The role of chromophore in the lipid–protein interactions in bacteriorhodopsin–phosphatidylcholine vesicles

Bryl, Krzysztof; Yoshihara, Kazuo

doi:10.1016/s0014-5793(00)01910-4

Cited by 4 publications

(7 citation statements)

References 30 publications

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“…Previously, the deuterium exchange and atomic force microscopy (AFM) experiments showed that removal of the retinal induces subtle changes of the tertiary structure and the loops of bR to the more open conformation. , Related to this, the change of protein−lipid interaction by retinal removal was observed in the artificial lipid vesicle system . In this study, this protein−lipid interaction change on the membrane was successfully detected as the difference of the solubility between bR and bO in DDM (Figure ).…”

Section: Discussionsupporting

confidence: 53%

“…7,8 Related to this, the change of protein-lipid interaction by retinal removal was observed in the artificial lipid vesicle system. 29 In this study, this protein-lipid interaction change on the membrane was successfully detected as the difference of the solubility between bR and bO in DDM (Figure 4). Interestingly, the bR solubility was also increased by the cyclic and milliseconds order of structural change after light absorption ( Figure 5).…”

Section: Solubility Of Bleached Br In Ddmmentioning

confidence: 66%

“…For instance, Bryl and Yoshihara demonstrated that the removal of retinal from bR causes loosening of the lipid packing around the bO by fluorescence measurement in the reconstituted vesicle system. 29 13 C NMR measurement also showed increase in the proportion of surrounding lipids per protein by retinal release. 30 In addition, the elimination of some native lipids from PM affects the photocycle of bR, 31 indicating the importance of the lipidprotein interactions and those dynamic changes for a normal photocycle.…”

mentioning

confidence: 88%

“…On this background, some researchers have focused on the change of bR−lipid interaction accompanied by the conformational change of bR. For instance, Bryl and Yoshihara demonstrated that the removal of retinal from bR causes loosening of the lipid packing around the bO by fluorescence measurement in the reconstituted vesicle system .…”

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confidence: 99%

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Sensitive Detection of Protein−Lipid Interaction Change on Bacteriorhodopsin Using Dodecyl β-d-Maltoside

et al. 2011

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A light-driven proton pump bacteriorhodopsin (bR) forms a two-dimensional hexagonal lattice with about 10 archaeal lipids per monomer bR on purple membrane (PM) of Halobacterium salinarum. In this study, we found that the weakening of the bR-lipid interaction on PM by addition of alcohol can be detected as the significant increase of protein solubility in a nonionic detergent, dodecyl β-D-maltoside (DDM). The protein solubility in DDM was also increased by bR-lipid interaction change accompanied by structural change of the apoprotein after retinal removal and was about 7 times higher in the case of completely bleached membrane than that of intact PM. Interestingly, the cyclic and milliseconds order of structural change of bR under light irradiation also led to increasing the protein solubility and had a characteristic light intensity dependence with a phase transition. These results indicate that there is a photointermediate in which bR-lipid interaction has been changed by its dynamic structural change. Because partial delipidation of PM by CHAPS gave minor influence for the change of the protein solubility compared to intact PM in both dark and light conditions, it is suggested that specific interactions of bR with some lipids which remain on PM even after delipidation treatment have a key role for the change of solubility in DDM induced by alcohol binding, ligand release, and photon absorption on bR.

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Section: Discussionsupporting

confidence: 53%

Section: Solubility Of Bleached Br In Ddmmentioning

confidence: 66%

mentioning

confidence: 88%

mentioning

confidence: 99%

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Sensitive Detection of Protein−Lipid Interaction Change on Bacteriorhodopsin Using Dodecyl β-d-Maltoside

et al. 2011

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“…31 The incorporation of fluorinated retinal analogues with changed shape and altered electronic properties into the binding site of bR (or bR mutant, D96N) was used to strengthen the feedback between the protein surrounding and chromophore in bRs. 22,32 Fluorine atom is a highly electronegative atom. Its incorporation into chromophore structure causes enlargement mostly of electrostatic interactions with charged amino acids (although steric interactions cannot be excluded).…”

Section: Introductionmentioning

confidence: 99%

Fluorescence Resonance Energy Transfer (FRET) as a Spectroscopic Ruler for the Investigation of Protein Induced Lipid Membrane Curvature: Bacteriorhodopsin and Bacteriorhodopsin Analogs in Model Lipid Membranes

Bryl

2022

Appl Spectrosc

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Bacteriorhodopsin (bR) is a light-driven proton pump existing in the purple membranes (PM) of Halobacterium salinarum. The effects associated with changes in proton distribution (proton gradient, membrane electric potential) play a key role in ATP-ase stimulation. However, how the bioenergetic modulus (bR-PM-ATPase) functions remains unclear. One can find indications that hydrophobic matching and the curvature of the lipid membrane may form a functional link between bR and ATP-ase. To verify whether an interaction between bR and lipids can lead to curvature of the lipid membrane, a spectroscopic ruler – a fluorescence resonance energy transfer (FRET) tool – was used. The distances from fluorescent lipid probes [octadecyl rhodamine B chloride (RhB), 1,1’-dioctadecyl-3,3,3’,3’-tetramethylindocarbocyanine perchlorate (DiI), 16-(9-anthroyloxy) palmitic acid (16AP)] and hydrophobic probe 1,6-diphenyl-1,3,5-hexatriene (DPH), to the retinal chromophore of bR incorporated into phospholipid vesicles, were measured. The incorporation of retinal analogues with changed shape and/or altered electronic properties into the binding site of a bR or bR mutant were used to strengthen the feedback between the protein surrounding and chromophore. The experiments were performed with wild-type and D96N-mutated bR carrying retinal or 14-(12-,10-, 13,14-bi-) Fluororetinal. As far as it is known, this is the first time that results obtained by the FRET method show that bR can induce a change in lipid structure interpreted as hydrophobically induced curving of the lipid membrane. Evidence was provided that the chromophore contributed to this effect. The extent of contribution was dependent on the chromophore structure in close vicinity to the place of its link with opsin. The implications of these findings for bR-PM-ATPase module functioning are also discussed.

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Action spectrum for reorientations in bacteriorhodopsin of purple membrane in suspension

Mostafa

2023

Sci Rep

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In the present study, the dependency of purple membrane (PM) dielectric responses on the wavelength of light in the range 380–750 nm has showed meaningful changes about the rotation of PM in suspension and about the rotation of bacteriorhodopsin (bR) trimer inside PM, as well. The action spectrum of PM random walk substantiates the existence of two states of bR. One of them (blue edge-state) lies at the blue edge and the other (red edge-state) at the red edge of the visible absorption of bR. The results might bear on correlation of these bands to some bR photocycle intermediates or bR photoproducts. The results implicate the protein–chromophore interactions that eventually underlie protein–lipid interactions. Disrupting the protein–lipid contact during the illumination with light of wavelength in ranges of (410–470 nm) and (610–720 nm) has resulted in emergence of distinct dielectric dispersion at 0.06–0.08 MHz which is comparable to the size of bR trimer or monomer.The work reports on the chromatic adaptation of bR in view of the dielectric spectral parameters of PM. It aimed to explore a correlation seemingly found between the light wavelength and the relaxations of bR trimer inside PM. Changes in rotational diffusion of bR trimer upon blue and red light illumination can influence the three dimensional data storage based on bR, which may implicate bR in bioelectronics.

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The role of chromophore in the lipid–protein interactions in bacteriorhodopsin–phosphatidylcholine vesicles

Cited by 4 publications

References 30 publications

Sensitive Detection of Protein−Lipid Interaction Change on Bacteriorhodopsin Using Dodecyl β-d-Maltoside

Sensitive Detection of Protein−Lipid Interaction Change on Bacteriorhodopsin Using Dodecyl β-d-Maltoside

Fluorescence Resonance Energy Transfer (FRET) as a Spectroscopic Ruler for the Investigation of Protein Induced Lipid Membrane Curvature: Bacteriorhodopsin and Bacteriorhodopsin Analogs in Model Lipid Membranes

Action spectrum for reorientations in bacteriorhodopsin of purple membrane in suspension

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