Photochemistry of rhodopsin and isorhodopsin investigated on a picosecond time scale.
Bovine rhodopsin and isorhodopsin were excited with a single 530-nm, 7-ps light pulse emitted by a mode-locked Nd 3+ glass laser at room temperature. Within 3 ps of excitation, absorbance changes due to formation of bathorhodopsin were observed. The difference spectra generated during and 100 ps after pulse excitation are presented. The data show that bathorhodopsin formation is completed within 3 ps for both the primary pigments and suggest that a single common bathorhodopsin is photochemically formed from both primary pigments. Our findings provide additional support for the cis-trans isomerization model of the primary event in vision. Additional absorption transients that were observed near 670 and 460 nm are discussed.
D000818:Animals; D002417:Cattle; D007700:Kinetics; D007834:Lasers; D010777:Photochemistry; D010786:Photoreceptor Cells; D012168:Retinal Pigments; D012243:Rhodopsin; D013053:Spectrophotometry / Q000295:instrumentation; D013997:Time Factors
D012168:Retinal Pigments; D012243:Rhodopsin
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