The effects of chloride ion upon chicken visual pigments

Knowles, Aubrey

doi:10.1016/0006-291x(76)90496-4

Cited by 52 publications

(16 citation statements)

References 5 publications

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“…This chloride ionochromic effect has been observed to occur with P-521 in extracts prepared with digitonin, with Triton X-100 and with other detergent solubilizers (Crescitelli, 1977(Crescitelli, a, 1977 as well as with the P-521 in situ within outer segment particles (Crescitelli, 1978). The same responses to chloride have been reported to occur for chicken iodopsin (Knowles, 1976;Fager and Fager, 1977). All these similarities between P-521, a pigment of the so-called gecko rods, and the cone pigment, iodopsin, call to mind the transmutation theory of Walls, 1934), whereby the gecko rods are conceived as visual cells in process of evolutionary transition from ancestral photopic precursors of the diurnal lizard stock that gave rise to geckos.…”

Section: Introductionsupporting

confidence: 61%

The gecko visual pigments. The behavior of opsin.

Crescitelli¹

1979

The Journal of General Physiology

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A B S T R A C T The 521-pigment extracted out of the retina of the Tokay gecko has the typical stereospecificity of the vertebrate visual pigments. This is true for the pigment in the chloride-depleted, "blue-shifted" state as well as for the normal pigment with added chloride. While in the chloride-deficient state, pigment regeneration occurred with both l l-cis-and 9-cis-retinals and the regenerated photopigments were also in the blue-shifted, chloride-depleted state. As with the native pigment, these regenerated pigments were bathochromically shifted to their normal positions by the addition of chloride. Chloride-deficient opsin by itself also responded to chloride for the pigment regenerated with l l-cis-retinal from such chloride-treated opsin was in the normal 521-position. Regeneration was always rapid, reaching completion in <5 min, and was significantly faster than for cow rhodopsin regenerating under the same conditions. This rapid rate was found with or without chloride, with both ll-cis-and 9-cis-retinals and in the presence of the sulfhydryl poison, p-hydroxymercuribenzoate (PMB). Like the native chloridedeficient pigment, the regenerated chloride-depleted photopigments responded to PMB by a blue shift beyond the position of the chloride-deficient state. The addition of chloride to these "poisoned" regenerated pigments caused a bathochromic shift of such magnitude as to indicate a repair of both the PMB and chloride-deficient blue shift. In this discussion the possible implications of these results to phylogenetic considerations are considered as well as to some molecular properties of the 521-pigment.

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Section: Introductionsupporting

confidence: 61%

The gecko visual pigments. The behavior of opsin.

Crescitelli¹

1979

The Journal of General Physiology

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“…The difference between the two is about 3 nm and is similar to that found for frog rhodopsin (Bowmaker, 1973;Bowmaker et at. 1975 (Knowles, 1976) and in the rod outer segment (Bowmaker & Knowles, 1977). The shift found for primate rhodopsin is difficult to assess, owing to the low signal-to-noise ratios in MSP studies and to the possible interference by photoproducts, cone pigments and isorhodopsin in measurements of extracts; but prima face the MSP measurements are the most appropriate for psychophysical comparisons.…”

Section: Resultsmentioning

confidence: 99%

The visual pigments of rods and cones in the rhesus monkey, Macaca mulatta.

Bowmaker¹,

Dartnall²,

Lythgoe³

et al. 1978

The Journal of Physiology

109

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SUMMARY1. New microspectrophotometric measurements have been made of the photopigments of individual rods and cones from the retina of the rhesus monkey (Macaca mulatta). The measuring beam was passed transversely through isolated outer segments.2. The transverse absorbance for rods ranged from 0-02 to 0'04 and that for cones from 0.01 to 0'03.3. The mean absorbance spectrum for rods (n = 25) had a peak at 502 + 2*7 nm. A digitonin extract from the same group of eyes gave a Amax. of 499 + 1 nm.4. Of a sample of 82 cones, 40 were 'red' (P565 nm) and 42 were 'green' (P536 nm). The mean absorbance spectrum for the green cones is very similar to the Dartnall nomogram, but that for the red cones is narrower.5. No bleachable, blue-sensitive outer segments were recorded, although structures were found that absorbed at short wave-lengths and were neither photosensitive nor dichroic. 6. If the long wave-length and middle wave-length cone pigments of the rhesus monkey are assumed to be identical to those of man and if additional assumptions are made about the lengths of human outer segments and about prereceptoral absorption, it is possible to derive psychophysical sensitivities that closely resemble the 7rT and i4 mechanisms of W. S. Stiles.

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“…). In the right panels, spectral changes are shown by subtracting the absorption spectrum immediately after irradiation (curve 2) from the subsequent spectra (curves [3][4][5][6][7][8][9][10][11][12][13].…”

Section: Resultsmentioning

confidence: 99%

“…Iodopsin and the other L-group pigments bind to chloride, which causes a spectral redshift (10)(11)(12)(13)(14). The chloride-binding site is proposed to be the conserved His and Lys residues located in the second extracellular loop (14), likely to be proximate to the chromophore considered from the crystal structure of bovine rhodopsin (15).…”

Section: Introductionmentioning

confidence: 99%

Thermal Recovery of Iodopsin from Photobleaching Intermediates^†

Imamoto¹,

Shichida

2008

Photochem & Photobiology

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The chloride effect on the photobleaching process of iodopsin, a chicken red-sensitive cone visual pigment, was studied in detail by time-resolved low-temperature spectroscopy at -40 degrees C to -10 degrees C. Decay-associated difference spectra obtained by kinetic analysis using the singular value decomposition method were composed of spectra of BL-iodopsin, lumiiodopsin, metaiodopsin I, metaiodopsin II and metaiodopsin III, essentially identical to those at room temperature. In each conversion step however, iodopsin was partially regenerated, which is not observed in the bleaching process for other visual pigments or iodopsin at room temperature. Moreover, iodopsin was slowly regenerated from the bleached species. The reverse reactions were completely suppressed by substitution of lyotropic NO(3)(-) for Cl(-), suggesting that Cl(-) binding to iodopsin interferes with light-induced cis-trans isomerization of the chromophore. It is likely that the water molecule hydrating Cl(-) forms the additional hydrogen bond(s), by which the protein conformational change necessary to release this steric hindrance becomes enthalpic. As progress of the bleaching process is a consequence of protein conformational change, it is suppressed at low temperatures, resulting in thermal back-isomerization.

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The effects of chloride ion upon chicken visual pigments

Cited by 52 publications

References 5 publications

The gecko visual pigments. The behavior of opsin.

The gecko visual pigments. The behavior of opsin.

The visual pigments of rods and cones in the rhesus monkey, Macaca mulatta.

Thermal Recovery of Iodopsin from Photobleaching Intermediates^†

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The effects of chloride ion upon chicken visual pigments

Cited by 52 publications

References 5 publications

The gecko visual pigments. The behavior of opsin.

The gecko visual pigments. The behavior of opsin.

The visual pigments of rods and cones in the rhesus monkey, Macaca mulatta.

Thermal Recovery of Iodopsin from Photobleaching Intermediates†

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Thermal Recovery of Iodopsin from Photobleaching Intermediates^†