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Y Shichida

Publications and source records attributed to Y Shichida.

97 records · Page 6Linked to original sources
PubMed1981

Photochemical reactions of 13-demethyl visual pigment analogues at low temperatures.

The photobleaching reaction of 13-demethylisorhodopsin (hereafter designated as 9-cis- 13-dm-rhodopsin), which was synthesized from 9-cis- 13-demethylretinal and cattle opsin, was investigated by low-temperature spectrophotometry in order to elucidate the role of the 13-methyl group of retinal in photobleaching. When 9-cis- 13-dm-rhodopsin was irradiated at-190 degrees C, batho-13-dm-rhodopsin was produced. Its absorption maximum lay at 532 nm, 11 nm shorter than that of cattle bathorhodopsin (gamma max 543 nm), and batho-13-dm-rhodopsin had an extinction coefficient about 0.6 times that of bathorhodopsin. Batho-13-dm-rhodopsin was thermally unstable. Above-180 degrees C, it converted to a new intermediate, BL-13-dm-rhodopsin, which in turn changed to lumi-13-dm-rhodopsin- above -140 degrees C. BL-13-dm-rhodopsin was "photosensitive" at temperatures around -188 degrees C, though batho-13-dm-rhodopsin and lumi-13-dm-rhodopsin was "photosensitive" at the same temperature. In the photobleaching process, lumi-13-dm-rhodopsin and meta-I-13-dm-rhodopsin were observed. Their thermostabilities were very similar to those of lumirhodopsin and metarhodopsin I, but each dm intermediate differed from its methylated counterpart in its value of gamma max and extinction coefficient.

Animals↗
PubMed1979

Formation of 7-cis- and 13-cis-retinal pigments by irradiating squid rhodopsin.

Squid rhodopsin was irradiated with orange light (greater than 530 nm) at various temperatures from -190 to 10 degrees C until a photo-steady-state mixture was formed. Then the chromophoric retinals were extracted from the photo-steady-state mixtures and their isomer composition was analyzed by high-performance liquid chromatography. In the case of photo-steady-state mixture formed at -85 degrees C, large peaks in the chromatogram were found at the positions of both 7-cis- and 13-cis-retinals. Each peak was further identified by synthesizing the pigments from these retinals with cattle opsin or apobacteriorhodopsin. Both 7-cis- and 13-cis-retinals were also extracted from a photo-steady-state mixture formed by irradiation at -40, at 0, or at 10 degrees C. These isomers were scarcely detected in a photo-steady-state mixture formed by irradiation at -190 degrees C, though 9-cis-retinal was found as a major constituent in this mixture. Irradiation of lumirhodopsin at -190 degrees C, however, produced 7-cis-retinal pigment. These findings suggest that bathorhodopsin may have a conformation to prevent the formation of 7-cis-retinal from the all-trans form and that this particular conformation may be relaxed by the conversion of bathorhodopsin to lumirhodopsin.

Animals↗
PubMed1978

Circular dichroism of squid rhodopsin and its intermediates.

Circular dichroism (CD) and absorption spectra of squid (Todarodes pacificus) rhodopsin, isorhodopsin and the intermediates was measured at low temperatures. Squid rhodopsin has positive CD bands at wavelengths corresponding the alpha- and beta-absorption bands at liquid nitrogen temperature (CD maxima: 485 nm at alpha-band and 348 nm at beta-band) as well as at room temperature (CD maxima: 474 nm at alpha-band and 347 nm at beta-band). The rotational strength of the alpha-band has a molecular ellipticity about twice that of cattle rhodopsin. The CD spectrum of bathorhodopsin displays a negative peak at 532 nm, the rotational strength of which has an absolute value slightly larger than that of rhodopsin. The reversal in sign at alpha-band of the CD spectrum may indicate that the isomerization of retinal chromophore from twisted 11-cis form to twisted 11-trans form has occurred in the process of conversion from rhodopsin to bathorhodopsin. Lumirhodopsin has a small negative CD band at 490 nm, the maximum of which lies at 25 nm shorter wavelengths than the absorption maximum (515 nm), and a large positive CD band near 290 nm, which is not observed in rhodopsin and the other intermediates. This band may de derived from a conformational change of the opsin. In the process of changing from lumirhodopsin to LM-rhodopsin, The CD bands at visible and near ultraviolet regions disappear. Both alkaline and acid metarhodopsins have no CD bands at visible and near ultraviolet regions.

Animals↗