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Updated: Jul 1, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
Water molecules in the schiff base region of bacteriorhodopsin
Mikihiro Shibata1, Taro Tanimoto, Hideki Kandori
1Department of Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Nagoya 466-8555, Japan.
Abstract:
The Schiff base region of bacteriorhodopsin (BR), a light-driven proton pump, contains a pentagonal cluster, being composed of three water molecules and one oxygen each of Asp85 and Asp212. Asp85 and Asp212 are located at similar distances from the retinal Schiff base, whereas the Schiff base proton is transferred only to Asp85 during the pump function. The present FTIR study experimentally established the stretching vibration of water402 hydrating with Asp85 by use of various BR mutants, whose frequency (2171 cm-1 as the O-D stretch) indicates very strong hydrogen bond.
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