ArticleJournal of the American Chemical Society2019
Unified Model for Photophysical and Electro-Optical Properties of Green Fluorescent Proteins.
Article in Journal of the American Chemical Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Tuning Polyacrylate Composition to Recognize and Modulate Fluorescent Proteins.Angewandte Chemie (International ed. in English) · 2026Article
- Ultrafast photophysics of a positive reversibly switchable fluorescent protein.Chemical science · 2025Article
- DNA-Regulated Multi-Protein Complement Control.Journal of the American Chemical Society · 2024Article
- Chemical control of excited-state reactivity of the anionic green fluorescent protein chromophore.Communications chemistry · 2024Article
- Engineering the ChlorON Series: Turn-On Fluorescent Protein Sensors for Imaging Labile Chloride in Living Cells.ACS central science · 2024Article
- Simulation-guided engineering of split GFPs with efficient β-strand photodissociation.Nature communications · 2023Article
- Structural Characterization of Fluorescent Proteins Using Tunable Femtosecond Stimulated Raman Spectroscopy.International journal of molecular sciences · 2023Article
- Structural origin and rational development of bright red noncanonical variants of green fluorescent protein.Physical chemistry chemical physics : PCCP · 2023Article
- PARPs and ADP-ribosylation: Deciphering the complexity with molecular tools.Molecular cell · 2023Review
- Delineating Ultrafast Structural Dynamics of a Green-Red Fluorescent Protein for Calcium Sensing.Biosensors · 2023Article
- Retinal chromophore charge delocalization and confinement explain the extreme photophysics of Neorhodopsin.Nature communications · 2022Article
- Solvent Organization and Electrostatics Tuned by Solute Electronic Structure: Amide versus Non-Amide Carbonyls.The journal of physical chemistry. B · 2022Article
- Structure-based analysis and evolution of a monomerized red-colored chromoprotein from the Olindias formosa jellyfish.Protein science : a publication of the Protein Society · 2022Article
- Energetic Basis and Design of Enzyme Function Demonstrated Using GFP, an Excited-State Enzyme.Journal of the American Chemical Society · 2022Article
- Complexation of Green and Red Kaede Fluorescent Protein Chromophores by a Zwitterion to Probe Electrostatic and Induction Field Effects.The journal of physical chemistry. A · 2022Article
- Internal conversion of the anionic GFP chromophore: in and out of the I-twisted SChemical science · 2022Article
- Photosynthetic reaction center variants made via genetic code expansion show Tyr at M210 tunes the initial electron transfer mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Energy, Structures, and Response Properties with a Fully Coupled QM/AMOEBA/ddCOSMO Implementation.Journal of chemical theory and computation · 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
- Structural and spectrophotometric investigation of two unnatural amino-acid altered chromophores in the superfolder green fluorescent protein.Acta crystallographica. Section D, Structural biology · 2021Article
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Authors and funding
5 authors.
Funding
Abstract
Green fluorescent proteins (GFPs) have become indispensable imaging and optogenetic tools. Their absorption and emission properties can be optimized for specific applications. Currently, no unified framework exists to comprehensively describe these photophysical properties, namely the absorption maxima, emission maxima, Stokes shifts, vibronic progressions, extinction coefficients, Stark tuning rates, and spontaneous emission rates, especially one that includes the effects of the protein environment. In this work, we study the correlations among these properties from systematically tuned GFP environmental mutants and chromophore variants. Correlation plots reveal monotonic trends, suggesting that all these properties are governed by one underlying factor dependent on the chromophore's environment. By treating the anionic GFP chromophore as a mixed-valence compound existing as a superposition of two resonance forms, we argue that this underlying factor is defined as the difference in energy between the two forms, or the driving force, which is tuned by the environment. We then introduce a Marcus-Hush model with the bond length alternation vibrational mode, treating the GFP absorption band as an intervalence charge transfer band. This model explains all of the observed strong correlations among photophysical properties; related subtopics are extensively discussed in the Supporting Information. Finally, we demonstrate the model's predictive power by utilizing the additivity of the driving force. The model described here elucidates the role of the protein environment in modulating the photophysical properties of the chromophore, providing insights and limitations for designing new GFPs with desired phenotypes. We argue that this model should also be generally applicable to both biological and nonbiological polymethine dyes.
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