19F NMR spectra of 11-cis and 9-cis
isomers of six fluorinated rhodopsin analogs with the label(s)
located at
the vinylic positions of the polyene chain (8-F, 10-F, 12-F, 14-F,
8,12-F2, 10,14-F2) are reported along
with
their UV−vis and CD spectra. The regiospecific F chemical shift
data are analyzed in terms of chromophore
changes and local perturbation resulting from specific interactions
with protein. Two analogs (11-cis-12-F
and 11-cis-8-F) and also 9,11-di-cis-12-F
possess FOS (fluorine opsin shift) values uniquely different
from
others. Ab initio F NMR chemical shielding calculations
of model structures provide support that a strong
protein perturbation to the 12-F position prevails in the binding
cavity and that F-8 shift is sensitive to variation
of the nearby dihedral angle(s). Possible causes for the
broad line width of the F signals of these membrane
proteins are discussed.