Fourier transform raman study of retinal isomeric composition and equilibration in halorhodopsin

L. Zimányi, Janos K. Lanyi

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

Earlier results suggested that the description of the photoreaction of halorhodopsin depends on our being able to distinguish and dissect the photoproducts of the all-trans chromophore from those of the 13-cis, 15-syn chromophore. We have used FT Raman spectroscopy, a nonperturbing method, to analyze the isomeric states of the retinal under various conditions in halorhodopsins from Halobacterium salinarium and Natronobacterium pharaonis. The results indicate that light adaptation occurs in the former protein, and the amounts of the two isomers in the light-adapted and dark-adapted forms are consistent with the weights given to them, from spectroscopic and mathematical criteria, in the earlier calculations. No light adaptation occurs in the latter protein, which contains mostly, but not entirely, all-trans-retinal. There is no light adaptation in either protein in the absence of chloride, the transported substrate of these anion pumps, and in spite of a 13-cis-like photocycle, they contain both all-trans- and 13-cis,15-syn-retinal under these conditions. These findings emphasize the need to consider the photoreactions of both isomers when studying halorhodopsin and provide a reliable method for determining the isomeric mixtures in this protein.

Original languageEnglish
Pages (from-to)1930-1933
Number of pages4
JournalJournal of Physical Chemistry B
Volume101
Issue number10
Publication statusPublished - Mar 6 1997

Fingerprint

Halorhodopsins
light adaptation
Fourier transforms
proteins
Proteins
Chromophores
Chemical analysis
Isomers
chromophores
Anion Transport Proteins
isomers
Raman spectroscopy
Chlorides
Negative ions
chlorides
Pumps
pumps
anions
Substrates

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry

Cite this

Fourier transform raman study of retinal isomeric composition and equilibration in halorhodopsin. / Zimányi, L.; Lanyi, Janos K.

In: Journal of Physical Chemistry B, Vol. 101, No. 10, 06.03.1997, p. 1930-1933.

Research output: Contribution to journalArticle

@article{7576dd90bf954ec7b5fc177ce17cd162,
title = "Fourier transform raman study of retinal isomeric composition and equilibration in halorhodopsin",
abstract = "Earlier results suggested that the description of the photoreaction of halorhodopsin depends on our being able to distinguish and dissect the photoproducts of the all-trans chromophore from those of the 13-cis, 15-syn chromophore. We have used FT Raman spectroscopy, a nonperturbing method, to analyze the isomeric states of the retinal under various conditions in halorhodopsins from Halobacterium salinarium and Natronobacterium pharaonis. The results indicate that light adaptation occurs in the former protein, and the amounts of the two isomers in the light-adapted and dark-adapted forms are consistent with the weights given to them, from spectroscopic and mathematical criteria, in the earlier calculations. No light adaptation occurs in the latter protein, which contains mostly, but not entirely, all-trans-retinal. There is no light adaptation in either protein in the absence of chloride, the transported substrate of these anion pumps, and in spite of a 13-cis-like photocycle, they contain both all-trans- and 13-cis,15-syn-retinal under these conditions. These findings emphasize the need to consider the photoreactions of both isomers when studying halorhodopsin and provide a reliable method for determining the isomeric mixtures in this protein.",
author = "L. Zim{\'a}nyi and Lanyi, {Janos K.}",
year = "1997",
month = "3",
day = "6",
language = "English",
volume = "101",
pages = "1930--1933",
journal = "Journal of Physical Chemistry B Materials",
issn = "1520-6106",
publisher = "American Chemical Society",
number = "10",

}

TY - JOUR

T1 - Fourier transform raman study of retinal isomeric composition and equilibration in halorhodopsin

AU - Zimányi, L.

AU - Lanyi, Janos K.

PY - 1997/3/6

Y1 - 1997/3/6

N2 - Earlier results suggested that the description of the photoreaction of halorhodopsin depends on our being able to distinguish and dissect the photoproducts of the all-trans chromophore from those of the 13-cis, 15-syn chromophore. We have used FT Raman spectroscopy, a nonperturbing method, to analyze the isomeric states of the retinal under various conditions in halorhodopsins from Halobacterium salinarium and Natronobacterium pharaonis. The results indicate that light adaptation occurs in the former protein, and the amounts of the two isomers in the light-adapted and dark-adapted forms are consistent with the weights given to them, from spectroscopic and mathematical criteria, in the earlier calculations. No light adaptation occurs in the latter protein, which contains mostly, but not entirely, all-trans-retinal. There is no light adaptation in either protein in the absence of chloride, the transported substrate of these anion pumps, and in spite of a 13-cis-like photocycle, they contain both all-trans- and 13-cis,15-syn-retinal under these conditions. These findings emphasize the need to consider the photoreactions of both isomers when studying halorhodopsin and provide a reliable method for determining the isomeric mixtures in this protein.

AB - Earlier results suggested that the description of the photoreaction of halorhodopsin depends on our being able to distinguish and dissect the photoproducts of the all-trans chromophore from those of the 13-cis, 15-syn chromophore. We have used FT Raman spectroscopy, a nonperturbing method, to analyze the isomeric states of the retinal under various conditions in halorhodopsins from Halobacterium salinarium and Natronobacterium pharaonis. The results indicate that light adaptation occurs in the former protein, and the amounts of the two isomers in the light-adapted and dark-adapted forms are consistent with the weights given to them, from spectroscopic and mathematical criteria, in the earlier calculations. No light adaptation occurs in the latter protein, which contains mostly, but not entirely, all-trans-retinal. There is no light adaptation in either protein in the absence of chloride, the transported substrate of these anion pumps, and in spite of a 13-cis-like photocycle, they contain both all-trans- and 13-cis,15-syn-retinal under these conditions. These findings emphasize the need to consider the photoreactions of both isomers when studying halorhodopsin and provide a reliable method for determining the isomeric mixtures in this protein.

UR - http://www.scopus.com/inward/record.url?scp=0000942888&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0000942888&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:0000942888

VL - 101

SP - 1930

EP - 1933

JO - Journal of Physical Chemistry B Materials

JF - Journal of Physical Chemistry B Materials

SN - 1520-6106

IS - 10

ER -