Solid-state NMR studies of mechanism of the opsin shift in the visual pigment rhodopsin
| Autor: | J. Lugtenburg, M. E. Miley, Robert G. Griffin, I. Palings, H. J. M. de Groot, S. O. Smith, J. M. L. Courtin, Richard A. Mathies |
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| Jazyk: | angličtina |
| Rok vydání: | 1990 |
| Předmět: |
Rhodopsin
Opsin Magnetic Resonance Spectroscopy Molecular Structure biology Protein Conformation Chemical shift Analytical chemistry Retinal Protonation Carbon-13 NMR Polyene Biochemistry chemistry.chemical_compound Crystallography chemistry Solid-state nuclear magnetic resonance biology.protein Animals Cattle sense organs Schiff Bases |
| Zdroj: | Biochemistry, 29(35), 8158-8164. AMER CHEMICAL SOC |
| Popis: | Solid-state 13C NMR spectra have been obtained of bovine rhodopsin and isorhodopsin regenerated with retinal selectively 13C labeled along the polyene chain. In rhodopsin, the chemical shifts for 13C-5, 13C-6, 13C-7, 13C-14, and 13C-15 correspond closely to the chemical shifts observed in the 11-cis protonated Schiff base (PSB) model compound. Differences in chemical shift relative to the 11-cis PSB chloride salt are observed for positions 8 through 13, with the largest deshielding (6.2 ppm) localized at position 13. The localized deshielding at C-13 supports previous models of the opsin shift in rhodopsin that place a protein perturbation in the vicinity of position 13. Spectra obtained of isorhodopsin regenerated with 13C-labeled 9-cis-retinals reveal large perturbations at 13C-7 and 13C-13. The similar deshielding of the 13C-13 resonance in both pigments supports the presence of a protein perturbation near position 13. However, the chemical shifts at positions 7 and 12 in isorhodopsin are not analogous to those observed in rhodopsin and suggest that the binding site interactions near these positions are different for the two pigments. The implications of these results for the mechanism of the opsin shift in these proteins are discussed. |
| Databáze: | OpenAIRE |
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