scholarly journals Subpicosecond Excited-State Proton Transfer Preceding Isomerization During the Photorecovery of Photoactive Yellow Protein

2010 ◽  
Vol 1 (19) ◽  
pp. 2793-2799 ◽  
Author(s):  
Elizabeth C. Carroll ◽  
Sang-Hun Song ◽  
Masato Kumauchi ◽  
Ivo H. M. van Stokkum ◽  
Askat Jailaubekov ◽  
...  
Keyword(s):  
Excited State ◽  
Proton Transfer ◽  
Photoactive Yellow Protein ◽  
Excited State Proton Transfer

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.

scholarly journals Subpicosecond Excited State Proton Transfer Preceding Isomerization during the Photorecovery of Photoactive Yellow Protein

2011 ◽  
Vol 100 (3) ◽  
pp. 308a
Author(s):  
Elizabeth C. Carroll ◽  
Masato Kumauchi ◽  
Wouter D. Hoff ◽  
Delmar S. Larsen
Keyword(s):  
Excited State ◽  
Proton Transfer ◽  
Photoactive Yellow Protein ◽  
Excited State Proton Transfer

scholarly journals 2P253 Excited State Proton Transfer of Fluorescent Photoactive Yellow Protein Reconstituted with Hydroxycoumarin(18A. Photobiology: Vision & Photoreception,Poster)

2013 ◽  
Vol 53 (supplement1-2) ◽  
pp. S200
Author(s):  
Dian Novitasari ◽  
Hironari Kamikubo ◽  
Yoichi Yamazaki ◽  
Mariko Yamaguchi ◽  
Mikio Kataoka
Keyword(s):  
Excited State ◽  
Proton Transfer ◽  
Photoactive Yellow Protein ◽  
Excited State Proton Transfer

scholarly journals Revealing the role of excited state proton transfer (ESPT) in excited state hydrogen transfer (ESHT): systematic study in phenol–(NH3)n clusters

2021 ◽  
Author(s):  
Christophe Jouvet ◽  
Mitsuhiko Miyazaki ◽  
Masaaki Fujii
Keyword(s):  
Excited State ◽  
Proton Transfer ◽  
Systematic Study ◽  
General Model ◽  
Hydrogen Transfer ◽  
Excited State Proton Transfer

A general model of excited state hydrogen transfer (ESHT) which unifies ESHT and the excited state proton transfer (ESPT) is presented from experimental and theoretical works on phenol–(NH3)n. The hidden role of ESPT is revealed.

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