Unifying photocycle model for light adaptation and temporal evolution of cation conductance in channelrhodopsin-2.

ABSTRACT: Although channelrhodopsin (ChR) is a widely applied light-activated ion channel, important properties such as light adaptation, photocurrent inactivation, and alteration of the ion selectivity during continuous illumination are not well understood from a molecular perspective. Herein, we address these open questions using single-turnover electrophysiology, time-resolved step-scan FTIR, and Raman spectroscopy of fully dark-adapted ChR2. This yields a unifying parallel photocycle model integrating now all so far controversial discussed data. In dark-adapted ChR2, the protonated retinal Schiff base chromophore (RSBH⁺) adopts an all-trans,C=N-anti conformation only. Upon light activation, a branching reaction into either a 13-cis,C=N-anti or a 13-cis</

SUBMITTER: Kuhne J 

PROVIDER: S-EPMC6510988 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature