Abstract
Two retinal proteins act as light-driven pumps in halobacteria. Bacteriorhodopsin (BR) translocates protons to the medium and halorhodopsin (HR) transports chloride into the cytoplasma. Bacteriorhodopsin’s functional and structural properties are well known. Transport is mediated by a photochemical cycle of the retinal chromophore accompanied by trans to cis isomerization and a reversible deprotonation of its Schiff base. Spectroscopy in combination with the use of retinal analogue compounds demonstrated that the trans to cis isomerization is connected to the primary photochemical reaction (1).
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© 1986 Plenum Press, New York
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Tittor, J., Hegemann, P., Oesterhelt, D. (1986). Comparison of the Two Retinal Proteins Bacteriorhodopsin and Halorhodopsin. In: Papageorgiou, G.C., Barber, J., Papa, S. (eds) Ion Interactions in Energy Transfer Biomembranes. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-8410-6_16
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DOI: https://doi.org/10.1007/978-1-4684-8410-6_16
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