Is the purple color of bacteriorhodopsin maintained by lipid-protein interactions?

Baribeau, Johanne; Boucher, François

doi:10.1016/0005-2728(87)90029-6

Cited by 18 publications

(13 citation statements)

References 11 publications

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“…This is a strong possibility. Nevertheless, we must keep in mind that bR has strong interactions with its vicinal lipids which can be considered as co-factors [12,23]. Then, the structural unit consisting of the protein with its closely associated lipids, namely the lipid protein interface, could constitute a likely molecular target as well.…”

Section: Discussionmentioning

confidence: 99%

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Interaction of the general volatile anesthetic Enflurane with bacteriorhodopsin-DPPC proteoliposomes

Hauet

Paternostre

Létourneau

et al. 2009

J Therm Anal Calorim

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Homogenous bacteriorhodopsin-DPPC proteoliposomes were characterized and used as a target for the general anesthetic Enflurane. Dose-response curves for the protein and the lipids, in the very same sample, at high (2800) and low (360) lipid: bacteriorhodopsin molar ratios, were compared simultaneously. Above the main phase transition temperature of DPPC, there is no difference between the protein and lipid sensitivities toward the anesthetic. Below the main phase transition temperature of DPPC, the bacteriorhodopsin sensitivity toward Enflurane is much higher than that of lipids. Its dose-response curves reach saturation at anesthetic concentrations where their effect on lipids is barely visible, indicating that bulk lipids do not mediate the anesthetic action.

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Section: Discussionmentioning

confidence: 99%

“…Purple membranes were prepared from cultured cells of Halobacterium salinarium strain S 9 provided by Prof. T. Ebrey (U. of Washington), purified, and stored according to our standard procedures [12]. Before use, they were washed free of salt by successive sedimentations and then suspended in 10 mM Tris-Cl buffer containing 150 mM NaCl.…”

Section: Methodsmentioning

confidence: 99%

Interaction of the general volatile anesthetic Enflurane with bacteriorhodopsin-DPPC proteoliposomes

Hauet

Paternostre

Létourneau

et al. 2009

J Therm Anal Calorim

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“…BR5h8 is reversibly converted to a blue absorbing species by simply raising the p H to 12.6 (pK, = 13.2), yielding BR4h0 whose v~=~ R R band is at 1621 cm-' (Druckman et al, 1982). Detergent solubilization of B R and subsequent delipidation also gives rise to a blue shifted species, BR4#,] (Baribeau and Boucher, 1987), which has its v~=~ R R band at 1668 cm-I in H 2 0 and at 1644 cm-I in D 2 0 (Pande et al, 1989a), although acidification converts it reversibly to its red shifted form, BRS40. with pK,,=2.6.…”

Section: = N Stretching Mode and Protonation Of Schiff Basementioning

confidence: 99%

Vibrational Spectra of Rhodopsin and Bacteriorhodopsin

Kitagawa

Maeda

1989

Photochem & Photobiology

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“…In fact, the equilibrium between the 570 nm and 480 nm forms of bacteriorhodopsin is an acid-base equilibrium that appears under a wide variety of experimental conditions. In purified bacteriorhodopsin, detergent microenvironmental effects shift its pKa within a 8-pH unit range ( Baribeau and Boucher, 1987). In anesthetic-or solventtreated purple membranes, the same spectral transition occurs, between pH 4.5 and 7.5, depending on the solvent (Messaoudi et al, 1992, and references therein).…”

Section: Introductionmentioning

confidence: 99%

Reversible inhibition of proton release activity and the anesthetic-induced acid-base equilibrium between the 480 and 570 nm forms of bacteriorhodopsin

Boucher¹,

Taneva²,

Elouatik³

et al. 1996

Biophysical Journal

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In purple membrane added with general anesthetics, there exists an acid-base equilibrium between two spectral forms of the pigment: bR570 and bR480 (apparent pKa = 7.3). As the purple 570 nm bacteriorhodopsin is reversibly transformed into its red 480 nm form, the proton pumping capability of the pigment reversibly decreases, as indicated by transient proton release measurements and proton translocation action spectra of mixture of both spectral forms. It happens in spite of a complete photochemical activity in bR480 that is mostly characterized by fast deprotonation and slow reprotonation steps and which, under continuous illumination, bleaches with a yield comparable to that of bR570. This modified photochemical activity has a correlated specific photoelectrical counterpart: a faster proton extrusion current and a slower reprotonation current. The relative areas of all photocurrent phases are reduced in bR480, most likely because its photochemistry is accompanied by charge movements for shorter distances than in the native pigment, reflecting a reversible inhibition of the pumping activity.

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Is the purple color of bacteriorhodopsin maintained by lipid-protein interactions?

Cited by 18 publications

References 11 publications

Interaction of the general volatile anesthetic Enflurane with bacteriorhodopsin-DPPC proteoliposomes

Interaction of the general volatile anesthetic Enflurane with bacteriorhodopsin-DPPC proteoliposomes

Vibrational Spectra of Rhodopsin and Bacteriorhodopsin

Reversible inhibition of proton release activity and the anesthetic-induced acid-base equilibrium between the 480 and 570 nm forms of bacteriorhodopsin

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