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Unprotonated chromophore-protein bond in visual pigments from 13C-NMR spectra

Abstract

THE chromophore of visual pigments is generally assumed to be a protonated Schiff base of the 11-cis retinylidene (rhodopsins) or the 11-cis 3-dehydroretinylidene (porphyropsins) groups linked through a lysine amino group to a specific glycoli-poprotein moiety (opsin)1. This protonated Schiff base hypothesis has been supported by plausible though not unequivocal chemical evidence2,3. Recent studies using the physical technique of resonance Raman spectroscopy have also seemed to support this view4–7. In an attempt to confirm this assignment and to explore further the structure and microenvironment of the chomophore, we have studied the nuclear magnetic resonance (NMR) spectra of aqueous suspensions of bovine rhodopsin which contain the chromophore enriched with 13C at specific positions in the retinylidene carbon chain. We report here our findings which clearly support an unprotonated retinylidene Schiff base as the visual chromophore in contrast to the earlier chemical and physical evidence which supports a protonated form.

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SHRIVER, J., MATEESCU, G., FAGER, R. et al. Unprotonated chromophore-protein bond in visual pigments from 13C-NMR spectra. Nature 270, 271–274 (1977). https://doi.org/10.1038/270271a0

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