title: [Photo-induced processes and reaction dynamics in bacteriorhodopsin].
abstract: In this review we have focused on the advances madein observing the photo-induced response in bacteriorhodopsin and understanding the mechanisms of retinal-protein interactions which are still obscure. We discuss our recent data obtained on the wild type of bacteriorhodopsin and model compounds. This paper presents our new spectroscopic data on amino acids obtained using FT-IR emission spectroscopy. Based on the characteristics of the structure and optical properties of glycine and L-lysine that simulate a photo-induced behaviour of an opsin under natural conditions we tried to find an answer to one of the most important questions concerning the role of protein in the primary processes in bacteriorhodopsin.
authors.forename: E L
authors.initials: EL
authors.lastname: Terpugov
authors.forename: O V
authors.initials: OV
authors.lastname: Degtyareva
mesh_terms: D001436:Bacteriorhodopsins / Q000737:chemistry*; D005998:Glycine / Q000737:chemistry*; D007700:Kinetics; D008027:Light; D008239:Lysine / Q000737:chemistry*; D055355:Opsins / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D012172:Retinaldehyde / Q000737:chemistry; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D055355:Opsins; D001436:Bacteriorhodopsins; D008239:Lysine; D012172:Retinaldehyde; D005998:Glycine