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Bacteriorhodopsin wildtype and variant aspartate-96 --> aspargine as reversible holographic media.

Abstract：

:Air dried films of purple membranes (PM) from Halobacterium halobium containing the photochromic protein bacteriorhodopsin (BR) were prepared and the BR-photocycle of this material analyzed. The absorption maxima of the initial state B (lambda(max) = 570 nm) and the photochemical intermediate M (lambda(max) = 412 nm), which is the longest living intermediate in suspension (tau approximately 10 ms), were spectrally well separated. Light-induced population gratings between B and M were used for reversible holographic recording in these dry PM films. The resolution (>5,000 lines/mm) of PM films was comparable to the corresponding values of conventional photochromic recording materials. The longterm stability toward photochemical degradation of PM films is excellent (> 100.000 recording cycles). The spectral bandwidth (400-680 nm) of such films covers nearly the whole visible spectrum. Both the photochemical transition from B --> M with wavelengths in the green-red range and from M --> B with blue light were utilized for holographic recording. The latter possibility (M --> B) seems to be advantageous for several applications because the holographic grating is only formed during reconstruction. Higher reading intensities lead to higher population of the M-state and result in an increase of the fringe contrast instead of decreasing it. New possibilities for the further development of holographic media based on bacteriorhodopsin are raised by the availability of PM variants with modified optical properties. By the use of the variant BR-326, which differs from the wildtype PM by a single amino acid exchange (aspartate-96 --> asparagine), the sensitivity of PM films is increased by approximately 50% from 12 cm(2)/J to 19 cm(2)/J for recording with 568 nm. The sensitivity for recording with 413 nm (33 cm(2)/J) is not influenced by the amino acid exchange. The observed diffraction efficiency eta of PM films with BR-326 is twice that of BR-wildtype (BR-WT) films and is in the range of conventional organic photochromics ( approximately 1%). In dried films of both BR-WT and BR-326 the M-decay was shown to be at least biexponential.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Hampp N,Bräuchle C,Oesterhelt D

doi

10.1016/S0006-3495(90)82355-9

subject

Has Abstract

pub_date

1990-07-01 00:00:00

pages

83-93

issue

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(90)82355-9

journal_volume

pub_type

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Bacteriorhodopsin wildtype and variant aspartate-96 --> aspargine as reversible holographic media.