Abstract:
:Magic angle sample spinning (MASS) 13C NMR spectra have been obtained of bovine rhodopsin regenerated with retinal prosthetic groups isotopically enriched with 13C at C-5 and C-14. In order to observe the 13C retinal chromophore resonances, it was necessary to employ low temperatures (-15-----35 degrees C) to restrict rotational diffusion of the protein. The isotropic chemical shift and principal values of the chemical shift tensor of the 13C-5 label indicate that the retinal chromophore is in the twisted 6-s-cis conformation in rhodopsin, in contrast to the planar 6-s-trans conformation found in bacteriorhodopsin. The 13C-14 isotropic shift and shift tensor principal values show that the Schiff base C = N bond is anti. Furthermore, the 13C-14 chemical shift (121.2 ppm) is within the range of values (120-123 ppm) exhibited by protonated (C = N anti) Schiff base model compounds, indicating that the C = N linkage is protonated. Our results are discussed with regard to the mechanism of wavelength regulation in rhodopsin.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Smith SO,Palings I,Copié V,Raleigh DP,Courtin J,Pardoen JA,Lugtenburg J,Mathies RA,Griffin RGdoi
10.1021/bi00380a018subject
Has Abstractpub_date
1987-03-24 00:00:00pages
1606-11issue
6eissn
0006-2960issn
1520-4995journal_volume
26pub_type
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