Ultrafast photochemistry of anabaena sensory rhodopsin: experiment and theory.
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.
['Schapiro|Igor|I|', 'Ruhman|Sanford|S|']
D017033:Anabaena D049673:History, 20th Century D049674:History, 21st Century D007536:Isomerism D008027:Light D008958:Models, Molecular D010777:Photochemistry D011789:Quantum Theory D012172:Retinaldehyde D025603:Sensory Rhodopsins D013057:Spectrum Analysis D013816:Thermodynamics D013997:Time Factors
Anabaena Sensory Rhodopsin Retinal chromophore Excited state molecular dynamics Photochromism Photoisomerization Time resolved spectroscopy