scholarly journals Hydrogen Bonding Controls Excited-State Decay of the Photoactive Yellow Protein Chromophore

2009 ◽  
Vol 131 (38) ◽  
pp. 13580-13581 ◽  
Author(s):  
Martial Boggio-Pasqua ◽  
Michael A. Robb ◽  
Gerrit Groenhof
Keyword(s):  
Hydrogen Bonding ◽  
Excited State ◽  
Photoactive Yellow Protein ◽  
State Decay

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.

Effects of intramolecular hydrogen bonding and sterically forced non-coplanarity on organic donor/acceptor two-photon-absorbing molecules

2018 ◽  
Vol 20 (29) ◽  
pp. 19398-19407 ◽  
Author(s):  
David J. Stewart ◽  
Ramamurthi Kannan ◽  
Tod A. Grusenmeyer ◽  
Jacob M. Artz ◽  
Stephanie L. Long ◽  
...  
Keyword(s):  
Hydrogen Bonding ◽  
Excited State ◽  
Decay Rate ◽  
Rate Constant ◽  
Intramolecular Hydrogen Bonding ◽  
Decay Rate Constant ◽  
Two Photon ◽  
State Decay ◽  
Donor Acceptor ◽  
Intramolecular Hydrogen

Excited-state decay rate constant is controlled by hydrogen bonding, which is switched from intramolecular to intermolecular by choice of solvent.

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