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PMID: 15778447 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, U.S. Gov't, P.H.S.

Does the chromophore's ring move after photoexcitation of rhodopsin?

Biophysical journal ·Vol. 88 ·No. 6 ·2005-06-00 ·Pages L41-2

Ebrey TG, Kumauchi M

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
References (11)
11 references, click to expand
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Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
Published
2005-06-00
Epub
2005-00-18
Pages
L41-2
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1305671
Subset
IM
Grants
NEI NIH HHS · EY01323 · United States
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