Skip to main content
NCBI home page
Biophysical Journal logoLink to Biophysical Journal
. 1977 Dec;20(3):369–375. doi: 10.1016/S0006-3495(77)85555-0

Resonance Raman kinetic spectroscopy of bacteriorhodopsin on the microsecond time scale.

A Campion, M A El-Sayed, J Terner
PMCID: PMC1473361  PMID: 922125

Abstract

Using a rotating disk with a slit of variable width, a continuous wave argon ion laser, and an Optical Multichannel Analyzer for detection, a new technique is reported which should, in principle, be capable of recording resonance Raman spectra with time resolution of 100 ns. The resonance Raman spectra of the intermediates of the photosynthetic cycle of bacteriorhodopsin are recorded on the microsecond time scale. Both the kinetic results and the resonance enhancement profile suggest that deprotonation results in an intermediate preceding bM412 that has an optical absorption maximum at a wavelength longer than that of bM412.

Full text

PDF
369

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Becher B. M., Cassim J. Y. Improved isolation procedures for the purple membrane of Halobacterium halobium. Prep Biochem. 1975;5(2):161–178. doi: 10.1080/00327487508061568. [DOI] [PubMed] [Google Scholar]
  2. Campion A., Terner J., El-Sayed M. A. Time-resolved resonance Raman spectroscopy of bacteriorhodopsin. Nature. 1977 Feb 17;265(5595):659–661. doi: 10.1038/265659a0. [DOI] [PubMed] [Google Scholar]
  3. Chance B., Porte M., Hess B., Oesterhelt D. Low temperature kinetics of H+ changes of bacterial rhodopsin. Biophys J. 1975 Sep;15(9):913–917. doi: 10.1016/S0006-3495(75)85865-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Chu Kung M., DeVault D., Hess B., Oesterhelt D. Photolysis of bacterial rhodopsin. Biophys J. 1975 Sep;15(9):907–911. doi: 10.1016/S0006-3495(75)85864-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Dencher N., Wilms M. Flash photometric experiments on the photochemical cycle of bacteriorhodopsin. Biophys Struct Mech. 1975 May 30;1(3):259–271. doi: 10.1007/BF00535760. [DOI] [PubMed] [Google Scholar]
  6. Korenstein R., Sherman W. V., Caplan S. R. Kinetic isotope effects in the photochemical cycle of bacteriorhodopsin. Biophys Struct Mech. 1976 Dec 22;2(3):267–276. doi: 10.1007/BF00535372. [DOI] [PubMed] [Google Scholar]
  7. Lewis A., Spoonhower J., Bogomolni R. A., Lozier R. H., Stoeckenius W. Tunable laser resonance raman spectroscopy of bacteriorhodopsin. Proc Natl Acad Sci U S A. 1974 Nov;71(11):4462–4466. doi: 10.1073/pnas.71.11.4462. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Marcus M. A., Lewis A. Kinetic resonance Raman spectroscopy: dynamics of deprotonation of the Schiff base of bacteriorhodopsin. Science. 1977 Mar 25;195(4284):1328–1330. doi: 10.1126/science.841330. [DOI] [PubMed] [Google Scholar]
  9. Mendelsohn R., Verma A. L., Bernstein H. J., Kates M. Structural studies of bacteriorhodopsin from Halobacterium cutirubrum by resonance Raman spectroscopy. Can J Biochem. 1974 Sep;52(9):774–781. doi: 10.1139/o74-110. [DOI] [PubMed] [Google Scholar]
  10. Oesterhelt D. Bacteriorhodopsin as an example of a light-driven proton pump. Angew Chem Int Ed Engl. 1976 Jan;15(1):17–24. doi: 10.1002/anie.197600171. [DOI] [PubMed] [Google Scholar]
  11. Oesterhelt D., Hess B. Reversible photolysis of the purple complex in the purple membrane of Halobacterium halobium. Eur J Biochem. 1973 Aug 17;37(2):316–326. doi: 10.1111/j.1432-1033.1973.tb02990.x. [DOI] [PubMed] [Google Scholar]

Articles from Biophysical Journal are provided here courtesy of The Biophysical Society

RESOURCES