Photoinduced isomerization sampling of retinal in bacteriorhodopsin.

ABSTRACT: Photoisomerization of retinoids inside a confined protein pocket represents a critical chemical event in many important biological processes from animal vision, nonvisual light effects, to bacterial light sensing and harvesting. Light-driven proton pumping in bacteriorhodopsin entails exquisite electronic and conformational reconfigurations during its photocycle. However, it has been a major challenge to delineate transient molecular events preceding and following the photoisomerization of the retinal from noisy electron density maps when varying populations of intermediates coexist and evolve as a function of time. Here, I report several distinct early photoproducts deconvoluted from the recently observed mixtures in time-resolved serial crystallography. This deconvolution substantially i

SUBMITTER: Ren Z 

PROVIDER: S-EPMC9364214 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature