Evidence for light-induced lysine conformational changes during the primary event of the bacteriorhodopsin photocycle.
Fourier transform infrared difference spectroscopy is used to examine the role of lysine in the primary event of the bacteriorhodopsin photocycle. Isotopically labeled lysine is used to tentatively assign the lysine modes in the BR and K species. The results suggest that the lysine side-chain undergoes conformational changes in concert with the known light-induced chromophore structural alterations.
D001436:Bacteriorhodopsins / Q000378:metabolism / Q000528:radiation effects*; D005583:Fourier Analysis; D006217:Halobacterium / Q000378:metabolism; D008027:Light; D008239:Lysine / Q000528:radiation effects*; D011107:Polylysine / Q000528:radiation effects; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared
D011107:Polylysine; D001436:Bacteriorhodopsins; D008239:Lysine