Pre-Lumirhodopsin and the Bleaching of Visual Pigments

@article{Yoshizawa1963PreLumirhodopsinAT,
  title={Pre-Lumirhodopsin and the Bleaching of Visual Pigments},
  author={Toru Yoshizawa and George Wald},
  journal={Nature},
  year={1963},
  volume={197},
  pages={1279-1286}
}
Constraints of Opsin Structure on the Ligand-binding Site: Studies with Ring-fused Retinals¶
Abstract Ring-fused retinal analogs were designed to examine the hula-twist mode of the photoisomerization of the 9-cis retinylidene chromophore. Two 9-cis retinal analogs, the C11–C13 five-memberedExpand
Constraints of Opsin Structure on the Ligand‐binding Site: Studies with Ring‐fused Retinals ¶
TLDR
Ring‐fused retinal analogs designed to examine the hula‐twist mode of the photoisomerization of the 9‐cis retinylidene chromophore suggested that the analogs do not form pigments in the retinal‐binding site of rhodopsin but form Pigments with opsin structures, which have larger binding space generated by the movement of transmembrane helices. Expand
Photoreversal of Rhodopsin Bleaching
  • T. Williams
  • Chemistry, Medicine
  • The Journal of general physiology
  • 1964
TLDR
The relevance of these results to other experiments is pointed out and emphasis is placed on the explanation of observed quantum efficiencies which obtain at both low and high intensities. Expand
Characteristics of the Photoconversion of Rhodopsin in the Early Stages of Photolysis
TLDR
Low-temperature spectrophotometry was used to study the primary stages of rhodopsin photolysis and formation of an intermediate product spectrally similar to the known “blue-shifted intermediate” (BSI) was demonstrated. Expand
Electrostatic Control of Photoisomerization in Channelrhodopsin 2.
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This work combines ab initio nonadiabatic dynamics simulation, excited state free energy calculation, and reaction path search to comprehensively characterize the RPSB photoisomerization mechanism in the E123T mutant of ChR2, a useful optogenetic tool when fast neuronal stimulation is needed. Expand
Functional Integrity of Membrane Protein Rhodopsin Solubilized by Styrene-Maleic Acid Copolymer.
TLDR
The results confirm that SMA is a useful tool for membrane protein research, but SMA added in excess can interfere with the dynamics of protein activation. Expand
Nonequilibrium thermodynamics of light-induced reactions.
TLDR
This work uses a thermodynamic coarse-graining procedure and a local equilibrium assumption to derive the chemical potential of photons relative to the system they interact with, and uses this framework to treat two paradigmatic photochemical mechanisms describing light-induced unimolecular reactions and highlight the different thermodynamics they lead to. Expand
Photoisomerization-coupled electron transfer.
TLDR
This work proposes a theoretical model for an ultrafast electron transfer triggered by a simultaneous photoisomerization of the donor or the acceptor moiety and applies it to the case of a dihydropyrene-type photochromic molecular donor. Expand
Unique retinal binding pocket of primate blue-sensitive visual pigment
TLDR
Mutation of the blue-specific tyrosine at position 265 into tryptophan, which is highly conserved in other animal rhodopsins, led to formation of the 9-cis form in monkey blue, suggesting that Y265 is one of the determinants of the unique photochemistry in blue pigments. Expand
Electrophysiological Changes During Early Steps of Retinitis Pigmentosa.
TLDR
The results indicate that in P23H rods light-induced degeneration occurs in at least two stages, the first involving impairment of phototransduction and the second involving initiation of morphologic changes. Expand
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References

SHOWING 1-10 OF 17 REFERENCES
On the labile intermediate of rhodopsin as demonstrated by low temperature illumination.
TLDR
The trend was that, after exposure of the samples to lights of different wavelengths, the shorter the wavelength was, the more the absorptions decreased, and the solution illuminated at low temperature was a photochemical steady-state mixture composed of rhodopin, iso-rhodopsin and the labile fraction, which is thermolabile at lowTemperature. Expand
Studies on the metastable states in the rhodopsin cycle.
TLDR
The photochemical properties of the labile fraction of lumi- or meta-rhodopsin and the essential of the “liquid air illuminated rhodopin” are discussed. Expand
Spectra of sodium and potassium azide crystals coloured by ultra-violet and X -ray radiation
  • J. Cunningham, F. Tompkins
  • Chemistry
  • Proceedings of the Royal Society of London. Series A. Mathematical and Physical Sciences
  • 1959
The spectra of sodium and potassium azide crystals that had been coloured by irradiation with both ultra-violet and X-ray radiation for varying periods at liquid-nitrogen temperature have beenExpand
Bleaching of Rhodopsin by Light and by Heat
TLDR
This work finds that light and heat bleach rhodopsin by different mechanisms, yielding different products. Expand
Chemistry of the Rhodopsin Cycle
TLDR
It is believed that the rhodopsin remaining unbleached after low-temperature illumination should not be regarded as having been regenerated from retinene and opsin, but could be recovered directly from lumi-rhodopin. Expand
THE ACTION OF LIGHT ON RHODOPSIN.
  • R. Hubbard, A. Kropf
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1958
TLDR
Rhodopsin, a red visual pigment of vertebrate rods, is composed of the yellow carotenoid derivative, retinene, joined to the colorless protein, opsin, which bleaches in the light to a mixture of opsin and all-trans retinenes and opsIn, and the chromophore of squid rhodops in, has the neo-b (1 -cis) configuration. Expand
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