Tunable laser resonance Raman spectroscopy of the visual process. I: The spectrum of rhodopsin

Tunable laser resonance Raman spectra have been obained of a solution of bovine rhodopsin. The spectra were obtained without causing the cis-trans isomerization of the retinylidene chromophore which is the primary photochemical act in vision. The spectra appear to be sensitive to the structure, the environment and the interactions of the retinylidene chromophore in its opsin matrix. The ease with which the spectra were obtained, the experimental flexibility of Raman spectroscopy and the apparent sensitivity of the spectra suggests a wide range of possible applications for resonance Raman spectroscopy in the elucidation of the principal molecular steps in vision.

[1]  T. Spiro,et al.  Resonance Raman spectra of hemoglobin and cytochrome c: inverse polarization and vibronic scattering. , 1972, Proceedings of the National Academy of Sciences of the United States of America.

[2]  M. Heyde,et al.  Raman spectra of Schiff bases of retinal (models of visual photoreceptors). , 1971, Journal of the American Chemical Society.

[3]  M. Heyde,et al.  Raman spectrum of the 11-cis isomer of retinaldehyde. , 1971, Journal of the American Chemical Society.

[4]  H. Scheraga,et al.  Laser Raman Spectroscopy of Polypeptides. I. Water-Soluble Block Copoymers of L-Alanine and D,L-Lysine , 1971 .

[5]  J. Karle,et al.  Crystal Structure of the Visual Chromophores, 11-cis and all-trans Retinal , 1971, Nature.

[6]  D. Gill,et al.  Raman spectra of dilute solutions of some steroisomers of vitamin A type molecules , 1971 .

[7]  D. Gill,et al.  Resonance-enhanced Raman spectra of visual pigments in intact bovine retinas at low temperatures. , 1970, Biochemical and biophysical research communications.

[8]  N. Yu,et al.  Laser-excited Raman spectroscopy of biomolecules: II. Native ribonuclease and α-chymotrypsin☆☆☆ , 1970 .

[9]  N. Yu,et al.  Laser-excited Raman spectroscopy of biomolecules. I. Native lysozyme and its constituent amino acids. , 1970, Journal of molecular biology.

[10]  D. Bownds.  Site of Attachment of Retinal in Rhodopsin , 1967, Nature.

[11]  J. Behringer.  Observed Resonance Raman Spectra , 1967 .

[12]  E. W. Abrahamson,et al.  Protein configuration changes in the photolysis of rhodopsin. I. The thermal decay of cattle lumirhodopsin in vitro. , 1966, Biochimica et biophysica acta.

[13]  A. C. Albrecht.  On the Theory of Raman Intensities , 1961 .

[14]  A. Kropf,et al.  THE MECHANISM OF BLEACHING RHODOPSIN , 1958, Annals of the New York Academy of Sciences.

[15]  R. A. Morton,et al.  Carotenoids, vitamin A and 7-dehydrosteroid in the frog, Rana temporaria. , 1949, The Biochemical journal.

[16]  F. Collins,et al.  Studies in vitamin A; reactions of retinene1 with amino compounds. , 1949, The Biochemical journal.