Ultrafast photochemistry of Anabaena Sensory Rhodopsin: Experiment and theory

Igor Schapiro, Sanford Ruhman

Research output: Contribution to journalReview articlepeer-review

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 languageEnglish
Pages (from-to)589-597
Number of pages9
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1837
Issue number5
DOIs
StatePublished - May 2014
Externally publishedYes

Keywords

  • Anabaena Sensory Rhodopsin
  • Excited state molecular dynamics
  • Photochromism
  • Photoisomerization
  • Retinal chromophore
  • Time resolved spectroscopy

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Cell Biology

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