Ultrafast Structural Evolution of Photoactive Yellow Protein Chromophore Revealed by Ultraviolet Resonance Femtosecond Stimulated Raman Spectroscopy

2012 ◽  
Vol 3 (15) ◽  
pp. 2025-2029 ◽  
Author(s):  
Hikaru Kuramochi ◽  
Satoshi Takeuchi ◽  
Tahei Tahara
Keyword(s):  
Raman Spectroscopy ◽  
Structural Evolution ◽  
Photoactive Yellow Protein ◽  
Stimulated Raman

Probing structural evolution along multidimensional reaction coordinates with femtosecond stimulated Raman spectroscopy

2012 ◽  
Vol 14 (2) ◽  
pp. 405-414 ◽  
Author(s):  
Renee R. Frontiera ◽  
Chong Fang ◽  
Jyotishman Dasgupta ◽  
Richard A. Mathies
Keyword(s):  
Raman Spectroscopy ◽  
Structural Evolution ◽  
Reaction Coordinates ◽  
Stimulated Raman

scholarly journals Excited State Structural Evolution of a GFP Single-Site Mutant Tracked by Tunable Femtosecond-Stimulated Raman Spectroscopy

Molecules ◽  
2018 ◽  
Vol 23 (9) ◽  
pp. 2226 ◽  
Author(s):  
Longteng Tang ◽  
Liangdong Zhu ◽  
Miles Taylor ◽  
Yanli Wang ◽  
S. Remington ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Excited State ◽  
Time Constant ◽  
Fluorescent Protein ◽  
Stable State ◽  
Structural Evolution ◽  
Single Site ◽  
Vibrational Cooling ◽  
Raman Pump ◽  
Stimulated Raman

Tracking vibrational motions during a photochemical or photophysical process has gained momentum, due to its sensitivity to the progression of reaction and change of environment. In this work, we implemented an advanced ultrafast vibrational technique, femtosecond-stimulated Raman spectroscopy (FSRS), to monitor the excited state structural evolution of an engineered green fluorescent protein (GFP) single-site mutant S205V. This mutation alters the original excited state proton transfer (ESPT) chain. By strategically tuning the Raman pump to different wavelengths (i.e., 801, 539, and 504 nm) to achieve pre-resonance with transient excited state electronic bands, the characteristic Raman modes of the excited protonated (A*) chromophore species and intermediate deprotonated (I*) species can be selectively monitored. The inhomogeneous distribution/population of A* species go through ESPT with a similar ~300 ps time constant, confirming that bridging a water molecule to protein residue T203 in the ESPT chain is the rate-limiting step. Some A* species undergo vibrational cooling through high-frequency motions on the ~190 ps time scale. At early times, a portion of the largely protonated A* species could also undergo vibrational cooling or return to the ground state with a ~80 ps time constant. On the photoproduct side, a ~1330 cm−1 delocalized motion is observed, with dispersive line shapes in both the Stokes and anti-Stokes FSRS with a pre-resonance Raman pump, which indicates strong vibronic coupling, as the mode could facilitate the I* species to reach a relatively stable state (e.g., the main fluorescent state) after conversion from A*. Our findings disentangle the contributions of various vibrational motions active during the ESPT reaction, and offer new structural dynamics insights into the fluorescence mechanisms of engineered GFPs and other analogous autofluorescent proteins.

Early Time Excited-State Structural Evolution of Pyranine in Methanol Revealed by Femtosecond Stimulated Raman Spectroscopy

2013 ◽  
Vol 117 (29) ◽  
pp. 6024-6042 ◽  
Author(s):  
Yanli Wang ◽  
Weimin Liu ◽  
Longteng Tang ◽  
Breland Oscar ◽  
Fangyuan Han ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Excited State ◽  
Structural Evolution ◽  
Early Time ◽  
Stimulated Raman

Reactive and unreactive pathways in a photochemical ring opening reaction from 2D femtosecond stimulated Raman

2015 ◽  
Vol 17 (14) ◽  
pp. 9231-9240 ◽  
Author(s):  
David T. Valley ◽  
David P. Hoffman ◽  
Richard A. Mathies
Keyword(s):  
Raman Spectroscopy ◽  
Ring Opening ◽  
Structural Evolution ◽  
Two Dimensional ◽  
Ring Opening Reaction ◽  
Stimulated Raman

Two-dimensional femtosecond stimulated Raman spectroscopy (2D-FSRS) is used to probe the structural evolution of a modified cyclohexadiene as it undergoes a photoinduced ring opening reaction.

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