Ultraviolet resonance Raman evidence for the absence of tyrosinate in octopus rhodopsin and the participation of Trp residues in the transition to acid metarhodopsin

FEBS Letters
S HashimotoM Tsuda

Abstract

The ultraviolet (244 nm) resonance Raman spectra of octopus rhodopsin and its photoproduct, acid metarhodopsin, do not give any evidence for a tyrosinate. This finding excludes the possibility that Tyr-112 serves as the counter anion to the protonated Schiff base as does Glu-113 in bovine rhodopsin. Upon photoconversion from rhodopsin to acid metarhodopsin, Trp and Tyr Raman bands decrease in intensity and concomitantly a Trp band shifts in frequency. The changes of Trp Raman bands are ascribed to changes in hydrophobic interactions and conformation, suggesting a possible role of Trp in the photoconversion process of octopus rhodopsin.

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Citations

May 26, 1999·Proceedings of the National Academy of Sciences of the United States of America·M NakagawaT G Ebrey
Sep 16, 2010·Photochemical & Photobiological Sciences : Official Journal of the European Photochemistry Association and the European Society for Photobiology·Kei Tsutsui, Yoshinori Shichida
Aug 29, 2003·Journal of Enzyme Inhibition and Medicinal Chemistry·Cédric LogéMichel Luyckx

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