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. 1985 Jun;82(11):3662–3664. doi: 10.1073/pnas.82.11.3662

Importance of bound divalent cations to the tyrosine deprotonation during the photocycle of bacteriorhodopsin

Paul Dupuis 1, Timothy C Corcoran 1, M A El-Sayed 1
PMCID: PMC397846  PMID: 16593567

Abstract

The transient absorption changes occurring at 297 nm during the photocycles of the deionized and acidified bacteriorhodopsins (blue membranes) were studied. As opposed to what happens during the photocycle of the purple membrane, for the blue membranes only the fast absorption increase corresponding to trans-cis isomerization of the retinal chromophore is present; the slow rise attributed to the tyrosine deprotonation is not observed. The addition of different salts to the deionized membrane restores the original color and causes a tyrosine deprotonation during the photocycle. This suggests that the presence of cations is required for the deprotonation of tyrosine as it is for the deprotonation of the retinylidene Schiff base. These results are discussed in terms of the recently proposed cation model for the observed deprotonation processes in the photocycle of bacteriorhodopsin.

Keywords: deionized bacteriorhodopsin, acidified bacteriorhodopsin, blue membrane, tyrosinate formation, trans-cis isomerization

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Selected References

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  1. Belliveau J. W., Lanyi J. K. Analogies between respiration and a light-driven proton pump as sources of energy for active glutamate transport in Halobacterium holobium. Arch Biochem Biophys. 1977 Jan 15;178(1):308–314. doi: 10.1016/0003-9861(77)90196-5. [DOI] [PubMed] [Google Scholar]
  2. Bogomolni R. A., Stubbs L., Lanyi J. K. Illumination-dependent changes in the intrinsic fluorescence of bacteriorhodopsin. Biochemistry. 1978 Mar 21;17(6):1037–1041. doi: 10.1021/bi00599a015. [DOI] [PubMed] [Google Scholar]
  3. Bridgen J., Walker I. D. Photoreceptor protein from the purple membrane of Halobacterium halobium. Molecular weight and retinal binding site. Biochemistry. 1976 Feb 24;15(4):792–798. doi: 10.1021/bi00649a010. [DOI] [PubMed] [Google Scholar]
  4. 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]
  5. Fischer U., Oesterhelt D. Chromophore equilibria in bacteriorhodopsin. Biophys J. 1979 Nov;28(2):211–230. doi: 10.1016/S0006-3495(79)85172-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hanamoto J. H., Dupuis P., El-Sayed M. A. On the protein (tyrosine)-chromophore (protonated Schiff base) coupling in bacteriorhodopsin. Proc Natl Acad Sci U S A. 1984 Nov;81(22):7083–7087. doi: 10.1073/pnas.81.22.7083. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Henderson R. The purple membrane from Halobacterium halobium. Annu Rev Biophys Bioeng. 1977;6:87–109. doi: 10.1146/annurev.bb.06.060177.000511. [DOI] [PubMed] [Google Scholar]
  8. Hess B., Kuschmitz D. Kinetic interaction between aromatic residues and the retinal chromophore of bacteriorhodopsin during the photocycle. FEBS Lett. 1979 Apr 15;100(2):334–340. doi: 10.1016/0014-5793(79)80364-6. [DOI] [PubMed] [Google Scholar]
  9. Kimura Y., Ikegami A., Stoeckenius W. Salt and pH-dependent changes of the purple membrane absorption spectrum. Photochem Photobiol. 1984 Nov;40(5):641–646. doi: 10.1111/j.1751-1097.1984.tb05353.x. [DOI] [PubMed] [Google Scholar]
  10. Lam E., Seltzer S., Katsura T., Packer L. Light-dependent nitration of bacteriorhodopsin. Arch Biochem Biophys. 1983 Nov;227(1):321–328. doi: 10.1016/0003-9861(83)90376-4. [DOI] [PubMed] [Google Scholar]
  11. Lemke H. D., Oesterhelt D. The role of tyrosine residues in the function of bacteriorhodopsin. Specific nitration of tyrosine 26. Eur J Biochem. 1981 Apr;115(3):595–604. doi: 10.1111/j.1432-1033.1981.tb06244.x. [DOI] [PubMed] [Google Scholar]
  12. 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]
  13. Moore T. A., Edgerton M. E., Parr G., Greenwood C., Perham R. N. Studies of an acid-induced species of purple membrane from Halobacterium halobium. Biochem J. 1978 May 1;171(2):469–476. doi: 10.1042/bj1710469. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Mowery P. C., Lozier R. H., Chae Q., Tseng Y. W., Taylor M., Stoeckenius W. Effect of acid pH on the absorption spectra and photoreactions of bacteriorhodopsin. Biochemistry. 1979 Sep 18;18(19):4100–4107. doi: 10.1021/bi00586a007. [DOI] [PubMed] [Google Scholar]
  15. Muccio D. D., Cassim J. Y. Interpretations of the effects of pH on the spectra of purple membrane. J Mol Biol. 1979 Dec 15;135(3):595–609. doi: 10.1016/0022-2836(79)90166-9. [DOI] [PubMed] [Google Scholar]
  16. 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]
  17. Scherrer P., Packer L., Seltzer S. Effect of iodination of the purple membrane on the photocycle of bacteriorhodopsin. Arch Biochem Biophys. 1981 Dec;212(2):589–601. doi: 10.1016/0003-9861(81)90402-1. [DOI] [PubMed] [Google Scholar]
  18. Stoeckenius W., Bogomolni R. A. Bacteriorhodopsin and related pigments of halobacteria. Annu Rev Biochem. 1982;51:587–616. doi: 10.1146/annurev.bi.51.070182.003103. [DOI] [PubMed] [Google Scholar]
  19. 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]
  20. Tsuji K., Rosenheck K. The low pH species of bacteriorhodopsin. Structure and proton pump activity. FEBS Lett. 1979 Feb 15;98(2):368–372. doi: 10.1016/0014-5793(79)80219-7. [DOI] [PubMed] [Google Scholar]

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