A charge transfer process in the visual pigments View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1967-12

AUTHORS

Ignacio G. Galindo

ABSTRACT

A physical model that incorporates all the experimental information on the formation of the visual pigment rhodopsin is presented. The visual pigments consist of a chromophore bound to an appropriate protein. Thus rhodopsin (λm 505 mμ) is formed by a Schiff’s base linkage C19H27CH=NH+-opsin (λm 440 mμ) between 11-cis retinal (λm 380 mμ) and the protein opsin (λm 280 mμ). It is found that there exists a red shift in the spectrum of rhodopsin from the Schiff’s base. The model brings an explanation for this red shift. It is shown that such a shift may be due to a charge transfer process (R. S. Mulliken,J. Am. Chem. Soc.,74, 811–824, 1952) between an electron at the double bond of carbons C11−C12 and an atomic orbital of the sulphur present in cysteine. This provides an explanation of the presence of SH-groups in the protein after the absorption of light. A one-electron approximation is used and the dipole momentμNV; hence, the oscillator strengthf of the transitionNV is estimated and compared with the experimentally determined extinction coefficient ∈m by mixing 3.5×10−3 M of 11-cis retinal with 8.3×10−5 M of cysteine at pH ranges 6 through 8. Reasonable agreement is found. Solvent, concentration and temperature dependence are shown also. More... »

PAGES

677-690

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf02476919

DOI

http://dx.doi.org/10.1007/bf02476919

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1044096141

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/5582147


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