Femtosecond laser-induced permanent anisotropy in bacteriorhodopsin films and applications in optical data storage

Yu, Xianghua; Lei, Ming; Gao, Peng; Ma, Bo

doi:10.1080/09500340.2013.774067

Cited by 10 publications

(12 citation statements)

References 16 publications

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“…However, we estimate that the fully resonant 2-photon absorption of retinal at 535 nm is at least 2 orders of magnitude larger than the nonresonant process for Trp 10,11 . This estimate is further reinforced by the observed saturation of the nonresonant 2-photon absorption (800 nm) of retinal (bR) at 700 GW/cm 2 -to give a completely different photoproductthat is specifically exploited for optical memory 12,13 . The fully resonant 2-photon absorption of retinal (at 535 nm) would saturate at more than an order of magnitude lower peak power than observed at 800 nm, approximately where the authors see the onset of nonlinear behavior (>30 GW/cm 2 , Fig.…”

Section: The Peak Power Problemmentioning

confidence: 98%

Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin in the multiphoton regime and biological relevance

et al. 2020

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How does chemistry scale in complexity to unerringly direct biological functions? Nass Kovacs et al. have shown that bacteriorhodopsin undergoes structural changes tantalizingly similar to the expected pathway even under excessive excitation. Is the protein structure so highly evolved that it directs all deposited energy into the designed function? It is difficult to overstate the importance of having atomic structures to help shape our thinking and understanding of matter. Structural information constrains the number of possible solutions in trying to piece together a puzzle in how matter undergoes transformation from one structure to another and the associated changes in material properties 1,2. In terms of understanding biological processes, this question always reduces to how the protein structure surrounding an active site has evolved to direct chemical processes into biological functions, typically with efficiencies well beyond our current capabilities to exploit chemistry. In this respect, bacteriorhodopsin (bR) serves as a model system for understanding structurefunction relationships for membrane proteins 3-5. This system functions as a light-driven, outward proton pump, which can be triggered by light to use time resolved optical methods to watch it function in real time. Its structure is composed of seven transmembrane α-helices that are covalently bound to a photoactive retinal molecule via a lysine residue through a Schiff base linkage (Fig. 1b). Upon absorbing a photon, the retinal chromophore undergoes rapid isomerization from an all-trans to 13-cis form passing through the I 460 (charge separated), J 625 (highly twisted) and K 590 (isomerized) intermediates. The retinal isomerization acts like a push in changing the electrostatic and structural environment around the active site. These changes in turn lead to a series of cascaded protein conformational changes to facilitate the transport of a proton from the retinal Schiff base to the extracellular side of the membrane via L 550 and M 410 intermediates. The retinal then undergoes reprotonation and thermal re-isomerization through the N 560 and O 630 intermediates, respectively, where it can then return to the bR 568 ground state. These processes have been well characterized spectroscopically and many of the long-lived

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Section: The Peak Power Problemmentioning

confidence: 98%

Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin in the multiphoton regime and biological relevance

et al. 2020

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“…The goal of bR orientation technology is to orient the protein effectively and prevent the purple membrane (PM) from denaturation. Different technologies have been introduced to reconstitute bR layer on various substrates, including Langmuir–Blodgett deposition [ 77 , 78 , 79 , 80 , 81 , 82 , 83 , 84 , 85 , 86 , 87 , 88 ], electrophoretic sedimentation [ 85 , 89 , 90 , 91 ], biotin-streptavidin mediated monolayer [ 92 , 93 ], antibody-mediated monolayer [ 94 , 95 ] and electrostatic adsorption [ 22 , 96 , 97 , 98 , 99 , 100 ]. Figure 5 shows different typical PM preparation methods.…”

Section: Working Principle and Properties Of Bacteriorhodopsinmentioning

confidence: 99%

“…Most applications are based on the so-called M-type photochromic effect of bR, and the quantum efficiency is quite low, only about 0.02%, which limits its practical application and can only be used for transient optical data storage, while, in the case of bR, a light conversion product called F540 state excited by a 790 nm femtosecond laser pulse is stable for photochemical reactions or thermal pathways. Yao Baoli et al studied the optical properties of the F540 state and analyzed the photo anisotropy of the F540 state using the Jones matrix theory [ 22 ]. When the bR film is excited by a linearly polarized femtosecond laser pulse, the selection of molecules occurs.…”

Section: Photochemical Application Of Bacteriorhodopsinmentioning

confidence: 99%

“… Optical settings for polarized multiplexing write once (WORM) optical memory. Reproduced from [ 22 ]. …”

Section: Figurementioning

confidence: 99%

“…Afterwards, bR related artificial retinal prostheses were firstly proposed for the similar optical properties between bR and retinal in the retina [ 19 ]. Then, bR was applied in the field of computer systems and sensors, leading to production of optical volumetric memories [ 20 , 21 , 22 ], holographic associative processors [ 23 , 24 ] and motion biosensors [ 25 , 26 , 27 ] in the early 2000s. After that, bR was used to compound with a variety of photoelectric materials, which resulted in the generation of photovoltaic cells based on different composite material systems [ 28 , 29 , 30 , 31 , 32 , 33 , 34 ].…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

A Review on Bacteriorhodopsin-Based Bioelectronic Devices

Tian

et al. 2018

Sensors

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Bacteriorhodopsin protein extracted from Halobacterium salinarum is widely used in many biohybrid electronic devices and forms a research subject known as bioelectronics, which merges biology with electronic technique. The specific molecule structure and components of bR lead to its unique photocycle characteristic, which consists of several intermediates (bR, K, L, M, N, and O) and results in proton pump function. In this review, working principles and properties of bacteriorhodopsin are briefly introduced, as well as bR layer preparation method. After that, different bR-based devices divided into photochemical and photoelectric applications are shown. Finally, outlook and conclusions are drawn to inspire new design of high-performance bR-based biohybrid electronic devices.

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Polarization-sensitive diffractive optical elements fabricated in BR films with femtosecond laser

Lei

Hampp

et al. 2013

Appl. Phys. B

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Femtosecond laser-induced permanent anisotropy in bacteriorhodopsin films and applications in optical data storage

Cited by 10 publications

References 16 publications

Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin in the multiphoton regime and biological relevance

Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin in the multiphoton regime and biological relevance

A Review on Bacteriorhodopsin-Based Bioelectronic Devices

Polarization-sensitive diffractive optical elements fabricated in BR films with femtosecond laser

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