Chromcrphore-Environment Interaction of Visual Pigments in Model System View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1971-09

AUTHORS

M. D. HIRTENSTEIN, M. AKHTAR

ABSTRACT

SEVERAL laboratories1–6 have recently been concerned with the mechanism of the bathochromic shift of about 120 nm which results when 11-cis retinal (λmax 380 nm) combines with the protein opsin to form rhodopsin (λmax 498 nm). A red shift of up to 186 nm is involved in the formation of iodopsin from 11-cis retinal and cone opsin7,8. The active site of bovine rhodopsin consists of the 11-cis retinylidene chromophore attached to a primary amine group of the protein forming a Schiff-base linkage of the type shown in Fig. 1, Ia. On the basis of the chemical reactions of rhodopsin and its derivatives it has been suggested that an interaction between a protonated form of the chromophore (structure of the type Ib) and a lipophilic environment contributes11 to the red shift. More... »

PAGES

94

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/newbio233094a0

DOI

http://dx.doi.org/10.1038/newbio233094a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1013482441

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/5287006


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