Alternative translocation of protons and halide ions by bacteriorhodopsin

A. Dér, S. Száraz, R. Tóth-Boconádi, Zs Tokaji, L. Keszthelyi, W. Stoeckenius

Research output: Contribution to journalArticle

87 Citations (Scopus)

Abstract

Bacteriorhodopsin (bR568) in purple membrane near pH 2 shifts its absorption maximum from 568 to 605 nm forming the blue protein bRacid605, which no longer transports protons and which shows no transient deprotonation of the Schiff base upon illumination. Continued acid titration with HCl or HBr but not H2SO4 restores the purple chromophore to yield bRHCl564 or bRHBr568. These acid purple forms also regain transmembrane charge transport, but no transient Schiff base deprotonation is observed. In contrast to bR568, no rate decrease of the bRacidpurple transport kinetics is detected in 2H2O; however, the transport rate decreases by a factor of ≈2 in bRHBr568 compared with bRHCl564. The data indicate that in the acid purple form bR transports the halide anions instead of protons. We present a testable model for the transport mechanism, which should also be applicable to halorhodopsin.

Original languageEnglish
Pages (from-to)4751-4755
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume88
Issue number11
Publication statusPublished - Jun 1 1991

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Bacteriorhodopsins
Protons
Schiff Bases
Ions
Acids
Halorhodopsins
Purple Membrane
Lighting
Anions
Proteins

Keywords

  • Electric signals
  • Halorhodopsin
  • Isotope effects
  • Photocycle kinetics

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

Dér, A., Száraz, S., Tóth-Boconádi, R., Tokaji, Z., Keszthelyi, L., & Stoeckenius, W. (1991). Alternative translocation of protons and halide ions by bacteriorhodopsin. Proceedings of the National Academy of Sciences of the United States of America, 88(11), 4751-4755.

Alternative translocation of protons and halide ions by bacteriorhodopsin. / Dér, A.; Száraz, S.; Tóth-Boconádi, R.; Tokaji, Zs; Keszthelyi, L.; Stoeckenius, W.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 88, No. 11, 01.06.1991, p. 4751-4755.

Research output: Contribution to journalArticle

Dér, A, Száraz, S, Tóth-Boconádi, R, Tokaji, Z, Keszthelyi, L & Stoeckenius, W 1991, 'Alternative translocation of protons and halide ions by bacteriorhodopsin', Proceedings of the National Academy of Sciences of the United States of America, vol. 88, no. 11, pp. 4751-4755.
Dér, A. ; Száraz, S. ; Tóth-Boconádi, R. ; Tokaji, Zs ; Keszthelyi, L. ; Stoeckenius, W. / Alternative translocation of protons and halide ions by bacteriorhodopsin. In: Proceedings of the National Academy of Sciences of the United States of America. 1991 ; Vol. 88, No. 11. pp. 4751-4755.
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AU - Keszthelyi, L.

AU - Stoeckenius, W.

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N2 - Bacteriorhodopsin (bR568) in purple membrane near pH 2 shifts its absorption maximum from 568 to 605 nm forming the blue protein bRacid605, which no longer transports protons and which shows no transient deprotonation of the Schiff base upon illumination. Continued acid titration with HCl or HBr but not H2SO4 restores the purple chromophore to yield bRHCl564 or bRHBr568. These acid purple forms also regain transmembrane charge transport, but no transient Schiff base deprotonation is observed. In contrast to bR568, no rate decrease of the bRacidpurple transport kinetics is detected in 2H2O; however, the transport rate decreases by a factor of ≈2 in bRHBr568 compared with bRHCl564. The data indicate that in the acid purple form bR transports the halide anions instead of protons. We present a testable model for the transport mechanism, which should also be applicable to halorhodopsin.

AB - Bacteriorhodopsin (bR568) in purple membrane near pH 2 shifts its absorption maximum from 568 to 605 nm forming the blue protein bRacid605, which no longer transports protons and which shows no transient deprotonation of the Schiff base upon illumination. Continued acid titration with HCl or HBr but not H2SO4 restores the purple chromophore to yield bRHCl564 or bRHBr568. These acid purple forms also regain transmembrane charge transport, but no transient Schiff base deprotonation is observed. In contrast to bR568, no rate decrease of the bRacidpurple transport kinetics is detected in 2H2O; however, the transport rate decreases by a factor of ≈2 in bRHBr568 compared with bRHCl564. The data indicate that in the acid purple form bR transports the halide anions instead of protons. We present a testable model for the transport mechanism, which should also be applicable to halorhodopsin.

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