Transient vibronic structure in ultrafast fluorescence spectra of photoactive yellow protein.
The ultrafast photo-induced dynamics of wild-type photoactive yellow protein and its site-directed mutant of E46Q in aqueous solution was studied at room temperature by femtosecond fluorescence spectroscopy using the optical Kerr-gate method. The vibronic structure appears, depending on the excitation photon energy, in the time-resolved fluorescence spectra just after photoexcitation, which winds with time and disappears on a time scale of sub-picoseconds. This result indicates that the wavepacket is localized in the electronic excited state followed by dumped oscillations and broadening, and also that the initial condition of the wavepacket prepared depending on the excitation photon energy affects much the following ultrafast dynamics in the electronic excited state.
Nakamura
Ryosuke
R
JST-CREST, Venture Business Laboratory, Center for Advanced Science and Innovation, Osaka University, Suita, Osaka, Japan. ryo@mls.eng.osaka-u.ac.jp
Hamada
Norio
N
Ichida
Hideki
H
Tokunaga
Fumio
F
Kanematsu
Yasuo
Y
D019943:Amino Acid Substitution; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D008164:Luminescent Proteins / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry; D013050:Spectrometry, Fluorescence / Q000379:methods; D013053:Spectrophotometry
D001426:Bacterial Proteins; D008164:Luminescent Proteins; D011994:Recombinant Proteins; C054562:yellow fluorescent protein, Bacteria