1972
DOI: 10.1073/pnas.69.10.2802
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Formation and Decay of Prelumirhodopsin at Room Temperatures

Abstract: We have excited detergent-solubilized bovine rhodopsin at room temperature with 530-nm light pulses from a mode locked laser, and have observed the appearance and decay of a transient species that absorbs more strongly at 560 nm than does ground-state rhodopsin. Our data show that the absorbing intermediate appears in a time that is at least as short as the experimental resolution (about 6 psec) and decays with a life time of about 30 nsec. The extremely fast risetime supports the hypothesis that prelumirhodop… Show more

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Cited by 251 publications
(107 citation statements)
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“…This event has been classically described as the isomerization of the 11-cis-retinal chromophore of rhodopsin to the all-trans-retinal form (5,6). That full isomerization of a bulky chromophore could occur within this time scale has been questioned (3,7), and speculation still exists as to the nature of this photochemical event.…”
mentioning
confidence: 99%
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“…This event has been classically described as the isomerization of the 11-cis-retinal chromophore of rhodopsin to the all-trans-retinal form (5,6). That full isomerization of a bulky chromophore could occur within this time scale has been questioned (3,7), and speculation still exists as to the nature of this photochemical event.…”
mentioning
confidence: 99%
“…The characterization of this new species has been carried out by photostationary studies in low-temperature glasses (1,2) and by picosecond kinetic studies near room temperatures (3,4). Prelumirhodopsin is formed within 6 X 10-12 sec (6 psec) following excitation of rhodopsin and has an absorption maximum at 543 nm which is bathochromically shifted compared to that of rhodopsin.…”
mentioning
confidence: 99%
“…Formation Times. Absorption of light by rhodopsin leads to formation of prelumirhodopsin in several picoseconds (16,17). Previous semiclassical trajectory studies (7) have demonstrated that this short time is sufficient for photoisomerization even in the restricted active site of a protein.…”
mentioning
confidence: 99%
“…The singlet or triplet excited states of the chromophore when complexed to opsin in rhodopsin have not yet been identified in absorption. The first intermediate that has been observed at room temperature is prelumirhodopsin formed in < 6 ps after light absorption [ 6 ] . An EPR signal was recently observed on illumination of rhodopsin with visible light at 77 K, which was assigned to the triplet state of tryptophan [28].…”
Section: Pimentioning
confidence: 99%