ArticleMolecules (Basel, Switzerland)2018
Excited State Structural Evolution of a GFP Single-Site Mutant Tracked by Tunable Femtosecond-Stimulated Raman Spectroscopy.
Article in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Ultrafast spectroscopic signatures forChemical science · 2026Article
- Mastering Femtosecond Stimulated Raman Spectroscopy: A Practical Guide.ACS physical chemistry Au · 2024Review
- Structural origin and rational development of bright red noncanonical variants of green fluorescent protein.Physical chemistry chemical physics : PCCP · 2023Article
- Photogrammetry of Ultrafast Excited-State Intramolecular Proton Transfer Pathways in the Fungal Pigment Draconin Red.Molecules (Basel, Switzerland) · 2023Article
- Delineating Ultrafast Structural Dynamics of a Green-Red Fluorescent Protein for Calcium Sensing.Biosensors · 2023Article
- Ultrafast Spectroscopies of Nitrophenols and Nitrophenolates in Solution: From Electronic Dynamics and Vibrational Structures to Photochemical and Environmental Implications.Molecules (Basel, Switzerland) · 2023Article
- To twist or not to twist: From chromophore structure to dynamics inside engineered photoconvertible and photoswitchable fluorescent proteins.Protein science : a publication of the Protein Society · 2023Article
- Rational Design for High Bioorthogonal Fluorogenicity of Tetrazine-Encoded Green Fluorescent Proteins.Natural sciences (Weinheim, Germany) · 2022Article
- Intramolecular Charge Transfer of 1-Aminoanthraquinone and Ultrafast Solvation Dynamics of Dimethylsulfoxide.International journal of molecular sciences · 2021Article
- Excitation ratiometric chloride sensing in a standalone yellow fluorescent protein is powered by the interplay between proton transfer and conformational reorganization.Chemical science · 2021Article
- Switching between Ultrafast Pathways Enables a Green-Red Emission Ratiometric Fluorescent-Protein-Based CaInternational journal of molecular sciences · 2021Article
- Dissecting Optical Response and Molecular Structure of Fluorescent Proteins With Non-canonical Chromophores.Frontiers in molecular biosciences · 2020Article
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Authors and funding
6 authors.
Funding
Abstract
Tracking vibrational motions during a photochemical or photophysical process has gained momentum, due to its sensitivity to the progression of reaction and change of environment. In this work, we implemented an advanced ultrafast vibrational technique, femtosecond-stimulated Raman spectroscopy (FSRS), to monitor the excited state structural evolution of an engineered green fluorescent protein (GFP) single-site mutant S205V. This mutation alters the original excited state proton transfer (ESPT) chain. By strategically tuning the Raman pump to different wavelengths (i.e., 801, 539, and 504 nm) to achieve pre-resonance with transient excited state electronic bands, the characteristic Raman modes of the excited protonated (A*) chromophore species and intermediate deprotonated (I*) species can be selectively monitored. The inhomogeneous distribution/population of A* species go through ESPT with a similar ~300 ps time constant, confirming that bridging a water molecule to protein residue T203 in the ESPT chain is the rate-limiting step. Some A* species undergo vibrational cooling through high-frequency motions on the ~190 ps time scale. At early times, a portion of the largely protonated A* species could also undergo vibrational cooling or return to the ground state with a ~80 ps time constant. On the photoproduct side, a ~1330 cm
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