Strong Hydrogen Bond between Glutamic Acid 46 and Chromophore Leads to the Intermediate Spectral Form and Excited State Proton Transfer in the Y42F Mutant of the Photoreceptor Photoactive Yellow Protein

Biochemistry ◽  
2009 ◽  
Vol 48 (42) ◽  
pp. 9980-9993 ◽  
Author(s):  
Chandra P. Joshi ◽  
Harald Otto ◽  
Daniel Hoersch ◽  
Terry E. Meyer ◽  
Michael A. Cusanovich ◽  
...  
2010 ◽  
Vol 1 (19) ◽  
pp. 2793-2799 ◽  
Author(s):  
Elizabeth C. Carroll ◽  
Sang-Hun Song ◽  
Masato Kumauchi ◽  
Ivo H. M. van Stokkum ◽  
Askat Jailaubekov ◽  
...  

2014 ◽  
Vol 896 ◽  
pp. 85-88
Author(s):  
Dian Novitasari ◽  
Hironari Kamikubo ◽  
Yoichi Yamazaki ◽  
Mariko Yamaguchi ◽  
Mikio Kataoka

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.


2011 ◽  
Vol 100 (3) ◽  
pp. 308a
Author(s):  
Elizabeth C. Carroll ◽  
Masato Kumauchi ◽  
Wouter D. Hoff ◽  
Delmar S. Larsen

2016 ◽  
Vol 22 (41) ◽  
pp. 14688-14695 ◽  
Author(s):  
Yi-An Chen ◽  
Fan-Yi Meng ◽  
Yen-Hao Hsu ◽  
Cheng-Hsien Hung ◽  
Chi-Lin Chen ◽  
...  

2015 ◽  
Vol 39 (12) ◽  
pp. 9910-9917 ◽  
Author(s):  
Yanling Cui ◽  
Hong Zhao ◽  
Jinfeng Zhao ◽  
Pengyu Li ◽  
Peng Song ◽  
...  

Two proposed competitive types of multiple excited-state proton transfer take place along the intermolecular hydrogen-bond for 7-hydroxyquinoline–(CH3OH)3.


2013 ◽  
Vol 53 (supplement1-2) ◽  
pp. S200
Author(s):  
Dian Novitasari ◽  
Hironari Kamikubo ◽  
Yoichi Yamazaki ◽  
Mariko Yamaguchi ◽  
Mikio Kataoka

2015 ◽  
Vol 44 (18) ◽  
pp. 8406-8418 ◽  
Author(s):  
Cheng-Huei Lin ◽  
Jia-Ling Liao ◽  
Yu-Sin Wu ◽  
Kuan-Yu Liao ◽  
Yun Chi ◽  
...  

Ir(pdpit)(pppo)(bptz) complex (3) reveals a PO–H–N inter- ligand H-bond from which proton transfer takes place.


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