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Internal Protonation in Retinylidene Phosphatidylethanolamine and the Red-shift in Rhodopsin

Nature volume 222, pages 879–881 (1969)Cite this article

Abstract

AN as yet unexplained aspect of visual pigment chemistry is the large red-shift in the absorption maximum of retinaldehyde, when it is bound to opsin in the visual pigment rhodopsin. The lipoprotein opsin does not absorb in the visible and near ultraviolet, 11-cis retinaldehyde has a λmax of 376 nm (in ethanol), while cattle rhodopsin has a λmax of 498 nm. In the latter substance retinaldehyde has been shown to be bound to an amino group in opsin by a Schiff base link1. Because a retinylidene Schiff base in neutral aqueous environment has a λmax about 20 nm lower than the free aldehyde, the discrepancy with the λmax of rhodopsin is about 140 nm.

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Authors and Affiliations

  1. Department of Biochemistry, University of Nijmegen, Nijmegen, The Netherlands

    F. J. M. DAEMEN & S. L. BONTING

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  1. F. J. M. DAEMEN
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  2. S. L. BONTING
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DAEMEN, F., BONTING, S. Internal Protonation in Retinylidene Phosphatidylethanolamine and the Red-shift in Rhodopsin. Nature 222, 879–881 (1969). https://doi.org/10.1038/222879a0

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