Deprotonation of retinal Schiff base and structural dynamics in the early photoreaction of primate blue cone visual pigment.

ABSTRACT: Animal rhodopsin is a photoreceptive protein crucial for vision, with activation triggered by the cis-trans isomerization of a retinal chromophore upon light absorption. This activation involves a series of thermal intermediates, ultimately leading to G protein-mediated signal transduction. The retinal chromophore is covalently bound to the protein through a protonated Schiff base, and its deprotonation during the formation of the active intermediate is believed to induce structural changes in α-helices that facilitate G-protein interactions. Using low-temperature UV-visible absorption and Fourier transform infrared spectroscopy, we investigated the early photoreaction of the primate blue cone visual pigment (MB). Our results demonstrate that Schiff base deprotonation in the early photorea

SUBMITTER: Mizuno Y 

PROVIDER: S-EPMC12256820 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature