Skip to main content
NCBI home page
Biophysical Journal logoLink to Biophysical Journal
. 1985 Aug;48(2):201–208. doi: 10.1016/S0006-3495(85)83773-5

Photoconversion from the light-adapted to the dark-adapted state of bacteriorhodopsin.

T Kouyama, R A Bogomolni, W Stoeckenius
PMCID: PMC1329311  PMID: 4052558

Abstract

Dark and light adaptation of bacteriorhodopsin in purple membrane multilayers at less than 100% relative humidity differs from that seen in suspensions. Equilibrium between the two bacteriorhodopsin isomers (bR cis 550 and bR trans 570) in the light-adapted state becomes dependent on the wavelength of actinic light. Excitation at the red edge of the visible absorption band causes dark adaptation in a light-adapted sample. Using polarized actinic and measuring light, we show that acceleration of the dark adaptation through heating by actinic light cannot explain this observation. A light-driven bR trans 570 to bR cis 550 reaction that competes with the well-known 13 cis-to-all-trans light adaptation reaction must exist under our experimental conditions. Trans-to-cis conversion is a one-photon process distinct from the two photon process observed by others in purple membrane suspensions (Sperling, W., C. N. Rafferty, K. D. Kohl, and N. A. Dencher, 1978, FEBS (Fed. Eur. Biochem. Soc.) Lett. 97:129-132). Its quantum efficiency increases monotonously on reducing the hydration level, and is paralleled by an increase in the lifetime of the M410 intermediate of the trans photocycle. We suggest that at this point a branch leads from the all-trans into the 13-cis photocycle. It is probably the same reaction that causes the reduced light adaptation in monomeric bacteriorhodopsin (Casadio, R., H. Gutowitz, P. Mowery, M. Taylor, and W. Stoeckenius, 1980, Biochim. Biophys. Acta. 590:13-23; Casadio, R., and W. Stoeckenius, 1980, Biochemistry. 19:3374-3381).

Full text

PDF
201

Selected References

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

  1. Bagley K., Dollinger G., Eisenstein L., Singh A. K., Zimányi L. Fourier transform infrared difference spectroscopy of bacteriorhodopsin and its photoproducts. Proc Natl Acad Sci U S A. 1982 Aug;79(16):4972–4976. doi: 10.1073/pnas.79.16.4972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bogomolni R. A., Baker R. A., Lozier R. H., Stoeckenius W. Action spectrum and quantum efficiency for proton pumping in Halobacterium halobium. Biochemistry. 1980 May 13;19(10):2152–2159. doi: 10.1021/bi00551a024. [DOI] [PubMed] [Google Scholar]
  3. Casadio R., Gutowitz H., Mowery P., Taylor M., Stoeckenius W. Light-dark adaptation of bacteriorhodopsin in triton-treated purple membrane. Biochim Biophys Acta. 1980 Mar 7;590(1):13–23. doi: 10.1016/0005-2728(80)90142-5. [DOI] [PubMed] [Google Scholar]
  4. Casadio R., Stoeckenius W. Effect of protein-protein interaction on light adaptation of bacteriorhodopsin. Biochemistry. 1980 Jul 8;19(14):3374–3381. doi: 10.1021/bi00555a043. [DOI] [PubMed] [Google Scholar]
  5. Dencher N. A., Kohl K. D., Heyn M. P. Photochemical cycle and light-dark adaptation of monomeric and aggregated bacteriorhodopsin in various lipid environments. Biochemistry. 1983 Mar 15;22(6):1323–1334. doi: 10.1021/bi00275a002. [DOI] [PubMed] [Google Scholar]
  6. 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]
  7. Hurley J. B., Becher B., Ebrey T. G. More evidence that light isomerises the cheomophore of purple membrane protein. Nature. 1978 Mar 2;272(5648):87–88. doi: 10.1038/272087a0. [DOI] [PubMed] [Google Scholar]
  8. Kalisky O., Goldschmidt C. R., Ottolenghi M. On the photocycle and light adaptation of dark-adapted bacteriorhodopsin. Biophys J. 1977 Aug;19(2):185–189. doi: 10.1016/S0006-3495(77)85579-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kalisky O., Ottolenghi M., Honig B., Korenstein R. Environmental effects on formation and photoreaction of the M412 photoproduct of bacteriorhodopsin: implications for the mechanism of proton pumping. Biochemistry. 1981 Feb 3;20(3):649–655. doi: 10.1021/bi00506a031. [DOI] [PubMed] [Google Scholar]
  10. Korenstein R., Hess B. Hydration effects on cis--trans isomerization of bacteriorhodopsin. FEBS Lett. 1977 Oct 1;82(1):7–11. doi: 10.1016/0014-5793(77)80874-0. [DOI] [PubMed] [Google Scholar]
  11. Korenstein R., Hess B. Hydration effects on the photocycle of bacteriorhodopsin in thin layers of purple membrane. Nature. 1977 Nov 10;270(5633):184–186. doi: 10.1038/270184a0. [DOI] [PubMed] [Google Scholar]
  12. Lazarev Y. A., Terpugov E. L. Effect of water on the structure of bacteriorhodopsin and photochemical processes in purple membranes. Biochim Biophys Acta. 1980 May 9;590(3):324–338. doi: 10.1016/0005-2728(80)90203-0. [DOI] [PubMed] [Google Scholar]
  13. 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]
  14. 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]
  15. Maeda A., Iwasa T., Yoshizawa T. Isomeric composition of retinal chromophore in dark-adapted bacteriorhodopsin. J Biochem. 1977 Dec;82(6):1599–1604. doi: 10.1093/oxfordjournals.jbchem.a131855. [DOI] [PubMed] [Google Scholar]
  16. 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]
  17. Oesterhelt D., Meentzen M., Schuhmann L. Reversible dissociation of the purple complex in bacteriorhodopsin and identification of 13-cis and all-trans-retinal as its chromophores. Eur J Biochem. 1973 Dec 17;40(2):453–463. doi: 10.1111/j.1432-1033.1973.tb03214.x. [DOI] [PubMed] [Google Scholar]
  18. 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]
  19. 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]
  20. Pettei M. J., Yudd A. P., Nakanishi K., Henselman R., Stoeckenius W. Identification of retinal isomers isolated from bacteriorhodopsin. Biochemistry. 1977 May 3;16(9):1955–1959. doi: 10.1021/bi00628a031. [DOI] [PubMed] [Google Scholar]
  21. Rothschild K. J., Zagaeski M., Cantore W. A. Conformational changes of bacteriorhodopsin detected by Fourier transform infrared difference spectroscopy. Biochem Biophys Res Commun. 1981 Nov 30;103(2):483–489. doi: 10.1016/0006-291x(81)90478-2. [DOI] [PubMed] [Google Scholar]
  22. Schreckenbach T., Oesterhelt D. Photochemical and chemical studies on the chromophore of bacteriorhodopsin. Fed Proc. 1977 May;36(6):1810–1814. [PubMed] [Google Scholar]
  23. Sperling W., Carl P., Rafferty Ch, Dencher N. A. Photochemistry and dark equilibrium of retinal isomers and bacteriorhodopsin isomers. Biophys Struct Mech. 1977 Jun 29;3(2):79–94. doi: 10.1007/BF00535798. [DOI] [PubMed] [Google Scholar]
  24. Váró G., Keszthelyi L. Photoelectric signals from dried oriented purple membranes of Halobacterium halobium. Biophys J. 1983 Jul;43(1):47–51. doi: 10.1016/S0006-3495(83)84322-7. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES