Resonance Raman study of the dark-adapted form of the purple membrane protein

B. Aton; A. G. Doukas; R. H. Callender; B. Becher; T. G. Ebrey

doi:10.1016/0005-2795(79)90417-3

Resonance Raman study of the dark-adapted form of the purple membrane protein

B. Aton, A. G. Doukas, R. H. Callender, B. Becher, T. G. Ebrey

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

19 Scopus citations

Abstract

The resonance Raman spectrum of the dark-adapted form of the purple membrane protein (bacteriorhodopsin) has been obtained and is compared to the light-adapted pigment and model chromophore spectra. As in the light-adapted form, the chromophore-protein linkage is found to be a protonated Schiff base. Electron delocalization appears to play the dominant role in color regulation. The dark-adapted spectrum indicates a conformation closer to 13-cis than the light-adapted spectrum.

Original language	English (US)
Pages (from-to)	424-428
Number of pages	5
Journal	BBA - Protein Structure
Volume	576
Issue number	2
DOIs	https://doi.org/10.1016/0005-2795(79)90417-3
State	Published - Feb 26 1979
Externally published	Yes

Keywords

(Purple membrane)
Bacteriorhodopsin
Chromaphore-protein linkage
Dark-adapted spectrum
Raman resonance

ASJC Scopus subject areas

General Medicine

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10.1016/0005-2795(79)90417-3

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@article{a0bc0822b20f49e7a3d0e15cac2a579f,

title = "Resonance Raman study of the dark-adapted form of the purple membrane protein",

abstract = "The resonance Raman spectrum of the dark-adapted form of the purple membrane protein (bacteriorhodopsin) has been obtained and is compared to the light-adapted pigment and model chromophore spectra. As in the light-adapted form, the chromophore-protein linkage is found to be a protonated Schiff base. Electron delocalization appears to play the dominant role in color regulation. The dark-adapted spectrum indicates a conformation closer to 13-cis than the light-adapted spectrum.",

keywords = "(Purple membrane), Bacteriorhodopsin, Chromaphore-protein linkage, Dark-adapted spectrum, Raman resonance",

author = "B. Aton and Doukas, {A. G.} and Callender, {R. H.} and B. Becher and Ebrey, {T. G.}",

note = "Funding Information: This research was supported in part by grants from the Research Corporation, PSC-BHE award program, and the National Science Foundation (PCM 75-03020 and PCM 77--06728) to City College and National Institutes of Health (EYO 1323 and EYO 0025) and National Science Foundation (PCM-82764) to the University of Ill. B.B. was the recipient of an Institutional National Service Award postdoctoral fellowship (EYO 7005).",

year = "1979",

month = feb,

day = "26",

doi = "10.1016/0005-2795(79)90417-3",

language = "English (US)",

volume = "576",

pages = "424--428",

journal = "BBA - Protein Structure",

issn = "0005-2795",

publisher = "Elsevier",

number = "2",

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TY - JOUR

T1 - Resonance Raman study of the dark-adapted form of the purple membrane protein

AU - Aton, B.

AU - Doukas, A. G.

AU - Callender, R. H.

AU - Becher, B.

AU - Ebrey, T. G.

N1 - Funding Information: This research was supported in part by grants from the Research Corporation, PSC-BHE award program, and the National Science Foundation (PCM 75-03020 and PCM 77--06728) to City College and National Institutes of Health (EYO 1323 and EYO 0025) and National Science Foundation (PCM-82764) to the University of Ill. B.B. was the recipient of an Institutional National Service Award postdoctoral fellowship (EYO 7005).

PY - 1979/2/26

Y1 - 1979/2/26

N2 - The resonance Raman spectrum of the dark-adapted form of the purple membrane protein (bacteriorhodopsin) has been obtained and is compared to the light-adapted pigment and model chromophore spectra. As in the light-adapted form, the chromophore-protein linkage is found to be a protonated Schiff base. Electron delocalization appears to play the dominant role in color regulation. The dark-adapted spectrum indicates a conformation closer to 13-cis than the light-adapted spectrum.

AB - The resonance Raman spectrum of the dark-adapted form of the purple membrane protein (bacteriorhodopsin) has been obtained and is compared to the light-adapted pigment and model chromophore spectra. As in the light-adapted form, the chromophore-protein linkage is found to be a protonated Schiff base. Electron delocalization appears to play the dominant role in color regulation. The dark-adapted spectrum indicates a conformation closer to 13-cis than the light-adapted spectrum.

KW - (Purple membrane)

KW - Bacteriorhodopsin

KW - Chromaphore-protein linkage

KW - Dark-adapted spectrum

KW - Raman resonance

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U2 - 10.1016/0005-2795(79)90417-3

DO - 10.1016/0005-2795(79)90417-3

M3 - Article

C2 - 427199

AN - SCOPUS:0018801766

SN - 0005-2795

VL - 576

SP - 424

EP - 428

JO - BBA - Protein Structure

JF - BBA - Protein Structure

IS - 2

ER -

Resonance Raman study of the dark-adapted form of the purple membrane protein

Abstract

Keywords

ASJC Scopus subject areas

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