scholarly journals Photoinduced Chromophore Hydration in the Fluorescent Protein Dreiklang Is Triggered by Ultrafast Excited-State Proton Transfer Coupled to a Low-Frequency Vibration

2017 ◽  
Vol 8 (7) ◽  
pp. 1489-1495 ◽  
Author(s):  
Fabien Lacombat ◽  
Pascal Plaza ◽  
Marie-Aude Plamont ◽  
Agathe Espagne
Keyword(s):  
Excited State ◽  
Proton Transfer ◽  
Fluorescent Protein ◽  
Low Frequency ◽  
Low Frequency Vibration ◽  
Excited State Proton Transfer

The effect of pressure on the excited-state proton transfer in the wild-type green fluorescent protein

2008 ◽  
Vol 455 (4-6) ◽  
pp. 303-306 ◽  
Author(s):  
Pavel Leiderman ◽  
Dan Huppert ◽  
S. James Remington ◽  
Laren M. Tolbert ◽  
Kyril M. Solntsev
Keyword(s):  
Excited State ◽  
Green Fluorescent Protein ◽  
Proton Transfer ◽  
Fluorescent Protein ◽  
Wild Type ◽  
Effect Of Pressure ◽  
Excited State Proton Transfer ◽  
In The Wild ◽  
Green Fluorescent

scholarly journals Excited State Proton Transfer in the Red Fluorescent Protein mKeima

2009 ◽  
Vol 131 (37) ◽  
pp. 13212-13213 ◽  
Author(s):  
J. Nathan Henderson ◽  
Maire F. Osborn ◽  
Nayden Koon ◽  
Rinat Gepshtein ◽  
Dan Huppert ◽  
...  
Keyword(s):  
Excited State ◽  
Proton Transfer ◽  
Fluorescent Protein ◽  
Red Fluorescent Protein ◽  
Excited State Proton Transfer

Against the NEER principle: The third type of photochromism for GFP chromophore derivatives

2021 ◽  
Author(s):  
Jun-Wei Liao ◽  
Robert Sung ◽  
Kuangsen Sung
Keyword(s):  
Excited State ◽  
Green Fluorescent Protein ◽  
Proton Transfer ◽  
Fluorescent Protein ◽  
Fluorescent Proteins ◽  
The Third ◽  
Excited State Proton Transfer ◽  
Gfp Chromophore ◽  
Green Fluorescent

Photochromism is the heart of photochromic fluorescent proteins. Excited-state proton transfer (ESPT) is the major photochromism for green fluorescent protein (GFP) and Z-E photoisomerization through τ-torsion is the major photochromism...

scholarly journals An alternative excited-state proton transfer pathway in green fluorescent protein variant S205V

2007 ◽  
Vol 16 (12) ◽  
pp. 2703-2710 ◽  
Author(s):  
Xiaokun Shu ◽  
Pavel Leiderman ◽  
Rinat Gepshtein ◽  
Nicholas R. Smith ◽  
Karen Kallio ◽  
...  
Keyword(s):  
Excited State ◽  
Green Fluorescent Protein ◽  
Proton Transfer ◽  
Fluorescent Protein ◽  
Protein Variant ◽  
Excited State Proton Transfer ◽  
Green Fluorescent ◽  
Green Fluorescent Protein Variant

Excited-State Proton Transfer in Fluorescent Photoactive Yellow Protein Containing 7-Hydroxycoumarin

2014 ◽  
Vol 896 ◽  
pp. 85-88
Author(s):  
Dian Novitasari ◽  
Hironari Kamikubo ◽  
Yoichi Yamazaki ◽  
Mariko Yamaguchi ◽  
Mikio Kataoka
Keyword(s):  
Hydrogen Bonding ◽  
Excited State ◽  
Proton Transfer ◽  
Fluorescent Protein ◽  
Stokes Shift ◽  
Spectroscopic Studies ◽  
Photoactive Yellow Protein ◽  
Excited State Proton Transfer ◽  
Hydrogen Bonding Network ◽  
Green Fluorescent

Green fluorescent protein (GFP) has been used as an effective tool in various biological fields. The large Stokes shift resulting from an excited-state proton transfer (ESPT) is the basis for the application of GFP in such techniques as ratiometric GFP biosensors. The chromophore of GFP is known to be involved in a hydrogen-bonding network. Previous X-ray crystallographic and FTIR studies suggest that a proton wire along the hydrogen-bonding network plays a role in the ESPT. In order to examine the relationship between the ESPT and hydrogen-bonding network within proteins, we prepared an artificial fluorescent protein using a light-sensor protein, photoactive yellow protein (PYP). The native chromophore of p-coumaric acid (pCA) of PYP undergoes trans-cis isomerization after absorbing a photon, which triggers proton transfers within the hydrogen-bonding network comprised of pCA and proximal amino acid residues. Although PYP emits little fluorescence, we succeeded to reconstitute an artificial fluorescent PYP (PYP-coumarin) by substituting the pCA with its trans-lock analog 7-hydroxycoumarin. Spectroscopic studies with PYP-coumarin revealed that the chromophore takes an anionic form at neutral pH, but is protonated by lowering pH. Both the protonated and deprotonated forms of PYP-coumarin emit intense fluorescence, as compared with the native PYP. In addition, both the deprotonated and protonated forms show identical λmax values in their fluorescence spectra, indicating that ESPT occurs in the artificial fluorescent protein.

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