title: Fourier transform infrared spectroscopic study on retinochrome and its primary photoproduct, lumiretinochrome.
abstract: Structural studies of retinochrome, and its photoproduct, lumiretinochrome, were done by Fourier transform infrared difference spectroscopy. The absorption bands in the carbonyl stretching region which shift in D2O show the changes in the protein part during the photoreaction. Strong absorption bands in the finger-print region show that the all-trans-retinal chromophore in retinochrome isomerizes to the 11-cis-retinal chromophore in lumiretinochrome upon illumination with yellow-green light at 83K.
authors.affiliation: Suntory Institute for Bioorganic Research, Osaka, Japan.
authors.forename: N
authors.initials: N
authors.lastname: Sekiya
authors.forename: A
authors.initials: A
authors.lastname: Kishigami
authors.forename: H
authors.initials: H
authors.lastname: Naoki
authors.forename: C W
authors.initials: CW
authors.lastname: Chang
authors.forename: K
authors.initials: K
authors.lastname: Yoshihara
authors.forename: R
authors.initials: R
authors.lastname: Hara
authors.forename: T
authors.initials: T
authors.lastname: Hara
authors.forename: F
authors.initials: F
authors.lastname: Tokunaga
mesh_terms: D000818:Animals; D049832:Decapodiformes; D012160:Retina / Q000737:chemistry; D012168:Retinal Pigments / Q000737:chemistry*; D012243:Rhodopsin / Q000031:analogs & derivatives* / Q000737:chemistry; D013055:Spectrophotometry, Infrared
chemical_list: D012168:Retinal Pigments; C018586:lumirhodopsin; C023421:retinochrome; D012243:Rhodopsin