Photochemistry of rhodopsin and isorhodopsin investigated on a picosecond time scale

T. G. Monger, R. R. Alfano, Robert Callender

Research output: Contribution to journalArticle

41 Citations (Scopus)

Abstract

Bovine rhodopsin and isorhodopsin were excited with a single 530-nm, 7-ps light pulse emitted by a mode-locked Nd3+ 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.

Original languageEnglish (US)
Pages (from-to)105-115
Number of pages11
JournalBiophysical Journal
Volume27
Issue number1
StatePublished - 1979
Externally publishedYes

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Photochemistry
Rhodopsin
Glass
Lasers
Light
Temperature
bathorhodopsin
isorhodopsin

ASJC Scopus subject areas

  • Biophysics

Cite this

Photochemistry of rhodopsin and isorhodopsin investigated on a picosecond time scale. / Monger, T. G.; Alfano, R. R.; Callender, Robert.

In: Biophysical Journal, Vol. 27, No. 1, 1979, p. 105-115.

Research output: Contribution to journalArticle

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