Resonance Raman study of the primary photochemistry of visual pigments. Hypsorhodopsin.

A. J. Pande, Robert Callender, T. G. Ebrey, M. Tsuda

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

We report here the first resonance Raman results of octopus hypsorhodopsin, a species formed photochemically at very low temperatures from visual pigments. A pump-probe technique was used to obtain Raman spectra from samples at 12 degrees K whose photostationary state mixtures were either hypsorhodopsin rich or hysorhodopsin poor. The data strongly suggest that the Schiff-base linkage between the chromophore of hysorhodopsin and apoprotein is protonated. Further, the results suggest that hypsorhodopsin's chromophore is in some torsionally distorted conformation, possibly having torsional departures from an all-trans isomeric form.

Original languageEnglish (US)
Pages (from-to)573-576
Number of pages4
JournalBiophysical Journal
Volume45
Issue number3
StatePublished - Mar 1984
Externally publishedYes

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Photochemistry
Retinal Pigments
Octopodiformes
Apoproteins
Schiff Bases
Temperature
hypsorhodopsin

ASJC Scopus subject areas

  • Biophysics

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Resonance Raman study of the primary photochemistry of visual pigments. Hypsorhodopsin. / Pande, A. J.; Callender, Robert; Ebrey, T. G.; Tsuda, M.

In: Biophysical Journal, Vol. 45, No. 3, 03.1984, p. 573-576.

Research output: Contribution to journalArticle

Pande, A. J. ; Callender, Robert ; Ebrey, T. G. ; Tsuda, M. / Resonance Raman study of the primary photochemistry of visual pigments. Hypsorhodopsin. In: Biophysical Journal. 1984 ; Vol. 45, No. 3. pp. 573-576.
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