Abstract
By comparing the shift of the absorption maxima when a visual pigment is converted to its lumirhodopsin photointermediate for two classes of pigments, we can infer whether or not the pigment's beta-ionone ring has left its binding site. We compare this shift for the long-wavelength sensitive visual pigment of chicken iodopsin (lambdamax = 571 nm), which has polar residues in the ring binding site that interact with the ring, with that for three pigments, which do not. We conclude that by the time the Lumi product of the pigment is formed, the ring has moved away from the ring binding site.
MeSH Terms
Animals
Binding Sites
Biophysical Phenomena
Biophysics
Chickens
Humans
In Vitro Techniques
Molecular Structure
Photochemistry
Rhodopsin/chemistry,radiation effects
Rod Opsins/chemistry,radiation effects
Spectrophotometry
Chemicals
Rod Opsins
iodopsin
Rhodopsin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Ebrey Thomas G
Department of Biology, University of Washington, Seattle, 98195, USA.
Kumauchi Masato
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