Ultrafast spectroscopy of bacteriorhodopsin

Atsushi Yabushita*, Takayoshi Kobayashi

*Corresponding author for this work

Research output: Contribution to conferencePaperpeer-review


Bacteriorhodopsin (bR) is a retinal protein with the function of a light-driven proton pump in a halobacterial cell membrane. The photocycle of bR is one of the most investigated biological photoinitiated reactions. The primary process in the cycle is the all-trans to 13-cis isomerization of the retinal moiety of bR. In the present work, pump and probe pulses were generated by a NOPA (Non-collinear Optical Parametric Amplifier) seeded by a white-light continuum with a 5-fs pulse compressor system. Both of the spectra of pump and probe pulses are nearly the same and cover a spectral range from 500 to 710 nm with a nearly constant phase. All measurements were performed at room temperature (294K). The spectrograms of the real-time traces probed at 585 nm corresponding to the bleaching spectral range is shown in Fig. 1. It is modulated both in terms of frequency and intensity.

Original languageEnglish
Number of pages1
StatePublished - 19 Oct 2006
Event55th SPSJ Annual Meeting - Nagoya, Japan
Duration: 24 May 200626 May 2006


Conference55th SPSJ Annual Meeting


  • Ultrafast spectroscopy


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