Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Low-temperature solid-state /sup 13/C NMR studies of the retinal chromophore in rhodopsin

Journal Article · · Biochemistry; (United States)
OSTI ID:6469727

Magic angle sample spinning (MASS) /sup 13/C NMR spectra have been obtained of bovine rhodopsin regenerated with retinal prosthetic groups isotopically enriched with /sup 13/C at C-5 and C-14. In order to observe the /sup 13/C retinal chromophore resonances, it was necessary to employ low temperatures (-15 ..-->.. -35/sup 0/C) to restrict rotational diffusion of the protein. The isotropic chemical shift and principal values of the chemical shift tensor of the /sup 13/C-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 confirmation found in bacteriorhodopsin. The /sup 13/C-14 isotropic shift and shift tensor principal values show that the Schiff base C=N bond is anti. Furthermore, the /sup 13/C-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. The results are discussed with regard to the mechanism of wavelength regulation in rhodopsin.

Research Organization:
Massachusetts Institute of Technology, Cambridge
OSTI ID:
6469727
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 26:6; ISSN BICHA
Country of Publication:
United States
Language:
English