Role of Coherent Low-Frequency Motion in Excited-State Proton Transfer of Green Fluorescent Protein Studied by Time-Resolved Impulsive Stimulated Raman Spectroscopy

被引：64
作者：
Fujisawa, Tomotsumi [1 ,4 ]
Kuramochi, Hikaru [1 ]
Hosoi, Haruko [3 ]
Takeuchi, Satoshi [1 ,2 ]
Tahara, Tahei [1 ,2 ]
机构：
[1] RIKEN, Mol Spect Lab, 2-1 Hirosawa, Wako, Saitama 3510198, Japan
[2] RIKEN, Ctr Adv Photon RAP, Ultrafast Spect Res Team, 2-1 Hirosawa, Wako, Saitama 3510198, Japan
[3] Toho Univ, Fac Sci, Dept Biomol Sci, 2-2-1 Miyama, Funabashi, Chiba 2748510, Japan
[4] Saga Univ, Grad Sch Sci & Engn, Dept Chem & Appl Chem, Saga 8408502, Japan
来源：
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2016年 / 138卷 / 12期
关键词：
VIBRATIONAL-SPECTROSCOPY; GROUND-STATE; DYNAMICS; PHOTOISOMERIZATION; MOLECULES; EVOLUTION; EMISSION; DOMAIN;
D O I：
10.1021/jacs.5b11038
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
Green fluorescent protein (GFP) from jellyfish Aequorea victoria, an essential bioimaging tool, luminesces via excited-state proton transfer (ESPT) in which the phenolic proton of the p-hydroxybenzylideneimidazolinone chromophore is transferred to G1u222 through a hydrogen-bond network. In this process, the ESPT mediated by the low-frequency motion of the chromophore has been proposed. We address this issue using femtosecond time-resolved impulsive stimulated Raman spectroscopy. After coherently exciting low frequency modes (<300 cm(-1)) in the excited state of GFP, we examined the excited-state structural evolution and the ESPT dynamics within the dephasing time of the low-frequency vibration. A clear anharmonic vibrational coupling is found between one high-frequency mode of the chromophore (phenolic CH bend) and a low frequency mode at similar to 104 cm(-1). However, the data show that this low-frequency motion does not substantially affect the ESPT dynamics.
引用
收藏
页码：3942 / 3945
页数：4
相关论文
共 28 条
[1]   Probing the ground state structure of the green fluorescent protein chromophore using Raman spectroscopy [J].
Bell, AF ;
He, X ;
Wachter, RM ;
Tonge, PJ .
BIOCHEMISTRY, 2000, 39 (15) :4423-4431
[2]   Structural basis for dual excitation and photoisomerization of the Aequorea victoria green fluorescent protein [J].
Brejc, K ;
Sixma, TK ;
Kitts, PA ;
Kain, SR ;
Tsien, RY ;
Ormo, M ;
Remington, SJ .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (06) :2306-2311
[3]   Time domain investigation of excited-state vibrational motion in organic molecules by stimulated emission pumping [J].
Cerullo, G ;
Lüer, L ;
Manzoni, C ;
De Silvestri, S ;
Shoshana, O ;
Ruhman, S .
JOURNAL OF PHYSICAL CHEMISTRY A, 2003, 107 (40) :8339-8344
[4]   Ultra-fast excited state dynamics in green fluorescent protein: Multiple states and proton transfer [J].
Chattoraj, M ;
King, BA ;
Bublitz, GU ;
Boxer, SG .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (16) :8362-8367
[5]   Green fluorescent protein: structure, folding and chromophore maturation [J].
Craggs, Timothy D. .
CHEMICAL SOCIETY REVIEWS, 2009, 38 (10) :2865-2875
[6]   The fluorescent protein palette: tools for cellular imaging [J].
Day, Richard N. ;
Davidson, Michael W. .
CHEMICAL SOCIETY REVIEWS, 2009, 38 (10) :2887-2921
[7]   Mapping GFP structure evolution during proton transfer with femtosecond Raman spectroscopy [J].
Fang, Chong ;
Frontiera, Renee R. ;
Tran, Rosalie ;
Mathies, Richard A. .
NATURE, 2009, 462 (7270) :200-U74
[8]   Time-resolved impulsive stimulated Raman scattering from excited-state polyatomic molecules in solution [J].
Fujiyoshi, S ;
Takeuchi, S ;
Tahara, T .
JOURNAL OF PHYSICAL CHEMISTRY A, 2003, 107 (04) :494-500
[9]   Review - The fluorescent toolbox for assessing protein location and function [J].
Giepmans, BNG ;
Adams, SR ;
Ellisman, MH ;
Tsien, RY .
SCIENCE, 2006, 312 (5771) :217-224
[10]   Normal modes and the Duschinsky mixing of the ground- and excited-state vibrations of the green fluorescent protein chromophore [J].
Gnanasekaran, Ramachandran .
CHEMICAL PHYSICS LETTERS, 2013, 587 :61-67
123