Related Experiment Video
Updated: Aug 13, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
Evidence for light-induced 13-cis, 14-s-cis isomerization in bacteriorhodopsin obtained by FTIR difference
1Institut für Biophysik und Strahlenbiologie der Universität, Albertstrasse 23, D-7800 Freiburg i. Brsg., FRG.
Abstract:
We have obtained by Fourier transformed infra-red (FTIR)-spectroscopy BR-K, BR-L and BR-M difference spectra of bacteriorhodopsin regenerated with isotopically labelled retinals. Thereby, we are able to assign reliably the C(14)-C(15) and C=N stretching vibrations of the various intermediates. The lower C(14)-C(15) stretching vibration frequency in L as compared with 13-cis protonated Schiff base model compounds indicates a 13-cis, 14-s-cis configuration of the retinal in this species. The unusually low C=N stretching vibration in K at 1615 cm indicates less stabilization of the positive charge at the Schiff base by the protein environment. Based on these results, a mechanism is suggested by which the stored light energy is transformed into proton transfers.
More Related Videos
05:03Quantitative Analysis of Dietary Vitamin A Metabolites in Murine Ocular and Non-Ocular Tissues Using High-Performance Liquid Chromatography
Published on: December 27, 2024
08:18Methodology for Studying Interactions of Vitamin A Membrane Receptors and Opsin Protein with their Ligands in Generating the Retinylidene Protein
Published on: October 4, 2024
Related Concept Videos
Channel Rhodopsins
Rhodopsins belong to the family of cell surface proteins called G-protein coupled receptors,...
Photoreceptors and Visual Pathways
Total Internal Reflection Fluorescence Microscopy
Infrared (IR) Spectroscopy: Overview
Different compounds display unique properties due to their...
Photochemical Electrocyclic Reactions: Stereochemistry
Selection Rules: Photochemical Activation