Organisms of all domains of life use photoreceptor proteins to sense and respond to light.
The light-sensitivity of photoreceptor proteins arises from bound chromophores such as …

Internal water molecules are considered to play a crucial role in the functional processes of
proton pump proteins. They may participate in hydrogen-bonding networks inside proteins …

The spectral and photochemical properties of proteorhodopsin (PR) were determined to
compare its proton transport steps to those of bacteriorhodopsin (BR). Static and time …

The various ion pumps in cells and organelles that generate transmembrane
electrochemical potential for protons are driven in various ways: changes in substrate …

Channelrhodopsin-2 (ChR2) is a microbial type rhodopsin and a light-gated cation channel
that controls phototaxis in Chlamydomonas. We expressed ChR2 in COS-cells, purified it …

Active proton transfer through membrane proteins is accomplished by shifts in the acidity of
internal amino acids, prosthetic groups, and water molecules. The recently introduced step …

Light-induced changes of the proton affinities of amino acid side groups are the driving force
for proton translocation in bacteriorhodopsin. Recent progress in obtaining structures of …

Bacteriorhodopsin (bR) is a light-driven proton pump whose function includes two key
membrane-based processes, active transport and energy transduction. Despite extensive …

We report a comprehensive electron crystallographic analysis of conformational changes in
the photocycle of wild-type bacteriorhodopsin and in a variety of mutant proteins with kinetic …

Revised Manuscript Received June 16, 1992 abstract: The pH dependencies of the rate
constants in the photocycles of recombinant D96N and D115N/D96N bacteriorhodopsins …