Early photolysis intermediates of the artificial visual pigment 13-demethylrhodopsin.

Nanosecond time-resolved absorption measurements are reported for the room temperature photolysis of a modified rhodopsin pigment, 13-demethylrhodopsin, which contains the chromophore 13-demethylretinal. The measurements are consistent with the formation of an equilibrium between a BA-THO-13-demethylrhodopsin species and a blue-shifted species (relative to the parent pigment), BSI-13-demethylrhodopsin. The results are compared to those acquired after photolysis of native bovine rhodopsin [Hug, S. J., Lewis, J. W., Einterz, C. M., Thorgeirsson, T. E., & Kliger, D. S. (1990) Biochemistry (preceding paper in this issue)] and to results obtained after photolysis of several modified isorhodopsin pigments in which the BSI species was first observed. It is concluded that in all of the pigments the results are consistent with the formation of an equilibrium between BATHO and BSI, which subsequently decays on a nanosecond time scale at room temperature to a lumirhodopsin intermediate.

[1]  D. Kliger,et al.  Transition dipole orientations in the early photolysis intermediates of rhodopsin. , 1989, Biophysical journal.

[2]  M. Sheves,et al.  Photolysis intermediates of the artificial visual pigment cis-5,6-dihydro-isorhodopsin. , 1989, Biophysical journal.

[3]  D. Kliger,et al.  Evidence for a common batho intermediate of rhodopsin and isorhodopsin , 1988 .

[4]  D. Kliger,et al.  Noise reduction in laser photolysis studies of photolabile samples using an optical multichannel analyzer , 1987 .

[5]  D. Kliger,et al.  Spectral and kinetic evidence for the existence of two forms of bathorhodopsin. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[6]  L. P. Murray,et al.  Energy storage in the primary photochemical events of rhodopsin and isorhodopsin. , 1987, Biochemistry.

[7]  K. Nakanishi,et al.  Fourier-transform infrared difference spectroscopy of rhodopsin and its photoproducts at low temperature. , 1985, Biochemistry.

[8]  E. Henry,et al.  Nanosecond optical spectra of iron-cobalt hybrid hemoglobins: geminate recombination, conformational changes, and intersubunit communication. , 1985, Biochemistry.

[9]  R. Leblanc,et al.  ENERGY STORAGE IN THE PRIMARY PHOTOREACTION OF BOVINE RHODOPSIN. A PHOTOACOUSTIC STUDY , 1985, Photochemistry and photobiology.

[10]  J. Horwitz,et al.  NANOSECOND LASER PHOTOLYSIS OF RHODOPSIN AND ISORHODOPSIN , 1983, Photochemistry and photobiology.

[11]  R. Lozier,et al.  Procedure for testing kinetic models of the photocycle of bacteriorhodopsin. , 1982, Biophysical journal.

[12]  R. Mathies,et al.  Assignment and interpretation of hydrogen out-of-plane vibrations in the resonance Raman spectra of rhodopsin and bathorhodopsin. , 1982, Biochemistry.

[13]  E. Dratz,et al.  KINETICS OF RHODOPSIN PHOTOLYSIS INTERMEDIATES IN RETINAL ROD DISK MEMBRANES—I. TEMPERATURE DEPENDENCE OF LUMIRHODOPSIN AND METARHODOPSIN I KINETICS , 1981, Photochemistry and photobiology.

[14]  T. Yoshizawa,et al.  Photochemical reactions of 13-demethyl visual pigment analogues at low temperatures. , 1981, Biochemistry.

[15]  R. Birge,et al.  Photophysics of light transduction in rhodopsin and bacteriorhodopsin. , 1981, Annual review of biophysics and bioengineering.

[16]  T. Yoshizawa,et al.  THE FORMATION OF TWO FORMS OF BATHORHODOPSIN AND THEIR OPTICAL PROPERTIES , 1980, Photochemistry and photobiology.

[17]  R. Mathies,et al.  Interpretation of the resonance Raman spectrum of bathorhodopsin based on visual pigment analogues. , 1980, Biochemistry.

[18]  T. Yoshizawa,et al.  Existence of two forms of bathorhodopsins , 1980, FEBS letters.

[19]  A. Cooper Energy uptake in the first step of visual excitation , 1979, Nature.

[20]  D. Metzler,et al.  Shapes of spectral bands of visual pigments , 1978, Vision Research.

[21]  E. Land,et al.  Nanosecond flash photolysis of rhodopsin , 1975, Nature.

[22]  T. Rosenfeld,et al.  Nanosecond Laser Photolysis of Rhodopsin in Solution , 1972, Nature.

[23]  P. Rentzepis,et al.  Formation and decay of prelumirhodopsin at room temperatures. , 1972, Proceedings of the National Academy of Sciences of the United States of America.

[24]  R. Cone Rotational diffusion of rhodopsin in the visual receptor membrane. , 1972, Nature: New biology.

[25]  A. Kropf,et al.  13-desmethyl rhodopsin and 13-desmethyl isorhodopsin: visual pigment analogues. , 1970, Proceedings of the National Academy of Sciences of the United States of America.