Abstract
Bacteriorhodopsin (BR) is the only protein in the purple membrane of Halobacterium halobium [1]. Like visual pigment rhodopsin, it contains retinal chromophore bonded to protein via a protonated Schiff base linkage [1, 3]. This results in an intense absorption band of purple membrane with its maximum at 570 nm [1]. The light action causes a number of subsequent chemical transformations in BR culminated in the proton transfer across membrane and return of BR to its initial state, designated as BR570 [2]. BR acts as a light-driven proton pump and the light energy is stored up as the energy of transmembrane potential difference [4].
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Kryukov, P.G., Matveetz, Y.A., Sharkov, A.V., Lazarev, Y.A., Terpugov, E.L. (1980). Direct and Reverse Photoreactions in Bacteriorhodopsin at Low Temperatures on Picosecond Time Scala. In: Pratesi, R., Sacchi, C.A. (eds) Lasers in Photomedicine and Photobiology. Springer Series in Optical Sciences, vol 22. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-38270-6_28
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DOI: https://doi.org/10.1007/978-3-540-38270-6_28
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