Fourier transform infrared spectroscopic study on retinochrome and its primary photoproduct, lumiretinochrome.
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.
Sekiya
N
N
Suntory Institute for Bioorganic Research, Osaka, Japan.
Kishigami
A
A
Naoki
H
H
Chang
C W
CW
Yoshihara
K
K
Hara
R
R
Hara
T
T
Tokunaga
F
F
D000818:Animals; D049832:Decapodiformes; D012160:Retina / Q000737:chemistry; D012168:Retinal Pigments / Q000737:chemistry*; D012243:Rhodopsin / Q000031:analogs & derivatives* / Q000737:chemistry; D013055:Spectrophotometry, Infrared
D012168:Retinal Pigments; C018586:lumirhodopsin; C023421:retinochrome; D012243:Rhodopsin