Picosecond kinetic absorption and fluorescence studies of bovine rhodopsin with a fixed 11-ene

J. Buchert; V. Stefancic; A. G. Doukas; R. R. Alfano; R. H. Callender; J. Pande; H. Akita; V. Balogh-Nair; K. Nakanishi

doi:10.1016/S0006-3495(83)84351-3

Picosecond kinetic absorption and fluorescence studies of bovine rhodopsin with a fixed 11-ene

J. Buchert, V. Stefancic, A. G. Doukas, R. R. Alfano, R. H. Callender, J. Pande, H. Akita, V. Balogh-Nair, K. Nakanishi

Research output: Contribution to journal › Article › peer-review

43 Scopus citations

Abstract

A synthetic retinal having a fixed 11-cis geometry has been used to prepare a nonbleachable analogue of bovine rhodopsin. Marked differences in the picosecond absorption and fluorescence behavior of this analogue at room temperature, compared with that of natural rhodopsin, were observed. This not only indicates that the 11-cis to trans isomerization of the retinal moiety is the crucial primary event in the photolysis of rhodopsin, but also it establishes that this isomerization must occur on the picosecond time scale or faster.

Original language	English (US)
Pages (from-to)	279-283
Number of pages	5
Journal	Biophysical journal
Volume	43
Issue number	3
DOIs	https://doi.org/10.1016/S0006-3495(83)84351-3
State	Published - 1983
Externally published	Yes

ASJC Scopus subject areas

Biophysics

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title = "Picosecond kinetic absorption and fluorescence studies of bovine rhodopsin with a fixed 11-ene",

abstract = "A synthetic retinal having a fixed 11-cis geometry has been used to prepare a nonbleachable analogue of bovine rhodopsin. Marked differences in the picosecond absorption and fluorescence behavior of this analogue at room temperature, compared with that of natural rhodopsin, were observed. This not only indicates that the 11-cis to trans isomerization of the retinal moiety is the crucial primary event in the photolysis of rhodopsin, but also it establishes that this isomerization must occur on the picosecond time scale or faster.",

author = "J. Buchert and V. Stefancic and Doukas, {A. G.} and Alfano, {R. R.} and Callender, {R. H.} and J. Pande and H. Akita and V. Balogh-Nair and K. Nakanishi",

note = "Funding Information: We are grateful to Professors B. Honig and R. Birge for discussions. This work was supported by grants from the National Institutes of Health, EY02515 to City College, and EY01253 to Columbia University.",

year = "1983",

doi = "10.1016/S0006-3495(83)84351-3",

language = "English (US)",

volume = "43",

pages = "279--283",

journal = "Biophysical journal",

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publisher = "Biophysical Society",

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T1 - Picosecond kinetic absorption and fluorescence studies of bovine rhodopsin with a fixed 11-ene

AU - Buchert, J.

AU - Stefancic, V.

AU - Doukas, A. G.

AU - Alfano, R. R.

AU - Callender, R. H.

AU - Pande, J.

AU - Akita, H.

AU - Balogh-Nair, V.

AU - Nakanishi, K.

N1 - Funding Information: We are grateful to Professors B. Honig and R. Birge for discussions. This work was supported by grants from the National Institutes of Health, EY02515 to City College, and EY01253 to Columbia University.

PY - 1983

Y1 - 1983

N2 - A synthetic retinal having a fixed 11-cis geometry has been used to prepare a nonbleachable analogue of bovine rhodopsin. Marked differences in the picosecond absorption and fluorescence behavior of this analogue at room temperature, compared with that of natural rhodopsin, were observed. This not only indicates that the 11-cis to trans isomerization of the retinal moiety is the crucial primary event in the photolysis of rhodopsin, but also it establishes that this isomerization must occur on the picosecond time scale or faster.

AB - A synthetic retinal having a fixed 11-cis geometry has been used to prepare a nonbleachable analogue of bovine rhodopsin. Marked differences in the picosecond absorption and fluorescence behavior of this analogue at room temperature, compared with that of natural rhodopsin, were observed. This not only indicates that the 11-cis to trans isomerization of the retinal moiety is the crucial primary event in the photolysis of rhodopsin, but also it establishes that this isomerization must occur on the picosecond time scale or faster.

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Picosecond kinetic absorption and fluorescence studies of bovine rhodopsin with a fixed 11-ene

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