• Journal of Photoscience
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• 제9권2호
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• pp.264-266
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• 2002

The absorption wavelength of the protonated retinal Schiff base can be controlled by the surrounding environment. An external anion is related to fine adjustment of the absorption wavelength. The addition of anion to retinochrome solution caused blue shift in spectra. The increase of the shift was dependent on the ion concentration. The large shift value was obtained as 20 nm at the saturated concentration of nitrate. The shift intensity for the nitrate addition exceeded that of chloride. Seemingly, it depends on the ionic strength or lyotropic character of the anion. However, neither of sulphate nor gluconate ion showed remarkable blue shift. These phenomena were accounted for with (1) delocalization of the positive charge in the conjugated polyene system, (2) ionic bonding strength between the counter ion (glutamate) and the proton, and/or (3) interaction of the added anion with the proton on Schiff base.

• Journal of Photoscience
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• 제9권2호
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• pp.33-36
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• 2002

In vertebrate rhodopsins the glutamic acid at position 113 serves as a counterion to stabilize the protonated retinylidene Schiff base linkage and to shift the spectrum to the visible region. Invertebrate rhodopsins and retinochrome have the amino acid residue different from glutamic acid or asparatic acid at this position and therefore, these pigments may have a counterion at different position. We first investigated the counterion in retinochrome by site specific mutagenesis. The results showed that the counterion is the glutamic acid at position 181, where almost of all the pigments including vertebrate and invertebrate rhodopsins in the rhodopsin family have a glutamic acid or an aspartic acid. In vertebrate rhodopsins, however, Glu 181 does not act as a counterion, and the red-sensitive cone pigments have a histidine at this position, which serves as a chloride-binding site for red-shift of the absorption spectrum. These findings suggested that the role of Glu181 as a counterion may be weakened by the newly acquired counterion at position 113. Taken together with our recent studies on an invertebrate-type rhodopsin, the rhodopsin diversity was discussed from viewpoint of counterion.

• Journal of Photoscience
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• 제9권2호
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• pp.37-40
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• 2002

Ascidians are lower chordates, and their tadpole-like larvae share a basic body plan with vertebrates. To study photoreceptive systems in ascidians, we have isolated and characterized cDNA clones for three opsins, five G protein ${\alpha}$ subunits (G${\alpha}$), catalytic and regulatory subunits of cGMP phosphodiesterase (PDE), and arrestin from the ascidian Ciona intestinalis tadpole larva. Ci-opsin1 and Ci-opsin2 are vertebrate-type opsins, while Ci-opsin3 is a retinal photoisomerase similar to retinochrome and mammalian RGR. Both Ci-opsin1 and arrestin are specifically localized in the photoreceptor cells of the ocellus, whereas Ci -opsin2 is not expressed in the photoreceptors, but is co-localized in another population of neurons in the brain with PDE (Ci-PDE9 and Ci-PDE$\delta$). Ci-opsin3 is present in the entire region of the brain. Though five different cDNAs encoding Ga have been cloned, no transducin-type G protein has been found yet. Interestingly, one of G${\alpha}$i isoform is conspicuously expressed in the entire region of the brain. The Ci-opsin3 gene expression was observed in a broad area of the brain vesicle as well as in the visceral ganglion. Genes encoding ascidian homologs of CRALBP and ${\beta}$-CD, whose function is required for the mammalian visual cycle, are co-expressed with Ci-opsin3 in the brain vesicle and visceral ganglion. Localization of Ci-opsin3, CRALBP, and ${\beta}$-CD in a broad area of the brain suggests that the brain of the ascidian larva has a visual cycle system similar to that of the vertebrate RPE. Based on these data, we discuss the evolution of vertebrate visual systems.