Illumination-dependent changes in the intrinsic fluorescence of bacteriorhodopsin

The paper describes the intrinsic UV fluorescence of bacteriorhodopsin in some detail and determines the changes during the rapid cyclic reaction following light flashes. The results suggest that several tryptophan residues are affected in the protein, among them one or more exposed to aqueous medium. The kinetics of the fluorescence changes coincide closely with events involving the retinal residue during the deprotonation and reprotonation of the Schiff base group.