Pyridinium Analogues of Green Fluorescent Protein Chromophore: Fluorogenic Dyes with Large Solvent-Dependent Stokes Shift

2018 ◽  
Vol 9 (8) ◽  
pp. 1958-1963 ◽  
Author(s):  
Yulia G. Ermakova ◽  
Tirthendu Sen ◽  
Yulia A. Bogdanova ◽  
Alexander Yu. Smirnov ◽  
Nadezhda S. Baleeva ◽  
...  
Keyword(s):  
Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Stokes Shift ◽  
Fluorogenic Dyes ◽  
Green Fluorescent

scholarly journals Excited-state locked amino analogues of the green fluorescent protein chromophore with a giant Stokes shift

RSC Advances ◽  
2019 ◽  
Vol 9 (66) ◽  
pp. 38730-38734 ◽  
Author(s):  
Snizhana O. Zaitseva ◽  
Dilara A. Farkhutdinova ◽  
Nadezhda S. Baleeva ◽  
Alexander Yu. Smirnov ◽  
Marina B. Zagudaylova ◽  
...  
Keyword(s):  
Excited State ◽  
Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Stokes Shift ◽  
Large Stokes Shift ◽  
New Class ◽  
Green Fluorescent

We design a new class of excited-state locked GFP chromophores which intrinsically exhibit a very large Stokes shift.

scholarly journals Mechanism of Color and Photoacidity Tuning for the Protonated Green Fluorescent Protein Chromophore

2020 ◽  
Author(s):  
Chi-Yun Lin ◽  
Steven Boxer
Keyword(s):  
Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Stokes Shift ◽  
Site Directed Mutagenesis ◽  
Color Tuning ◽  
Tuning Mechanism ◽  
Donor Acceptor ◽  
Form Model ◽  
Gfp Chromophore ◽  
Green Fluorescent

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 preferable 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 the color of the neutral chromophore to be much more sensitive to protein electrostatics. Electronic Stark spectroscopy reveals a fundamentally different electrostatic color tuning mechanism for the neutral state of the chromophore that demands a three-form model compared with that of the anionic state, which requires only two forms. Specifically, an underlying zwitterionic charge transfer state is required to explain its sensitivity to electrostatics. As the Stokes shift is tightly linked to the protonated chromophore’s photoacidity and excited-state proton transfer (ESPT), we infer design principles of the GFP chromophore as a photoacid through the color tuning mechanisms of both protonation states. The three-form model could also be applied to similar biological and nonbiological dyes and complements the failure of two-form model for donor–acceptor systems with localized electronic distributions.

scholarly journals Mechanism of Color and Photoacidity Tuning for the Protonated Green Fluorescent Protein Chromophore

2020 ◽  
Author(s):  
Chi-Yun Lin ◽  
Steven Boxer
Keyword(s):  
Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Stokes Shift ◽  
Site Directed Mutagenesis ◽  
Color Tuning ◽  
Tuning Mechanism ◽  
Donor Acceptor ◽  
Form Model ◽  
Gfp Chromophore ◽  
Green Fluorescent

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 preferable 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 the color of the neutral chromophore to be much more sensitive to protein electrostatics. Electronic Stark spectroscopy reveals a fundamentally different electrostatic color tuning mechanism for the neutral state of the chromophore that demands a three-form model compared with that of the anionic state, which requires only two forms. Specifically, an underlying zwitterionic charge transfer state is required to explain its sensitivity to electrostatics. As the Stokes shift is tightly linked to the protonated chromophore’s photoacidity and excited-state proton transfer (ESPT), we infer design principles of the GFP chromophore as a photoacid through the color tuning mechanisms of both protonation states. The three-form model could also be applied to similar biological and nonbiological dyes and complements the failure of two-form model for donor–acceptor systems with localized electronic distributions.

scholarly journals Dynamic Stokes shift in green fluorescent protein variants

2007 ◽  
Vol 104 (51) ◽  
pp. 20189-20194 ◽  
Author(s):  
P. Abbyad ◽  
W. Childs ◽  
X. Shi ◽  
S. G. Boxer
Keyword(s):  
Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Stokes Shift ◽  
Green Fluorescent ◽  
Protein Variants
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