Schenkl, SelmaZgrablic, GoranPortuondo-Campa, ErwinHaacke, StefanChergui, Majed2006-02-272006-02-272006-02-27200710.1016/j.cplett.2007.04.086https://infoscience.epfl.ch/handle/20.500.14299/225778WOS:00024798540003010947We present a systematic study of the time-integrated fluorescence of native bacteriorhodopsin, as a function of excitation wavelength across the visible absorption band. While the fluorescence max. is unaffected, the spectrum broadens on the high-energy side, with decreasing excitation wavelengths. In addn., there is no mirror image relation between emission and absorption, even for the longest excitation wavelengths. By comparison with the retinal cation in soln., we attribute these observations to vibrationally hot emission, and to the topol. of the excited state surface on the way to isomerization.Excited state; Fluorescence; Fluorescence excitation (excitation wavelength dependence of fluorescence of bacteriorhodopsin); Bacteriorhodopsins Role: BSU (Biological studyunclassified)PEP (Physicalengineering or chemical process)PRP (Properties)BIOL (Biological study)PROC (Process) (excitation wavelength dependence of fluorescence of bacteriorhodopsin); Vibrational relaxation (incomplete; excitation wavelength dependence of fluorescence of bacteriorhodopsin); Potential energy surface (of excited state; excitation wavelength dependence of fluorescence of bacteriorhodopsin)bacteriorhodopsin fluorescence excitation wavelengthtext::journal::journal article::research article