Effect of high pressure on the light-induced structural change of bacteriorhodopsin reconstituted in liposome

Dong Gon Park; Sang Sung Nam; Keon Kim; Hyoungman Kim

doi:10.1016/S0005-2728(89)80396-2

Effect of high pressure on the light-induced structural change of bacteriorhodopsin reconstituted in liposome

Dong Gon Park, Sang Sung Nam, Keon Kim, Hyoungman Kim

* Honorary professors

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

1 Citation (Scopus)

Abstract

Bacteriorhodopsin (BR) is reconstituted into multilamellar phosphatidylcholine vesicles. When this reconstituted bacteriorhodopsin is under high pressure without illumination, a structural transition, in which the absorption maximum of the retinal changes from 560 nm to 500 nm, occurs reversibly. Upon illumination, bacteriorhodopsin reconstituted into vesicles is denatured irreversibly and, under high pressure, a 460-nm absorption peak of the chromophore appears transiently.

Original language	English
Pages (from-to)	19-22
Number of pages	4
Journal	BBA - Bioenergetics
Volume	973
Issue number	1
DOIs	https://doi.org/10.1016/S0005-2728(89)80396-2
Publication status	Published - 1989 Jan

Bibliographical note

Funding Information:
This work was supported by the Korean Science and Engineering Foundation (to K.K.).

Keywords

Bacteriorhodopsin
High pressure
Photocycle
Reconstitution
Spectroscopy

ASJC Scopus subject areas

Biophysics
Biochemistry
Cell Biology

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10.1016/S0005-2728(89)80396-2

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title = "Effect of high pressure on the light-induced structural change of bacteriorhodopsin reconstituted in liposome",

abstract = "Bacteriorhodopsin (BR) is reconstituted into multilamellar phosphatidylcholine vesicles. When this reconstituted bacteriorhodopsin is under high pressure without illumination, a structural transition, in which the absorption maximum of the retinal changes from 560 nm to 500 nm, occurs reversibly. Upon illumination, bacteriorhodopsin reconstituted into vesicles is denatured irreversibly and, under high pressure, a 460-nm absorption peak of the chromophore appears transiently.",

keywords = "Bacteriorhodopsin, High pressure, Photocycle, Reconstitution, Spectroscopy",

author = "Park, {Dong Gon} and Nam, {Sang Sung} and Keon Kim and Hyoungman Kim",

note = "Funding Information: This work was supported by the Korean Science and Engineering Foundation (to K.K.).",

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doi = "10.1016/S0005-2728(89)80396-2",

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AU - Park, Dong Gon

AU - Nam, Sang Sung

AU - Kim, Keon

AU - Kim, Hyoungman

N1 - Funding Information: This work was supported by the Korean Science and Engineering Foundation (to K.K.).

PY - 1989/1

Y1 - 1989/1

N2 - Bacteriorhodopsin (BR) is reconstituted into multilamellar phosphatidylcholine vesicles. When this reconstituted bacteriorhodopsin is under high pressure without illumination, a structural transition, in which the absorption maximum of the retinal changes from 560 nm to 500 nm, occurs reversibly. Upon illumination, bacteriorhodopsin reconstituted into vesicles is denatured irreversibly and, under high pressure, a 460-nm absorption peak of the chromophore appears transiently.

AB - Bacteriorhodopsin (BR) is reconstituted into multilamellar phosphatidylcholine vesicles. When this reconstituted bacteriorhodopsin is under high pressure without illumination, a structural transition, in which the absorption maximum of the retinal changes from 560 nm to 500 nm, occurs reversibly. Upon illumination, bacteriorhodopsin reconstituted into vesicles is denatured irreversibly and, under high pressure, a 460-nm absorption peak of the chromophore appears transiently.

KW - Bacteriorhodopsin

KW - High pressure

KW - Photocycle

KW - Reconstitution

KW - Spectroscopy

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JO - BBA - Bioenergetics

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IS - 1

ER -

Effect of high pressure on the light-induced structural change of bacteriorhodopsin reconstituted in liposome

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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