Resonance raman spectroscopy of octopus rhodopsin and its photoproducts

Chandramohan Pande, Robert Callender, Kwok To Yue, Robert Callender, Thomas G. Ebrey, Motoyuki Tsuda

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

We report here the resonance Raman spectra of octopus rhodopsin and its photoproducts, bathorhodopsin and acid metarhodopsin. These studies were undertaken in order to make comparisons with the well-studied bovine pigments, so as to understand the similarities and the differences in pigment structure and photochemical processes between vertebrates and invertebrates. The flow method was used to obtain the Raman spectrum of rhodopsin at 13 °C. The bathorhodopsin spectrum was obtained by computer subtraction of the spectra containing different photostationary mixtures of rhodopsin, isorhodopsin, hypsorhodopsin, and bathorhodopsin, obtained at 12 K using the pump-probe technique and from measurements at 80 K. Like their bovine counterparts, the Schiff base vibrational mode appears at ∼1660 cm-1 in octopus rhodopsin and the photoproducts, bathorhodopsin and acid metarhodopsin, suggesting a protonated Schiff base linkage between the chromophore and the protein. Differences between the Raman spectra of octopus rhodopsin and bathorhodopsin indicate that the formation of bathorhodopsin is associated with chromophore isomerization. This inference is substantiated by the chromophore chemical extraction data which show that, like the bovine system, octopus rhodopsin is an 11-cis pigment, while the photoproducts contain an all-trans pigment, in agreement with previous work. The octopus rhodopsin and bathorhodopsin spectra ^how marked differences from their bovine counterparts in other respects, however. The differences are most dramatic in the structure-sensitive fingerprint and the HOOP regions. Thus, it appears that although the two species differ in the specific nature of the chromophore-protein interactions, the general process of visual transduction is the same.

Original languageEnglish (US)
Pages (from-to)4941-4947
Number of pages7
JournalBiochemistry
Volume26
Issue number16
StatePublished - 1987
Externally publishedYes

Fingerprint

Octopodiformes
Rhodopsin
Raman Spectrum Analysis
Raman spectroscopy
Chromophores
Pigments
Raman scattering
Schiff Bases
Photochemical Processes
Acids
Dermatoglyphics
Invertebrates
Isomerization
bathorhodopsin
Vertebrates
Proteins
Pumps

ASJC Scopus subject areas

  • Biochemistry

Cite this

Pande, C., Callender, R., Yue, K. T., Callender, R., Ebrey, T. G., & Tsuda, M. (1987). Resonance raman spectroscopy of octopus rhodopsin and its photoproducts. Biochemistry, 26(16), 4941-4947.

Resonance raman spectroscopy of octopus rhodopsin and its photoproducts. / Pande, Chandramohan; Callender, Robert; Yue, Kwok To; Callender, Robert; Ebrey, Thomas G.; Tsuda, Motoyuki.

In: Biochemistry, Vol. 26, No. 16, 1987, p. 4941-4947.

Research output: Contribution to journalArticle

Pande, C, Callender, R, Yue, KT, Callender, R, Ebrey, TG & Tsuda, M 1987, 'Resonance raman spectroscopy of octopus rhodopsin and its photoproducts', Biochemistry, vol. 26, no. 16, pp. 4941-4947.
Pande C, Callender R, Yue KT, Callender R, Ebrey TG, Tsuda M. Resonance raman spectroscopy of octopus rhodopsin and its photoproducts. Biochemistry. 1987;26(16):4941-4947.
Pande, Chandramohan ; Callender, Robert ; Yue, Kwok To ; Callender, Robert ; Ebrey, Thomas G. ; Tsuda, Motoyuki. / Resonance raman spectroscopy of octopus rhodopsin and its photoproducts. In: Biochemistry. 1987 ; Vol. 26, No. 16. pp. 4941-4947.
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