Action spectrum for reorientations in bacteriorhodopsin of purple membrane in suspension.

Publisher: Nature Publishing Group Country of Publication: England NLM ID: 101563288 Publication Model: Electronic Cited Medium: Internet ISSN: 2045-2322 (Electronic) Linking ISSN: 20452322 NLM ISO Abbreviation: Sci Rep Subsets: MEDLINE

Original Publication: London : Nature Publishing Group, copyright 2011-

Bacteriorhodopsins*; Purple Membrane ; Action Spectrum ; Lipids

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.
(© 2023. The Author(s).)

Sensors (Basel). 2018 Apr 27;18(5):. (PMID: 29702621)
FEBS Lett. 1977 Aug 15;80(2):465-9. (PMID: 891998)
FEBS Lett. 1999 Apr 30;450(1-2):154-7. (PMID: 10350076)
FEBS Lett. 1977;78(1):25-30. (PMID: 872937)
Nat New Biol. 1972 Mar 15;236(63):39-43. (PMID: 4537062)
Structure. 2002 Apr;10(4):515-25. (PMID: 11937056)
FEBS Lett. 1979 Dec 15;108(2):307-10. (PMID: 42560)
Biochemistry. 1991 Jan 15;30(2):394-400. (PMID: 1988038)
Biophys J. 1993 Aug;65(2):927-38. (PMID: 8218916)
Biophys J. 1985 Aug;48(2):201-8. (PMID: 4052558)
Biochim Biophys Acta. 2006 Aug;1757(8):1012-8. (PMID: 16376293)
Annu Rev Biophys Biomol Struct. 2003;32:285-310. (PMID: 12598369)
Ann Biomed Eng. 1992;20(3):269-88. (PMID: 1443824)
Biophys J. 1984 Jun;45(6):1039-49. (PMID: 6743741)
Biochemistry. 1978 Jun 13;17(12):2293-300. (PMID: 678507)
J Lipid Res. 2002 Jan;43(1):132-40. (PMID: 11792732)
Biophys Struct Mech. 1977 Jun 29;3(2):79-94. (PMID: 890059)
Biochemistry. 1983 Mar 15;22(6):1323-34. (PMID: 6838856)
Biochemistry. 1995 Dec 19;34(50):16320-6. (PMID: 8845357)
Biophys J. 1981 Oct;36(1):257-76. (PMID: 7284552)
Photochem Photobiol. 1990 Jun;51(6):793-818. (PMID: 2195566)
FEBS Lett. 1977 Oct 1;82(1):1-6. (PMID: 21098)
FEBS Lett. 2000 Sep 1;480(2-3):123-6. (PMID: 11034312)
EMBO J. 1991 Mar;10(3):521-6. (PMID: 2001671)

53026-44-1 (Bacteriorhodopsins)
0 (Lipids)

Date Created: 20230516 Date Completed: 20230518 Latest Revision: 20230606

20250114

PMC10188430

10.1038/s41598-023-35121-8

37193768