Abstract
In recent years, a large body of data on the structure and dynamic properties of bacteriorhodopsin has been obtained at the atomic level with high temporal and spatial resolution. This information has been summarized in many reviews. In this review, we focused on the recent advances in observing the photo-induced response of bacteriorhodopsin and understanding the mechanisms of retinal–protein interactions, which are still unclear. We discuss our recent spectroscopic data that was obtained for the wild-type bacteriorhodopsin and model amino-acid compounds using FT-IR emission spectroscopy and UV spectroscopy in the visible area. We attempt to find an answer to one of the most important questions concerning the role of protein in bacteriorhodopsin in the primary processes on the basis of the characteristics of the structure and optical properties of glycine and L-lysine, which model the photo-induced behavior of opsin under natural conditions.
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Abbreviations
- BR:
-
bacteriorhodopsin
- LC:
-
liquid crystals
- PSB:
-
protonated Schiff base
- SB:
-
Schiff base
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Original Russian Text © E.L. Terpugov, O.V. Degtyareva, 2015, published in Biofizika, 2015, Vol. 60, No. 2, pp. 293–306.
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Terpugov, E.L., Degtyareva, O.V. Photo-induced processes and the reaction dynamics of bacteriorhodopsin. BIOPHYSICS 60, 232–243 (2015). https://doi.org/10.1134/S0006350915020189
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DOI: https://doi.org/10.1134/S0006350915020189