BBiophysical-studies-ofBacteriorhodopsinacteriorhodopsin

An integral membrane protein, with seven membrane-spanninga-helices

and Contains aretinal moleculeprosthetic group, covalently bound in a
Schiff base linkage with the side chain amino group of a centrally-located
lysine residue.

In signaling processes, "7-TM helix receptor, and 247 amino acid residues
(26,000 MW).
When oxygen is scarce, uses light energy to pump protons across
membrane, out of cell, against a concentration gradient (example of primary
active transport).
Generates and maintains [H+] gradient (pH gradient) across cell membrane.
Resulting transmembrane proton gradient = "stored" potential energy, used
by a different protein (ATP synthase) to drive ATP synthesis in a
photosynthetic mode.

Most of protein structure in 7 closely packed transmembrane helices arranged in a

bundle almost perpendicular to plane of membrane. Outer sides of helices (interact
with hydrophobic interior of membrane): many hydrophobic R groups. Inner" sides of
helices, facing interior of bundle, have some charged residues (some charged/polar
residues interact with cofactor (retinal), some involved in proton translocation).

Arrangement sort of opposite of water-soluble globular proteins: in an integral

membrane protein, not only are most R groups on interior of protein hydrophobic, but
R groups on outside of protein are hydrophobic, in contact with membrane lipid core
(Can have hydrophilic groups in interior if needed to interact with prosthetic group like
retinal, or with water in channels, as in porin structures).

Bacteriorhodopsin is a light-driven proton pump

It is the retinal molecule that changes its conformation when absorbing a photon,
resulting in a conformational change of the surrounding protein and the proton
pumping action. It is covalently linked to Lys216 in the chromophore by Schiff base
action. After photo-isomerization of the retinal molecule, Asp85 becomes a proton
acceptor of the donor proton from the retinal molecule. This releases a proton from a
"holding site" into the extracellular side (EC) of the membrane.