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Fourier transform infrared studies of active-site-methylated rhodopsin. Implications for chromophore-protein interaction, transducin activation, and the reaction pathway.
Short-circuiting the visual cycle with retinotoxic aromatic amines.
Deprotonation of the Schiff base of bacteriorhodopsin is obligate in light-induced proton pumping.
Schiff-base deprotonation is mandatory for light-dependent rhodopsin phosphorylation.
Mechanism of action of aromatic amines that short-circuit the visual cycle.
Deprotonation of the Schiff base of rhodopsin is obligate in the activation of the G protein.