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. 1986 Feb;83(4):967–971. doi: 10.1073/pnas.83.4.967

Are C14-C15 single bond isomerizations of the retinal chromophore involved in the proton-pumping mechanism of bacteriorhodopsin?

S O Smith, I Hornung, R van der Steen, J A Pardoen, M S Braiman, J Lugtenburg, R A Mathies
PMCID: PMC322991  PMID: 3006035

Abstract

Resonance Raman spectroscopy is used to examine the possibility that C14-C15 single bond isomerizations of the retinal prosthetic group are involved in the photochemical reactions of bacteriorhodopsin. Normal mode calculations show that the vibration that contains predominantly C14-C15 stretch character is approximately equal to 70 cm-1 lower in frequency in the 14-s-cis conformer than in the s-trans case. This geometric effect is insensitive to out-of-plane twists and should be observed in the sterically hindered 13-cis, 14-s-cis retinal protonated Schiff base, which has been proposed as the chromophore in the K and L intermediates of bacteriorhodopsin. Resonance Raman spectra were obtained of K625 by using the low temperature (77 K) spinning-cell technique. Isotopic substitutions with 13C and 2H show that significant C14-C15 stretch character is observed in normal modes at approximately equal to 1185-1195 cm-1. The relatively high frequency of the C14-C15 stretch argues that K625 contains a 13-cis, 14-s-trans chromophore. Similarly, isotopic derivatives show that L550 has a localized C14-C15 stretch at 1172 cm-1, consistent with a 14-s-trans chromophore. These results argue that the primary step in bacteriorhodopsin is a C13=C14 trans----cis photoisomerization that does not involve C14-C15 s-cis structures.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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