Local and distant protein structural changes on photoisomerization of the retinal in bacteriorhodopsin.

ABSTRACT: The photoisomerization of the retinal in bacteriorhodopsin is selective and efficient and yields perturbation of the protein structure within femtoseconds. The stored light energy in the primary intermediate is then used for the net translocation of a proton across the membrane in the microsecond to millisecond regime. This study is aimed at identifying how the protein changes on photoisomerization by using the O-H groups of threonines as internal probes. Polarized Fourier-transform IR spectroscopy of [3-(18)O]threonine-labeled and unlabeled bacteriorhodopsin indicates that 3 of the threonines (of a total of 18) change their hydrogen bonding. One is exchangeable in D(2)O, but two are not. A comprehensive mutation study indicates that the residues involved are Thr-89, Thr-17, and Thr-121 (o

SUBMITTER: Kandori H 

PROVIDER: S-EPMC18286 | biostudies-literature | 2000 Apr

REPOSITORIES: biostudies-literature