Skip to main content
PMC home page
Biophysical Journal logoLink to Biophysical Journal
. 1985 May;47(5):721–724. doi: 10.1016/S0006-3495(85)83969-2

Characterization of the chromophore of the third rhodopsin-like pigment of Halobacterium halobium and its photoproduct.

M Tsuda, B Nelson, C H Chang, R Govindjee, T G Ebrey
PMCID: PMC1435195  PMID: 4016190

Abstract

Halobacterium halobium contains at least three retinal-containing pigments: bacteriorhodopsin, halorhodopsin, and a third rhodopsin-like pigment (tR) absorbing at approximately 590 nm, tR590. Illumination of tR590 gives rise to a very long-lived blue absorbing photoproduct, tR370. Using high-performance liquid chromatography we show that the chromophore of tR590 is primarily all-trans retinal and its conversion by light to tR370 causes the chromophore to isomerize primarily to the 13-cis conformation. Irradiation of the tR370 gives rise to a transient photoproduct absorbing at approximately 520 nm that decays back to the initial pigment tR590. In addition to all-trans retinal, the apomembrane of tR can also combine with 13-cis retinal but not with the 9- or 11-cis isomers.

Full text

PDF
723

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. Bogomolni R. A., Spudich J. L. Identification of a third rhodopsin-like pigment in phototactic Halobacterium halobium. Proc Natl Acad Sci U S A. 1982 Oct;79(20):6250–6254. doi: 10.1073/pnas.79.20.6250. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Govindjee R., Ebrey T. G., Crofts A. R. The quantum efficiency of proton pumping by the purple membrane of Halobacterium halobium. Biophys J. 1980 May;30(2):231–242. doi: 10.1016/S0006-3495(80)85091-0. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Groenendijk G. W., de Grip W. J., Daemen F. J. Identification and characterization of syn- and anti-isomers of retinaloximes. Anal Biochem. 1979 Nov 1;99(2):304–310. doi: 10.1016/s0003-2697(79)80011-1. [DOI] [PubMed] [Google Scholar]
  5. Hazemoto N., Kamo N., Kobatake Y., Tsuda M., Terayama Y. Effect of salt on photocycle and ion-pumping of halorhodopsin and third rhodopsinlike pigment of Halobacterium halobium. Biophys J. 1984 Jun;45(6):1073–1077. doi: 10.1016/S0006-3495(84)84254-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hazemoto N., Kamo N., Terayama Y., Kobatake Y., Tsuda M. Photochemistry of two rhodopsinlike pigments in bacteriorhodopsin-free mutant of Halobacterium halobium. Biophys J. 1983 Oct;44(1):59–64. doi: 10.1016/S0006-3495(83)84277-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Mukohata Y., Kaji Y. Light-induced membrane-potential increase, ATP synthesis, and proton uptake in Halobacterium halobium, R1mR catalyzed by halorhodopsin: Effects of N,N'-dicyclohexylcarbodiimide, triphenyltin chloride, and 3,5-di-tert-butyl-4-hydroxybenzylidenemalononitrile (SF6847). Arch Biochem Biophys. 1981 Jan;206(1):72–76. doi: 10.1016/0003-9861(81)90067-9. [DOI] [PubMed] [Google Scholar]
  8. Oesterhelt D., Stoeckenius W. Rhodopsin-like protein from the purple membrane of Halobacterium halobium. Nat New Biol. 1971 Sep 29;233(39):149–152. doi: 10.1038/newbio233149a0. [DOI] [PubMed] [Google Scholar]
  9. Spudich E. N., Spudich J. L. Control of transmembrane ion fluxes to select halorhodopsin-deficient and other energy-transduction mutants of Halobacterium halobium. Proc Natl Acad Sci U S A. 1982 Jul;79(14):4308–4312. doi: 10.1073/pnas.79.14.4308. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Spudich J. L., Bogomolni R. A. Spectroscopic discrimination of the three rhodopsinlike pigments in Halobacterium halobium membranes. Biophys J. 1983 Aug;43(2):243–246. doi: 10.1016/S0006-3495(83)84345-8. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Stoeckenius W., Lozier R. H., Bogomolni R. A. Bacteriorhodopsin and the purple membrane of halobacteria. Biochim Biophys Acta. 1979 Mar 14;505(3-4):215–278. doi: 10.1016/0304-4173(79)90006-5. [DOI] [PubMed] [Google Scholar]
  12. Tomioka H., Kamo N., Takahashi T., Kobatake Y. Photochemical intermediate of third rhodopsin-like pigment in Halobacterium halobium by simultaneous illumination with red and blue light. Biochem Biophys Res Commun. 1984 Sep 28;123(3):989–994. doi: 10.1016/s0006-291x(84)80231-4. [DOI] [PubMed] [Google Scholar]
  13. Tsuda M., Ebrey T. G. Effect of high pressure on the absorption spectrum and isomeric composition of bacteriorhodopsin. Biophys J. 1980 Apr;30(1):149–157. doi: 10.1016/S0006-3495(80)85083-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Tsuda M., Glaccum M., Nelson B., Ebrey T. G. Light isomerizes the chromophore of bacteriorhodopsin. Nature. 1980 Sep 25;287(5780):351–353. doi: 10.1038/287351a0. [DOI] [PubMed] [Google Scholar]
  15. Tsuda M., Hazemoto N., Kondo M., Kamo N., Kobatake Y., Terayama Y. Two photocycles in halobacterium halobium that lacks bacteriorhodopsin. Biochem Biophys Res Commun. 1982 Oct 15;108(3):970–976. doi: 10.1016/0006-291x(82)92094-0. [DOI] [PubMed] [Google Scholar]

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

RESOURCES