Studies on cephalopod rhodopsin conformational changes in chromophore and protein during the photoregeneration process.
The ultraviolet absorbance of squid and octopus rhodopsin changes reversibly at 234 nm and near 280 nm in the interconversion of rhodopsin and metarhodopsin. The absorbance change near 280 nm is ascribed to both protein and chromophore parts. Rhodopsin is photoregenerated from metarhodopsin via an intermediate, P380, on irradiation with yellow light (lamda >520 nm). The ultraviolet absorbance decreases in the change from rhodopsin to metarhodopsin and recovers in two steps; mostly in the process from metarhodopsin to P380 and to a lesser extent in the process from P380 to rhodopsin. P380 has a circular dichroism (CD) band at 380 nm and its magnitude is the same order as that of rhodopsin. Thus it is considered that the molecular structure of P380 is close to that of rhodopsin and that the chromophore is fixed to opsin as in rhodopsin. In the change from metarhodopsin to P380, the chromophore is isomerized from the all-trans to the 11-cis form, and the conformation of opsin changes to fit 11-cis retinal. In the change from P380 to rhodopsin, a small change in the conformation of the protein part and the protonation of the Schiff base, the primary retinal-opsin link, occur.
Suzuki
T
T
Department of Biology, Faculty of Science, Osaka University, Toyonaka, Osaka, Japan.
Sugahara
M
M
Azuma
K
K
Azuma
M
M
Saimi
Y
Y
Kito
Y
Y
D000818:Animals; D049830:Cephalopoda / Q000378:metabolism*; D002942:Circular Dichroism; D008027:Light; D011487:Protein Conformation; D012172:Retinaldehyde / Q000378:metabolism*; D012243:Rhodopsin / Q000737:chemistry*; D014466:Ultraviolet Rays
D012243:Rhodopsin; D012172:Retinaldehyde