Abstract
Bacteriorhodopsin (bR) from halobacterium salinarium converts light energy into chemical energy by pumping protons across the cytoplasmic membrane and thereby creating a proton gradient. The chromophor, all-trans-retinal, is covalently linked to one of the seven transmembrane helices via a protonated Schiff-base. After lightexcitation the chromophore isomerizes and the protein undergoes a photocycle during which one proton is transferred to the extracellular side. Using timeresolved FTIR-techniques two aspartic residues have been identified to be crucial for proton-pumping [1]. D85 works as internal proton-acceptor receiving a proton from the Schiffbase and D96 works as internal proton-donor to the Schiflbase.
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References
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© 1994 Springer-Verlag Berlin Heidelberg
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le Coutre, J., Gerwert, K. (1994). How Catalizes Azide Proton-Pumping in D96N Mutated Bacteriorhodopsin?. In: Lau, A., Werncke, W., Siebert, F. (eds) Time-Resolved Vibrational Spectroscopy VI. Springer Proceedings in Physics, vol 74. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-85060-8_62
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DOI: https://doi.org/10.1007/978-3-642-85060-8_62
Publisher Name: Springer, Berlin, Heidelberg
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