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Literature DB >> 2524224

Wavelength regulation in iodopsin, a cone pigment.

J G Chen¹, T Nakamura, T G Ebrey, H Ok, K Konno, F Derguini, K Nakanishi, B Honig.

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.

Entities: Chemical Gene Species

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Year: 1989 PMID： 2524224 PMCID： PMC1330556 DOI： 10.1016/S0006-3495(89)82871-1

Source DB: PubMed Journal: Biophys J ISSN： 0006-3495 Impact factor: 4.033

16 in total

1. The mechanism of bleaching rhodopsin.

Authors: A KROPF; R HUBBARD
Journal: Ann N Y Acad Sci Date: 1959-11-12 Impact factor: 5.691

2. Effect of selected anions and solvents on the electron absorption, nuclear magnetic resonance, and infrared spectra of the N-retinylidene-n-butylammonium cation.

Authors: P E Blatz; J H Mohler
Journal: Biochemistry Date: 1975-06-03 Impact factor: 3.162

10. QM/MM study of dehydro and dihydro β-ionone retinal analogues in squid and bovine rhodopsins: implications for vision in salamander rhodopsin.

Authors: Sivakumar Sekharan; Ahmet Altun; Keiji Morokuma
Journal: J Am Chem Soc Date: 2010-10-21 Impact factor: 15.419

Wavelength regulation in iodopsin, a cone pigment.

1. The mechanism of bleaching rhodopsin.

2. Effect of selected anions and solvents on the electron absorption, nuclear magnetic resonance, and infrared spectra of the N-retinylidene-n-butylammonium cation.

3. Molecular basis of visual excitation.

4. Resonance Raman studies of the conformation of retinal in rhodopsin and isorhodopsin.

5. The structure of bovine rhodopsin.

Review 6. Rhodopsin and bacteriorhodopsin: structure-function relationships.

7. On the mechanism of wavelength regulation in visual pigments.

8. Visual-pigment spectra: implications of the protonation of the retinal Schiff base.

9. Chicken blue and chicken violet, short wavelength sensitive visual pigments.

10. Solid-state 13C NMR detection of a perturbed 6-s-trans chromophore in bacteriorhodopsin.

1. Spectral tuning in salamander visual pigments studied with dihydroretinal chromophores.

2. High-pH form of bovine rhodopsin.

3. Bathoiodopsin, a primary intermediate of iodopsin at physiological temperature.

4. Breaking the covalent bond--a pigment property that contributes to desensitization in cones.

5. Effects of modified chromophores on the spectral sensitivity of salamander, squirrel and macaque cones.

6. Spectral tuning of deep red cone pigments.

Review 7. Synthetic retinals as probes for the binding site and photoreactions in rhodopsins.

8. Probing human red cone opsin activity with retinal analogues.

Review 9. The genetics of normal and defective color vision.

10. QM/MM study of dehydro and dihydro β-ionone retinal analogues in squid and bovine rhodopsins: implications for vision in salamander rhodopsin.