Spectral and kinetic fluorescence properties of native and nonisomerizing retinal in bacteriorhodopsin.

@article{Haacke2001SpectralAK,
  title={Spectral and kinetic fluorescence properties of native and nonisomerizing retinal in bacteriorhodopsin.},
  author={Stefan Haacke and S Vinzani and Selma Schenkl and Majed Chergui},
  journal={Chemphyschem : a European journal of chemical physics and physical chemistry},
  year={2001},
  volume={2 5},
  pages={310-5}
}
Steady-state and picosecond (ps) fluorescence studies of wild-type bacteriorhodopsin (wt-bR) and of a nonisomerizing analog locked in the all-trans configuration have been performed. Extending earlier work done by femtosecond absorption spectroscopy, we observe a strong similarity between both proteins in both fluorescence spectra and Stokes shift thus confirming the previous result that the fluorescent state I460 of the native bR proteins is in the all-trans configuration. Comparison of the… CONTINUE READING