Resonance Raman study of the pink membrane photochemically prepared from the deionized blue membrane of H. halobium.

C. Pande, Robert Callender, C. H. Chang, T. G. Ebrey

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Abstract

We report here the Resonance Raman spectrum of a 'pink' membrane (lambda max approximately 495 nm) photochemically generated from the deionized 'blue' membrane (Chang et al., 1985). Comparison of the Raman spectrum of the pink membrane with that of the model compounds, as well as the chromophore extraction data, indicate that the chromophore in the pink membrane is in the 9-cis configuration. The Schiff base peak at approximately 1,652 cm-1 shifts to approximately 1,622 cm-1 upon deuteration of the pink membrane, showing that the chromophore is bound to the bacterio-opsin by a protonated Schiff base linkage. The location of the Schiff base peak, as well as the 30 cm-1 shift that it undergoes upon deuteration, are quite different from the corresponding values for the native bacteriorhodopsin, suggesting differences in the local environment for the Schiff base in these pigments.

Original languageEnglish (US)
Pages (from-to)545-549
Number of pages5
JournalBiophysical Journal
Volume50
Issue number3
StatePublished - Sep 1986
Externally publishedYes

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Schiff Bases
Membranes
Bacteriorhodopsins

ASJC Scopus subject areas

  • Biophysics

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Resonance Raman study of the pink membrane photochemically prepared from the deionized blue membrane of H. halobium. / Pande, C.; Callender, Robert; Chang, C. H.; Ebrey, T. G.

In: Biophysical Journal, Vol. 50, No. 3, 09.1986, p. 545-549.

Research output: Contribution to journalArticle

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