title: Iodopsin, a red-sensitive cone visual pigment in the chicken retina.
abstract: The vertebrate retina contains two kinds of visual cells: rods, responsible for twilight (scotopic) vision (black and white discrimination); and cones, responsible for daylight (photopic) vision (color discrimination). Here we attempt to explain some of their functional differences and similarities in terms of their visual pigments. In the chicken retina there are four types of single cones and a double cone; each of the single cones has its own characteristic oil droplet (red, orange, blue, or colorless) and the double cone is composed of a set of principal and accessory members, the former of which has a green-colored oil droplet. Iodopsin, the chicken red-sensitive cone visual pigment, is located at outer segments of both the red single cones and the double cones, while the other single cones and the rod contain their own visual pigments with different absorption spectra. The diversity in absorption spectra among these visual pigments is caused by the difference in interaction between chromophore (11-cis retinal) and protein moiety (opsin). However, the chromophore-binding pocket in iodopsin is similar to that in rhodopsin. The difference in absorption maxima between both pigments could be explained by the difference in distances between the protonated Schiff-bases at the chromophore-binding site and their counter ions in iodopsin and rhodopsin. Furthermore, iodopsin has a unique chloride-binding site whose chloride ion serves for the red-shift of the absorption maximum of iodopsin. Visual pigment bleaches upon absorption of light through several intermediates and finally dissociates into all-trans retinal and opsin. That the sensitivity of cones is lower than rods cannot be explained by the relative photosensitivity of iodopsin to rhodopsin, but may be understood to some extent by the short lifetime of an enzymatically active intermediate (corresponding to metarhodopsin II) produced in the photobleaching process of iodopsin. The rapid formation and decay of the meta II-intermediate of iodopsin compared with metarhodopsin II are not contradictory to the rapid generation and recovery of cone receptor potential compared with rod receptor potential. The rapid recovery of the cone receptor potential may be due to a more effective shutoff mechanism of the visual excitation, including the phosphorylation of iodopsin. The rapid dark adaptation of cones compared with rods has been explained by the rapid regeneration of iodopsin from 11-cis retinal and opsin. One of the reasons for the rapid regeneration and susceptibility to chemicals of iodopsin compared with rhodopsin may be a unique structure near the chromophore-binding site of iodopsin.
authors.affiliation: Department of Applied Physics and Chemistry, University of Electro-Communications, Tokyo, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Yoshizawa
authors.forename: O
authors.initials: O
authors.lastname: Kuwata
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002645:Chickens; D008969:Molecular Sequence Data; D010786:Photoreceptor Cells / Q000502:physiology*; D011487:Protein Conformation; D012168:Retinal Pigments / Q000737:chemistry / Q000502:physiology*; D012243:Rhodopsin / Q000737:chemistry / Q000502:physiology; D017299:Rod Opsins; D012689:Sequence Homology, Nucleic Acid
chemical_list: D012168:Retinal Pigments; D017299:Rod Opsins; C034941:iodopsin; D012243:Rhodopsin