title: Spectral tuning in salamander visual pigments studied with dihydroretinal chromophores.
abstract: In visual pigments, opsin proteins regulate the spectral absorption of a retinal chromophore by mechanisms that change the energy level of the excited electronic state relative to the ground state. We have studied these mechanisms by using photocurrent recording to measure the spectral sensitivities of individual red rods and red (long-wavelength-sensitive) and blue (short-wavelength-sensitive) cones of salamander before and after replacing the native 3-dehydro 11-cis retinal chromophore with retinal analogs: 11-cis retinal, 3-dehydro 9-cis retinal, 9-cis retinal, and 5,6-dihydro 9-cis retinal. The protonated Schiff's bases of analogs with unsaturated bonds in the ring had broader spectra than the same chromophores bound to opsins. Saturation of the bonds in the ring reduced the spectral bandwidths of the protonated Schiff's bases and the opsin-bound chromophores and made them similar to each other. This indicates that torsion of the ring produces spectral broadening and that torsion is limited by opsin. Saturating the 5,6 double bond in retinal reduced the perturbation of the chromophore by opsin in red and in blue cones but not in red rods. Thus an interaction between opsin and the chromophoric ring shifts the spectral maxima of the red and blue cone pigments, but not that of the red rod pigment.
authors.affiliation: Department of Ophthalmology, Harvard Medical School, and the Massachusetts Eye and Ear Infirmary, Boston, Massachusetts 02114, USA. cmakino@meei.harvard.edu
authors.forename: C L
authors.initials: CL
authors.lastname: Makino
authors.forename: M
authors.initials: M
authors.lastname: Groesbeek
authors.forename: J
authors.initials: J
authors.lastname: Lugtenburg
authors.forename: D A
authors.initials: DA
authors.lastname: Baylor
mesh_terms: D000557:Ambystoma; D000818:Animals; D055592:Biophysical Phenomena; D001703:Biophysics; D004224:Diterpenes; D066298:In Vitro Techniques; D008968:Molecular Conformation; D010777:Photochemistry; D017949:Retinal Cone Photoreceptor Cells / Q000737:chemistry / Q000528:radiation effects; D012168:Retinal Pigments / Q000737:chemistry* / Q000528:radiation effects*; D017948:Retinal Rod Photoreceptor Cells / Q000737:chemistry / Q000528:radiation effects; D012172:Retinaldehyde / Q000031:analogs & derivatives* / Q000737:chemistry / Q000528:radiation effects; D017299:Rod Opsins / Q000737:chemistry / Q000528:radiation effects; D013053:Spectrophotometry
chemical_list: D004224:Diterpenes; D012168:Retinal Pigments; D017299:Rod Opsins; C028852:5,6-dihydroretinal; D012172:Retinaldehyde