Abstract
The chapter describes transformation of light energy by retinal-containing proteins. Special attention is given to the mechanism of functioning of bacteriorhodopsin. Bacteriorhodopsin structure, photocycle, and light-dependent transmembrane proton transport are discussed. A short description of other retinal-containing proteins, including halorhodopsin and various sensory rhodopsins, is provided.
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Notes
- 1.
Two intermediates in the bacteriorhodopsin photocycle before K 590 were discovered using spectroscopy with sub-picosecond resolution—a “truly initial” intermediate I 480, and J 625 which is formed from I 480 within 700 fs (7·10−13 s).
- 2.
Chlorophyll-containing photosystems also possess better light-absorbing properties, especially when one takes into account light-harvesting complexes (antennae) which seemed to be absent in case of bacteriorhodopsin (However, it was recently found that a bacteriorhodopsin homolog from the bacterium Salinibacter ruber contains a carotenoid molecule, which functions as a primitive light-harvesting antenna (Balashov and Lanyi 2007)).
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Skulachev, V.P., Bogachev, A.V., Kasparinsky, F.O. (2013). Bacteriorhodopsin. In: Principles of Bioenergetics. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-33430-6_6
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