ArticleJournal of the American Chemical Society2020
Mechanism of Color and Photoacidity Tuning for the Protonated Green Fluorescent Protein Chromophore.
Article in Journal of the American Chemical Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Electronic and Steric Tuning of Molecular Acidity toward Unified Models for Excited State Proton Transfer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Engineering a Green Fluorescent Protein-Core-Inspired NIR-Photocage: ExploringACS central science · 2025Article
- Structural characterization of green fluorescent protein in the I-state.Scientific reports · 2024Article
- Delineating Ultrafast Structural Dynamics of a Green-Red Fluorescent Protein for Calcium Sensing.Biosensors · 2023Article
- 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
- Excitation ratiometric chloride sensing in a standalone yellow fluorescent protein is powered by the interplay between proton transfer and conformational reorganization.Chemical science · 2021Article
- Generation of Fluorescent Bacteria with the Genes Coding for Lumazine Protein and Riboflavin Biosynthesis.Sensors (Basel, Switzerland) · 2021Article
- Unusual Spectroscopic and Electric Field Sensitivity of Chromophores with Short Hydrogen Bonds: GFP and PYP as Model Systems.The journal of physical chemistry. B · 2020Article
- Broadband fluorescence reveals mechanistic differences in excited-state proton transfer to protic and aprotic solvents.Chemical science · 2020Article
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2 authors.
Funding
Abstract
The neutral or A state of the green fluorescent protein (GFP) chromophore is a remarkable example of a photoacid naturally embedded in the protein environment and accounts for the large Stokes shift of GFP in response to near UV excitation. Its color tuning mechanism has been largely overlooked, as it is less preferred for imaging applications than the redder anionic or B state. Past studies, based on site-directed mutagenesis or solvatochromism of the isolated chromophore, have concluded that its color tuning range is much narrower than its anionic counterpart. However, as we performed extensive investigation on more GFP mutants, we found that the color of the neutral chromophore can be more sensitive to protein electrostatics than can the anionic counterpart. Electronic Stark spectroscopy reveals a fundamentally different electrostatic color tuning mechanism for the neutral state of the chromophore that demands a three-form model as compared to that of the anionic state, which requires only two forms (
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