title: Wavelength regulation in iodopsin, a cone pigment.
abstract: The opsin shift, the difference in wavenumber between the absorption peak of a visual pigment and the protonated Schiff base of the chromophore, represents the influence of the opsin binding site on the chromophore. The opsin shift for the chicken cone pigment iodopsin is much larger than that for rhodopsin. To understand the origin of this opsin shift and the mechanism of wavelength regulation in iodopsin, a series of synthetic 9-cis and 11-cis dehydro- and dihydro-retinals was used to regenerate iodopsin-based pigments. The opsin shifts of these pigments are quite similar to those found in bacteriorhodopsin-based artificial pigments. On the basis of these studies, a tentative model of wavelength regulation in iodopsin is proposed.
authors.affiliation: University of Illinois, Department of Physiology and Biophysics, Urbana 61801.
authors.forename: J G
authors.initials: JG
authors.lastname: Chen
authors.forename: T
authors.initials: T
authors.lastname: Nakamura
authors.forename: T G
authors.initials: TG
authors.lastname: Ebrey
authors.forename: H
authors.initials: H
authors.lastname: Ok
authors.forename: K
authors.initials: K
authors.lastname: Konno
authors.forename: F
authors.initials: F
authors.lastname: Derguini
authors.forename: K
authors.initials: K
authors.lastname: Nakanishi
authors.forename: B
authors.initials: B
authors.lastname: Honig
mesh_terms: D000818:Animals; D002645:Chickens; D005136:Eye Proteins / Q000502:physiology; D010786:Photoreceptor Cells / Q000502:physiology*; D012168:Retinal Pigments / Q000502:physiology*; D012243:Rhodopsin / Q000502:physiology; D017299:Rod Opsins; D013053:Spectrophotometry; D013329:Structure-Activity Relationship
chemical_list: D005136:Eye Proteins; D012168:Retinal Pigments; D017299:Rod Opsins; C034941:iodopsin; D012243:Rhodopsin