Time-resolved resonance Raman spectroscopy of intermediates of bacteriorhodopsin: the bK/sub 590/ intermediate

Journal Article · Sun Jul 01 04:00:00 EDT 1979 · Proc. Natl. Acad. Sci. U.S.A.; (United States)

DOI:https://doi.org/10.1073/pnas.76.7.3046· OSTI ID:5367968

Terner, J; Hsieh, C L; Burns, A R; El-Sayed, M A

We have combined microbeam and flow techniques with computer subtraction methods to obtain the resonance Raman spectrum of the short lived batho-intermediate (bK/sub 590/) of bacteriorhodopsin. Comparison of the spectra obtained in /sup 1/H/sub 2/O and /sup 2/H/sub 2/O, as well as the fact that the bK/sub 590/ intermediate shows large optical red shifts, suggests that the Schiff base linkage of this intermediate is protonated. The fingerprint region of the spectrum of bK/sub 590/, sensitive to the isomeric configuration of the retinal chromophore, does not resemble the corresponding region of the parent bR/sub 570/ form. The resonance Raman spectrum of bK/sub 590/ as well as the spectra of all of the other main intermediates in the photoreaction cycle of bacteriorhodopsin are discussed and compared with resonance Raman spectra of published model compounds.

• Research Organization: Univ. of California, Los Angeles
• OSTI ID: 5367968
• Journal Information: Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 76:7; ISSN PNASA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
BIOCHEMICAL REACTION KINETICS
CHEMISTRY
COMPARATIVE EVALUATIONS
KINETICS
METABOLITES
PHOTOCHEMISTRY
PIGMENTS
RAMAN SPECTRA
REACTION KINETICS
SPECTRA