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Time-resolved resonance Raman characterization of the bL/sub 550/ intermediate and the two dark-adapted bR/sub 560//sup DA/ forms of bacteriorhodopsin

Journal Article · · Biophys. J.; (United States)
The resonance Raman spectrum of the second intermediate in the bacteriorhodopsin cycle, bL/sub 550/, is obtained by a simple flow technique. The Schiff base linkage in this intermediate appears to be protonated, contrary to previous suggestion. The fingerprint region of the spectrum of bL/sub 550/ does not closely match those of any presently available model Schiff bases of retinal isomers, though some comparisons can be made. The resonance Raman spectrum of dark-adapted bacteriorhodopsin is obtained and decomposed by computer subtraction of the spectrum of bR/sub 570/. The remaining spectrum does not match the spectra of any model compounds presently in the literature. The spectra of bL/sub 550/ and dark-adapted bR/sub 560//sup DA/ from purple membrane in H/sub 2/O are compared to those in D/sub 2/O. It is found that changes in the spectrum occur in the 1,600--1,650 cm/sup -1/ region as well as in the 800--1,000 cm/sup -1/ region, but apparently not in the fingerprint region (1,100--1,400 cm/sup -1/). The possibilities of conformational changes of the retinal chromophore in the light adaptation process as well as the photosynthetic cycle are discussed.
Research Organization:
Univ. of California, Los Angeles
OSTI ID:
6189466
Journal Information:
Biophys. J.; (United States), Journal Name: Biophys. J.; (United States) Vol. 26:3; ISSN BIOJA
Country of Publication:
United States
Language:
English