entire photocycle pathway of the Photoactive Yellow Protein.Nature communications · 2020Article
- Nonlinear Optical Investigation of Microbial Chromoproteins.Frontiers in plant science · 2020Article
- Spectrokinetic characterization of photoactive yellow protein films for integrated optical applications.European biophysics journal : EBJ · 2019Article
- Regulation of Protein Structural Changes by Incorporation of a Small-Molecule Linker.International journal of molecular sciences · 2018Article
- Enzyme intermediates captured "on the fly" by mix-and-inject serial crystallography.BMC biology · 2018Article
- Measurements of complex refractive index change of photoactive yellow protein over a wide wavelength range using hyperspectral quantitative phase imaging.Scientific reports · 2018Article
- A short history of structure based research on the photocycle of photoactive yellow protein.Structural dynamics (Melville, N.Y.) · 2017Review
- Combined probes of X-ray scattering and optical spectroscopy reveal how global conformational change is temporally and spatially linked to local structural perturbation in photoactive yellow protein.Physical chemistry chemical physics : PCCP · 2016Article
- Protein structural dynamics revealed by time-resolved X-ray solution scattering.Accounts of chemical research · 2015Article
- Time-resolved crystallography and protein design: signalling photoreceptors and optogenetics.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014Review
- Enzyme transient state kinetics in crystal and solution from the perspective of a time-resolved crystallographer.Structural dynamics (Melville, N.Y.) · 2014Article
- Protein energy landscapes determined by five-dimensional crystallography.Acta crystallographica. Section D, Biological crystallography · 2013Article
- Spectroscopic studies of model photo-receptors: validation of a nanosecond time-resolved micro-spectrophotometer design using photoactive yellow protein and α-phycoerythrocyanin.International journal of molecular sciences · 2013Article
- High-throughput instant quantification of protein expression and purity based on photoactive yellow protein turn off/on label.Protein science : a publication of the Protein Society · 2013Article
- Time-resolved structural studies at synchrotrons and X-ray free electron lasers: opportunities and challenges.Current opinion in structural biology · 2012Review
- pH dependence of the photoactive yellow protein photocycle investigated by time-resolved crystallography.Biophysical journal · 2012Article
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4 authors.
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Abstract
Time-resolved ultraviolet-visible spectroscopy was used to characterize the photocycle transitions in single crystals of wild-type and the E-46Q mutant of photoactive yellow protein (PYP) with microsecond time resolution. The results were compared with the results of similar measurements on aqueous solutions of these two variants of PYP, with and without the components present in the mother liquor of crystals. The experimental data were analyzed with global and target analysis. Distinct differences in the reaction path of a PYP molecule are observed between these conditions when it progresses through its photocycle. In the crystalline state i), much faster relaxation of the late blue-shifted photocycle intermediate back to the ground state is observed; ii), this intermediate in crystalline PYP absorbs at 380 nm, rather than at 350-360 nm in solution; and iii), for various intermediates of this photocycle the forward reaction through the photocycle directly competes with a branching reaction that leads directly to the ground state. Significantly, with these altered characteristics, the spectroscopic data on PYP are fully consistent with the structural data obtained for this photoreceptor protein with time-resolved x-ray diffraction analysis, particularly for wild-type PYP.
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