Resonance Raman Studies of the Purple Membrane

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

Research output: Contribution to journalArticle

255 Scopus citations

Abstract

The individual resonance Raman spectra of the PM568 and M412 forms of light-adapted purple membrane from Halobacterium halobium have been measured using the newly developed flow technique. For comparison purposes, the Raman spectra of the model chromophores, all-trans- and 13-cis retinal n-butylamine, both as protonated and unprotonated Schiff bases, have also been obtained. In agreement with previous work, the Raman data indicate that the retinal chromophore is linked to the purple membrane protein via a protonated Schiff base in the case of the PM568 and an unprotonated Schiff base for the M412 form. The basic mechanism for color regulation in both forms appears to be electron delocalization. The spectral features of the two forms are different from each other and different from the model compound spectra.

Original languageEnglish (US)
Pages (from-to)2995-2999
Number of pages5
JournalBiochemistry
Volume16
Issue number13
DOIs
StatePublished - Jun 1 1977
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

Fingerprint Dive into the research topics of 'Resonance Raman Studies of the Purple Membrane'. Together they form a unique fingerprint.

  • Cite this

    Aton, B., Doukas, A. G., Callender, R. H., Becher, B., & Ebrey, T. G. (1977). Resonance Raman Studies of the Purple Membrane. Biochemistry, 16(13), 2995-2999. https://doi.org/10.1021/bi00632a029