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Wavelength regulation in iodopsin, a cone pigment
Abstract
The opsin shift, the difference in wavenumber between the absorption peak of a visual pigment and the protonated Schiff base of the chromophore, represents the influence of the opsin binding site on the chromophore. The opsin shift for the chicken cone pigment iodopsin is much larger than that for rhodopsin. To understand the origin of this opsin shift and the mechanism of wavelength regulation in iodopsin, a series of synthetic 9-cis and 11-cis dehydro- and dihydro-retinals was used to regenerate iodopsin-based pigments. The opsin shifts of these pigments are quite similar to those found in bacteriorhodopsin-based artificial pigments. On the basis of these studies, a tentative model of wavelength regulation in iodopsin is proposed.
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Binding of the chromophore to opsin red-shifts the chromophore's absorption spectrum.
“binding of the chromophore to opsin red-shifted the chromophore's absorption spectrum”
From The genetics of normal and defective color vision (2011) · cites this paper as Chen, Nakamura, Ebrey, Ok, Konno, Derguini Nakanishi & Honig, 1989
Amino acid sequence differences among the opsins are responsible for the spectral characteristics of each of the cone pigments.
“amino acid sequence differences among the opsins were responsible for the spectral characteristics of each of the cone pigments”
From The genetics of normal and defective color vision (2011) · cites this paper as Chen, Nakamura, Ebrey, Ok, Konno, Derguini Nakanishi & Honig, 1989
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The genetics of normal and defective color vision
Neitz, J., & Neitz, M. (2011) · Vision Research · doi:10.1016/j.visres.2010.12.002 · Cited by 377
Metadata
- Authors
- Chen, J. G., Nakamura, T., Ebrey, T. G., Ok, H., Konno, K., Derguini, F., Nakanishi, K., & Honig, B.
- Venue
- Biophysical Journal
- Publisher
- Elsevier BV
- Published
- 1989-04
- Volume
- 55
- Issue
- 4
- Pages
- 725-729
- ISSN
- 0006-3495
- Cited by
- 19
- References
- 0
- Language
- en
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