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.
| Original language | English |
|---|---|
| Pages (from-to) | 589-597 |
| Number of pages | 9 |
| Journal | Biochimica et Biophysica Acta - Bioenergetics |
| Volume | 1837 |
| Issue number | 5 |
| DOIs | |
| State | Published - May 2014 |
Bibliographical note
Funding Information:This work was supported by the Israel Science Foundation , which is administered by the Israel Academy of Sciences and Humanities and US-Israel Binational Science Foundation . S.R. thanks Amir Wand, Rinat Rozin, and Mordechai Sheves for their collaboration on the experimental study of ASR. I.S. thanks Massimo Olivucci, Federico Melaccio and Alessio Valentini for the valuable discussions.
Keywords
- Anabaena Sensory Rhodopsin
- Excited state molecular dynamics
- Photochromism
- Photoisomerization
- Retinal chromophore
- Time resolved spectroscopy