Anion-dependent transition of two acidic forms of bacteriorhodopsin

Drachev, Alexander L.; Drachev, Lel A.; Kaulen, Andrey D.; Khitrina, L. V.; Skulachev, Vladimir P.; Lepnev, Gerasim P.; Chekulaeva, L. N.

doi:10.1016/s0005-2728(89)80229-4

Cited by 8 publications

(6 citation statements)

References 33 publications

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“…Therefore, we conclude that the same binding site accounts for both effects. A similar behavior was reported for wild-type BR at acidic pH values (Varo & Lanyi, 1989;Drachev et al, 1989).…”

Section: Anion Effects On Photocycle Intermediatessupporting

confidence: 84%

“…Neutralization of the D85 anion by protonation (acid BR or BR600 (Fischer & Oesterhelt, 1979), pK a ca 3) or mutation of D85 to asparagine or threonine induce a red shift of the absorption maximum (l max ) of BR from 570 nm to around 600 nm (Marti et al, 1991;Turner et al, 1993;Tittor et al, 1994;Sasaki et al, 1995). Anion-dependent shifts of l max of the BR chromophore at low pH back to the original absorption maximum (Fischer & Oesterhelt, 1979;Drachev et al, 1989;Varo & Lanyi, 1989), resonance Raman experiments of the anion-bound form of BR (Diller et al, 1987) and alterations in the photo reaction dependent on anion concentration (Varo & Lanyi, 1989) suggested binding of chloride and other halides at a location close to the Schiff base and in the vicinity of D85. Mutants D85X, D85N/D212N and R82Q/D85N/D212N show red shifts and their absorption maxima similar to those observed with protonated D85.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Chloride and proton transport in bacteriorhodopsin mutant D85T: different modes of ion translocation in a retinal protein 1 1Edited by A.R.Fersht

Tittor

Haupts

et al. 1997

Journal of Molecular Biology

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“…Therefore, we conclude that the same binding site accounts for both effects. A similar behavior was reported for wild-type BR at acidic pH values (Varo & Lanyi, 1989;Drachev et al, 1989).…”

Section: Anion Effects On Photocycle Intermediatessupporting

confidence: 84%

Section: Introductionmentioning

confidence: 99%

Chloride and proton transport in bacteriorhodopsin mutant D85T: different modes of ion translocation in a retinal protein 1 1Edited by A.R.Fersht

Tittor

Haupts

et al. 1997

Journal of Molecular Biology

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“…The blue acid form of the wild‐type bR with protonated Asp‐85 gives the purple acid form after Cl − binding [4–14]. This transition is very similar to the corresponding transition in the D85T and D85S mutants.…”

Section: Resultsmentioning

confidence: 57%

“…Protonation of the D85 converts bR into an acid blue form incapable of proton transport. Further Cl − binding gives an acid purple form [4–14]. bR mutants D85T and D85S in the absence of Cl − are also blue pigments.…”

Section: Introductionmentioning

confidence: 99%

Cl⁻‐dependent photovoltage responses of bacteriorhodopsin: comparison of the D85T and D85S mutants and wild‐type acid purple form

Kalaidzidis

Kaulen

1997

FEBS Letters

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Laser flash-induced photovoltage responses of the D85S and D85T mutants as well as of the wild-type acid blue form are similar and reflect intraprotein charge redistribution caused by retinal isomerization. The Cl- -induced transition of all of these blue forms into purple ones is accompanied by the appearance of electrogenic stages, which is probably associated with Cl- translocation in the cytoplasmic direction. Cl- translocation efficiency of these purple forms is much lower than that of the proton transport by the wild-type bacteriorhodopsin. The values of the efficiency do not exceed 15, 8 and 3% for the D85T, D85S and wild-type acid purple form, respectively. Cl- induces an additional electrogenic phase in the photovoltage responses of the D85S mutant and the wild-type acid purple form. This phase is supposed to be associated with the reversible Cl- movement in the extracellular direction. It is interesting that this component is absent in the photovoltage response of the D85T mutant which has, like halorhodopsin, a threonine residue at position 85.

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“…Interestingly the H + and Cl~ specificities of bR and hR, respectively, are not absolute. Under certain conditions, (i) bR binds (Fischer & Oesterhelt, 1979;Drachev et al 1989;Varo & Lanyi, 1989) and maybe even transports (Der et al 1989(Der et al , 1991 Cl~ and (ii) hR can transport protons (Oesterhelt et al 1992;Bamberg et al 1993) in a light-dependent fashion. The former event occurs at low pH when the Schiff base remains protonated even in the light.…”

Section: Interrelations Of Retinal Protein Functionsmentioning

confidence: 99%

Interrelations of bioenergetic and sensory functions of the retinal proteins

Skulachev

1993

Quart. Rev. Biophys.

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Rhodopsins are intrinsic membrane retinal-containing proteins composed of 7 hydrophobic alpha-helical transmembrane columns and hydrophilic sequences of various length connecting the helices and localized at N- and C-ends of the polypeptide. The chromophore (retinal) forms a Schiff base with a lysine residue in the middle part of the last alpha-helix. Absorption of a photon results in isomerization of retinal which gives rise to a conformational change in the protein moiety. Rhodopsins can be involved in two entirely different types of activities, i.e. ion pumping and photosensing. Recent observations concerning the pumping and sensory mechanisms allowed both these events to be explained in terms of one and the same unitary concept, which postulates the formation of a hydrophilic cleft in the hydrophobic part of the protein molecule as a crucial step in energy conservation and photosensing.

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Anion-dependent transition of two acidic forms of bacteriorhodopsin

Cited by 8 publications

References 33 publications

Chloride and proton transport in bacteriorhodopsin mutant D85T: different modes of ion translocation in a retinal protein 1 1Edited by A.R.Fersht

Chloride and proton transport in bacteriorhodopsin mutant D85T: different modes of ion translocation in a retinal protein 1 1Edited by A.R.Fersht

Cl⁻‐dependent photovoltage responses of bacteriorhodopsin: comparison of the D85T and D85S mutants and wild‐type acid purple form

Interrelations of bioenergetic and sensory functions of the retinal proteins

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Anion-dependent transition of two acidic forms of bacteriorhodopsin

Cited by 8 publications

References 33 publications

Chloride and proton transport in bacteriorhodopsin mutant D85T: different modes of ion translocation in a retinal protein 1 1Edited by A.R.Fersht

Chloride and proton transport in bacteriorhodopsin mutant D85T: different modes of ion translocation in a retinal protein 1 1Edited by A.R.Fersht

Cl−‐dependent photovoltage responses of bacteriorhodopsin: comparison of the D85T and D85S mutants and wild‐type acid purple form

Interrelations of bioenergetic and sensory functions of the retinal proteins

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Cl⁻‐dependent photovoltage responses of bacteriorhodopsin: comparison of the D85T and D85S mutants and wild‐type acid purple form