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PMID: 16592669 Published · ppublish English Journal Article

Time-resolved resonance Raman spectroscopy of intermediates of bacteriorhodopsin: The bK(590) intermediate.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 76 ·No. 7 ·1979-07-00 ·Pages 3046-50

Terner J, Hsieh CL, Burns AR, El-Sayed MA

Abstract

We have combined microbeam and flow techniques with computer subtraction methods to obtain the resonance Raman spectrum of the short lived batho-intermediate (bK(590)) of bacteriorhodopsin. Comparison of the spectra obtained in (1)H(2)O and (2)H(2)O, as well as the fact that the bK(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(590), sensitive to the isomeric configuration of the retinal chromophore, does not resemble the corresponding region of the parent bR(570) form. The resonance Raman spectrum of bK(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.

Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Terner J
Department of Chemistry, University of California, Los Angeles, California 90024.
Hsieh C L
Burns A R
El-Sayed M A
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.76.7.3046
Published
1979-07-00
Pages
3046-50
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC383759
External Links
PubMed source DOI: 10.1073/pnas.76.7.3046 PMC Full Text View journal details
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