Action Spectrum for Reorientations in Bacteriorhodopsin of Purple Membrane in Suspension

Overview

Journal Sci Rep

Specialty Science

Date 2023 May 16

PMID 37193768

Authors

Hamdy I A Mostafa

Affiliations

Soon will be listed here.

Abstract

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.

References

Li Y, Tian Y, Tian H, Tu T, Gou G, Wang Q . A Review on Bacteriorhodopsin-Based Bioelectronic Devices. Sensors (Basel). 2018; 18(5). PMC: 5982678. DOI: 10.3390/s18051368. View

Cherry R, Muller U, Schneider G . Rotational diffusion of bacteriorhodopsin in lipid membranes. FEBS Lett. 1977; 80(2):465-9. DOI: 10.1016/0014-5793(77)80498-5. View

Dancshazy Z, Tokaji Z, Der A . Bleaching of bacteriorhodopsin by continuous light. FEBS Lett. 1999; 450(1-2):154-7. DOI: 10.1016/s0014-5793(99)00487-1. View

Cherry R, Heyn M, Oesterhelt D . Rotational diffusion and exciton coupling of bacteriorhodopsin in the cell membrane of Halobacterium halobium. FEBS Lett. 1977; 78(1):25-30. DOI: 10.1016/0014-5793(77)80265-2. View

Cone R . Rotational diffusion of rhodopsin in the visual receptor membrane. Nat New Biol. 1972; 236(63):39-43. DOI: 10.1038/newbio236039a0. View

Abdulaev N, Strassmaier T, Ngo T, Chen R, Luecke H, Oprian D . Grafting segments from the extracellular surface of CCR5 onto a bacteriorhodopsin transmembrane scaffold confers HIV-1 coreceptor activity. Structure. 2002; 10(4):515-25. DOI: 10.1016/s0969-2126(02)00752-9. View

Dencher N, Heyn M . Bacteriorhodopsin monomers pump protons. FEBS Lett. 1979; 108(2):307-10. DOI: 10.1016/0014-5793(79)80552-9. View

Wan C, Qian J, Johnson C . Conformational motion in bacteriorhodopsin: the K to L transition. Biochemistry. 1991; 30(2):394-400. DOI: 10.1021/bi00216a013. View

Wan C, Qian J, Johnson C . Light-induced reorientation in the purple membrane. Biophys J. 1993; 65(2):927-38. PMC: 1225794. DOI: 10.1016/S0006-3495(93)81118-4. View

10.

Kouyama T, Bogomolni R, Stoeckenius W . Photoconversion from the light-adapted to the dark-adapted state of bacteriorhodopsin. Biophys J. 1985; 48(2):201-8. PMC: 1329311. DOI: 10.1016/S0006-3495(85)83773-5. View

11.

Lanyi J . Proton transfers in the bacteriorhodopsin photocycle. Biochim Biophys Acta. 2005; 1757(8):1012-8. DOI: 10.1016/j.bbabio.2005.11.003. View

12.

Cartailler J, Luecke H . X-ray crystallographic analysis of lipid-protein interactions in the bacteriorhodopsin purple membrane. Annu Rev Biophys Biomol Struct. 2003; 32:285-310. DOI: 10.1146/annurev.biophys.32.110601.142516. View

13.

Schwan H . Linear and nonlinear electrode polarization and biological materials. Ann Biomed Eng. 1992; 20(3):269-88. DOI: 10.1007/BF02368531. View

14.

Ahl P, Cone R . Light activates rotations of bacteriorhodopsin in the purple membrane. Biophys J. 1984; 45(6):1039-49. PMC: 1434987. DOI: 10.1016/S0006-3495(84)84251-4. View

15.

Becher B, Tokunaga F, Ebrey T . Ultraviolet and visible absorption spectra of the purple membrane protein and the photocycle intermediates. Biochemistry. 1978; 17(12):2293-300. DOI: 10.1021/bi00605a006. View

16.

Corcelli A, Lattanzio V, Mascolo G, Papadia P, Fanizzi F . Lipid-protein stoichiometries in a crystalline biological membrane: NMR quantitative analysis of the lipid extract of the purple membrane. J Lipid Res. 2002; 43(1):132-40. View

17.

Sperling W, Carl P, Rafferty C, Dencher N . Photochemistry and dark equilibrium of retinal isomers and bacteriorhodopsin isomers. Biophys Struct Mech. 1977; 3(2):79-94. DOI: 10.1007/BF00535798. View

18.

Dencher N, Kohl K, Heyn M . Photochemical cycle and light-dark adaptation of monomeric and aggregated bacteriorhodopsin in various lipid environments. Biochemistry. 1983; 22(6):1323-34. DOI: 10.1021/bi00275a002. View

19.

Torres J, Sepulcre F, Padros E . Conformational changes in bacteriorhodopsin associated with protein-protein interactions: a functional alpha I-alpha II helix switch?. Biochemistry. 1995; 34(50):16320-6. DOI: 10.1021/bi00050a012. View

20.

Cherry R, Godfrey R . Anisotropic rotation of bacteriorhodopsin in lipid membranes. Comparison of theory with experiment. Biophys J. 1981; 36(1):257-76. PMC: 1327587. DOI: 10.1016/S0006-3495(81)84727-3. View