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Updated: Oct 2, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
Published on: June 27, 2014
Photoinduced kinetics of bacteriorhodopsin in a dried xerogel glass
Lisa M Shamansky1, Kenny Minh Luong, Duly Han
1Department of Chemistry, California State University, San Bernardino, CA 92407-2397, USA. lshamans@csusb.edu
Abstract:
Time-resolved absorption measurements of the formation and decay kinetics of the M (deprotonated) photocycle intermediate of bR purple membranes entrapped within a dried xerogel glass have been investigated. The dramatic change observed for the M state decay time is in contrast to the relatively insensitive half life reported for the M intermediate of the D96N mutant entrapped within a dried sol-gel glass. The decay kinetics of the M intermediate was observed to slow by a factor of almost 100 when the solvent was removed from the wet-gel to form the dry xerogel glass. Very long aging times for wet-gels resulted in highly biexponential M state decay kinetics. Upon drying, the M state formation rate initially decreased relative to that in solution before increasing in the dry xerogel to a formation rate nearly three times faster than in solution.
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