Photochemical and biochemical properties of chicken blue-sensitive cone visual pigment.
Through low-temperature spectroscopy and G-protein (transducin) activating experiments, we have investigated molecular properties of chicken blue, the cone visual pigment present in chicken blue-sensitive cones, and compared them with those of the other cone visual pigments, chicken green and chicken red (iodopsin), and rod visual pigment rhodopsin. Irradiation of chicken blue at -196 degrees C results in formation of a batho intermediate which then converts to BL, lumi, meta I, meta II, and meta III intermediates with the transition temperatures of -160, -110, -40, -20, and -10 degrees C. Batho intermediate exhibits an unique absorption spectrum having vibrational fine structure, suggesting that the chromophore of batho intermediate is in a C6-C7 conformation more restricted than those of chicken blue and its isopigment. As reflected by the difference in maxima of the original pigments, the absorption maxima of batho, BL, and lumi intermediates of chicken blue are located at wavelengths considerably shorter than those of the respective intermediates of chicken green, red and rhodopsin, but the maxima of meta I, meta II, and meta III are similar to those of the other visual pigments. These facts indicate that during the lumi-to-meta I transition, retinal chromophore changes its original position relative to the amino acid residues which regulate the maxima of original pigments through electrostatic interactions. Using time-resolved low-temperature spectroscopy, the decay rates of meta II and meta III intermediates of chicken blue are estimated to be similar to those of chicken red and green, but considerably faster than those of rhodopsin. Efficiency in activating transducin by the irradiated chicken blue is greatly diminished as the time before its addition to the reaction mixture containing transducin and GTP increases, while that by irradiated rhodopsin is not. The time profile is almost identical with those observed in chicken red and green. Thus, the faster decay of enzymatically active state is common in cone visual pigments, independent of their spectral sensitivity.
Imai
H
H
Department of Biophysics, Graduate School of Science, Kyoto University, Kyoto 606-01, Japan.
Terakita
A
A
Tachibanaki
S
S
Imamoto
Y
Y
Yoshizawa
T
T
Shichida
Y
Y
D000818:Animals; D030161:Avian Proteins; D002645:Chickens; D003118:Color Perception; D005136:Eye Proteins / Q000737:chemistry* / Q000378:metabolism* / Q000528:radiation effects; D007700:Kinetics; D008027:Light; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000378:metabolism* / Q000528:radiation effects; D011487:Protein Conformation; D017949:Retinal Cone Photoreceptor Cells / Q000502:physiology*; D017299:Rod Opsins / Q000737:chemistry* / Q000378:metabolism* / Q000528:radiation effects; D013053:Spectrophotometry; D013816:Thermodynamics; D015293:Transducin / Q000378:metabolism
D030161:Avian Proteins; D005136:Eye Proteins; D009419:Nerve Tissue Proteins; D017299:Rod Opsins; D015293:Transducin; C090139:OPNP protein, chicken; C095853:short-wavelength opsin