Photocyclic behavior of rhodopsin induced by an atypical isomerization mechanism.

ABSTRACT: Vertebrate rhodopsin (Rh) contains 11-cis-retinal as a chromophore to convert light energy into visual signals. On absorption of light, 11-cis-retinal is isomerized to all-trans-retinal, constituting a one-way reaction that activates transducin (G_t) followed by chromophore release. Here we report that bovine Rh, regenerated instead with a six-carbon-ring retinal chromophore featuring a C¹¹=C¹² double bond locked in its cis conformation (Rh6mr), employs an atypical isomerization mechanism by converting 11-cis to an 11,13-dicis configuration for prolonged G_t activation. Time-dependent UV-vis spectroscopy, HPLC, and molecular mechanics analyses revealed an atypical thermal reisomerization of the 11,13-dic

SUBMITTER: Gulati S 

PROVIDER: S-EPMC5380078 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature