Ultrafast photochemistry of Anabaena Sensory Rhodopsin: Experiment and theory |
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Authors: | Igor Schapiro Sanford Ruhman |
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Affiliation: | 1. Max Planck Institute for Chemical Energy Conversion, Stiftstr. 34-36, 45470 Mülheim an der Ruhr, Germany;2. Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem 91904, Israel |
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Abstract: | Light induced isomerization of the retinal chromophore activates biological function in all retinal protein (RP) driving processes such as ion-pumping, vertebrate vision and phototaxis in organisms as primitive as archea, or as complex as mammals. This process and its consecutive reactions have been the focus of experimental and theoretical research for decades. The aim of this review is to demonstrate how the experimental and theoretical research efforts can now be combined to reach a more comprehensive understanding of the excited state process on the molecular level. Using the Anabaena Sensory Rhodopsin as an example we will show how contemporary time-resolved spectroscopy and recently implemented excited state QM/MM methods consistently describe photochemistry in retinal proteins. This article is part of a Special Issue entitled: Retinal Proteins — You can teach an old dog new tricks. |
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Keywords: | RPSB, Retinal protonated Schiff base RP, Retinal protein MRP, Microbial retinal protein BR, Bacteriorhodopsin RH, Bovine rhodopsin ASR, Anabaena Sensory Rhodopsin |
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