Internal Protonation in Retinylidene Phosphatidylethanolamine and the Red-shift in Rhodopsin View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1969-05

AUTHORS

F. J. M. DAEMEN, S. L. BONTING

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. More... »

PAGES

879-881

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/222879a0

DOI

http://dx.doi.org/10.1038/222879a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1013683077

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/5770529


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