Related Experiment Video
Updated: Aug 14, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
Internal water molecules of archaeal rhodopsins (Review)
Yuji Furutani1, Hideki Kandori
1Department of Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Nagoya 466-8555, Japan.
Abstract:
Archaeal rhodopsins possess retinal molecule as their chromophores, and their light-energy and light-signal conversions are triggered by all-trans to 13-cis isomerization of the retinal chromophore. Relaxation through structural changes of protein then leads to functional processes, light-driven ion pump or transducer activation. Internal water molecules were considered to play an important role in the functional processes of archaeal rhodopsins, although limited information has been obtained about the structure and function of internal water molecules. Recent progress in Fourier-transform infrared (FTIR) spectroscopy and X-ray crystallography provided new information of water molecules inside archaeal rhodopsins. This article reviews studies on internal water molecules of archaeal rhodopsins by means of low-temperature FTIR spectroscopy.
Related Concept Videos
Gene Families
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
The Photochemical Reaction Center
The Antenna Complex
Channel Rhodopsins
Rhodopsins belong to the family of cell surface proteins called G-protein coupled receptors,...
Photoreceptors and Visual Pathways
Diversity of Archaea III

