Skip to main content
Biophysical Journal logoLink to Biophysical Journal
. 1977 Feb;17(2):179–183. doi: 10.1016/S0006-3495(77)85635-X

The quantum efficiency of the bacteriorhodopsin photocycle.

C R Goldschmidt, O Kalisky, T Rosenfeld, M Ottolenghi
PMCID: PMC1473461  PMID: 836935

Abstract

The quantum yield of the primary photoprocess in light-adapted bacteriorhodopsin (phi 1) was determined at room temperature with low-intensity 530 nm neodymium laser excitation, with bovine rhodopsin as a relative actinometer. The observed value of phi 1 - 0.25 +/- 0.05, and the previously determined parameter phi 1/phi 2 - 0.4 [where phi 2 denotes the quantum efficiency of the back photoprecess from the primary species K (590)] imply that phi 1 + phi 2 approximately equal 1. This feature, also characterizing the photochemistry of rhodopsin, bears on the nature and mechanism of the primary event in both systems.

Full text

PDF
179

Selected References

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

  1. Becher B., Ebrey T. G. The quantum efficiency for the photochemical conversion of the purple membrane protein. Biophys J. 1977 Feb;17(2):185–191. doi: 10.1016/S0006-3495(77)85636-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. 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]
  3. Dartnall H. J. The photosensitivities of visual pigments in the presence of hydroxylamine. Vision Res. 1968 Apr;8(4):339–358. doi: 10.1016/0042-6989(68)90104-1. [DOI] [PubMed] [Google Scholar]
  4. Ebrey T. G. The use of Ammonyx LO in the purification of rhodopsin and rod outer segments. Vision Res. 1971 Sep;11(9):1007–1009. doi: 10.1016/0042-6989(71)90220-3. [DOI] [PubMed] [Google Scholar]
  5. Goldschmidt C. R., Ottolenghi M., Korenstein R. On the primary quantum yields in the bacteriorhodopsin photocycle. Biophys J. 1976 Jul;16(7):839–843. doi: 10.1016/S0006-3495(76)85732-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Goldschmidt C. R., Ottolenghi M., Rosenfeld T. Primary processes in photochemistry of rhodopsin at room temperature. Nature. 1976 Sep 9;263(5573):169–171. doi: 10.1038/263169a0. [DOI] [PubMed] [Google Scholar]
  7. Lozier R. H., Bogomolni R. A., Stoeckenius W. Bacteriorhodopsin: a light-driven proton pump in Halobacterium Halobium. Biophys J. 1975 Sep;15(9):955–962. doi: 10.1016/S0006-3495(75)85875-9. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. 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]
  9. Oesterhelt D., Stoeckenius W. Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane. Methods Enzymol. 1974;31:667–678. doi: 10.1016/0076-6879(74)31072-5. [DOI] [PubMed] [Google Scholar]
  10. Papermaster D. S., Dreyer W. J. Rhodopsin content in the outer segment membranes of bovine and frog retinal rods. Biochemistry. 1974 May 21;13(11):2438–2444. doi: 10.1021/bi00708a031. [DOI] [PubMed] [Google Scholar]
  11. Sherman W. V., Korenstein R., Caplan S. R. Energetics and chronology of phototransients in the light response of the purple membrane of Halobacterium halobium. Biochim Biophys Acta. 1976 Jun 8;430(3):454–458. doi: 10.1016/0005-2728(76)90021-9. [DOI] [PubMed] [Google Scholar]
  12. Sherman W. V., Slifkin M. A., Caplan S. R. Kinetic studies of phototransients in bacteriorhodopsin. Biochim Biophys Acta. 1976 Feb 16;423(2):238–248. doi: 10.1016/0005-2728(76)90182-1. [DOI] [PubMed] [Google Scholar]

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

RESOURCES