Abstract
The simplest known proton pump is bacteriorhodopsin, which forms patches of plasma membrane in primitive halophilic bacteria. The mechanism by which light activates this pump is still uncertain, but extensive spectral and chemical analyses suggest that light-triggered isomerization of the chromophore (vitamin A aldehyde) causes the Schiff-base nitrogen to transfer a proton between two otherwise noninteracting acid-base groups arrayed along a transmembrane channel. The device can generate proton motive forces of nearly 300 mV, which in turn drive ATP synthesis, amino acid uptake, ionic exchange, and probably flagellar movement.
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