Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5377239 | Chemical Physics | 2006 | 4 Pages |
Abstract
Proteorhodopsin (PR), an archaeal-type rhodopsin found in marine bacteria, functions as a light-driven proton pump. The proton-pumping activity of PR is highly pH-dependent, its exact mechanism being still controversial. The present FTIR spectra are very similar at pH 10 and 5 in the 1800-900Â cmâ1 region, but significantly different in the 2700-2000Â cmâ1 region. This implies that the structure and structural changes are almost identical between the alkaline and acid forms of PR except for water-containing hydrogen-bonding network. In addition, different hydrogen-bonding strength of internal water molecule may be correlated with the pH-dependent proton-pumping activity of PR.
Related Topics
Physical Sciences and Engineering
Chemistry
Physical and Theoretical Chemistry
Authors
Yuji Furutani, Daisuke Ikeda, Mikihiro Shibata, Hideki Kandori,