Spatial Light Modulators And Optical Associative Memories Based On Bacteriorhodopsin

Birge, Robert R.; Fleitz, Paul A.; Gross, Richard B.; Izgi, J.C.; Lawrence, Albert F.; Stuart, Jeffrey A.; Tallent, Jack R.

doi:10.1109/iembs.1990.692019

Cited by 8 publications

(12 citation statements)

References 10 publications

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“…There may also be applications where BPR can be used, as many devices do not require cyclicities above 10 3 4,82. Most significant is the ability of the solubilized PR variants, described in this work, to maintain spectral activity for several years at the operational temperature of most electronic devices ( i.e.…”

Section: Comments and Conclusionmentioning

confidence: 98%

Photochemical and Thermal Stability of Green and Blue Proteorhodopsins: Implications for Protein-Based Bioelectronic Devices

Ranaghan

Shima²,

Ramos³

et al. 2010

J. Phys. Chem. B

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The photochemical and thermal stability of the detergent solubilized blue- and green-absorbing proteorhodpsins, BPR and GPR respectively, are investigated to determine viability of these proteins for photonic device applications. Photochemical stability is studied by using pulsed laser excitation and differential uv-vis spectroscopy to assign the photocyclicity. GPR, with a cyclicity of 7×104 photocycles protein−1, is 4–5 times more stable than BPR (9×103 photocycles protein−1), but is less stable than native bacteriorhodopsin (9×105 photocycles protein−1) or the 4-keto-bacteriorhodopsin analog (1×105 photocycles protein−1). The thermal stabilities are assigned by using differential scanning calorimetry and thermal bleaching experiments. Both proteorhodopsins display excellent thermal stability, with melting temperatures above 85°C, and remain photochemically stable up to 75°C. The biological relevance of our results is also discussed. The lower cyclicity of BPR is found to be adequate for the long-term biological function of the host organism at ocean depths of 50 m or more.

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Section: Comments and Conclusionmentioning

confidence: 98%

Photochemical and Thermal Stability of Green and Blue Proteorhodopsins: Implications for Protein-Based Bioelectronic Devices

Ranaghan

Shima²,

Ramos³

et al. 2010

J. Phys. Chem. B

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“…At the time, interest in pursuing bioelectronic devices was tied to military development and international competition towards designing new nanobiotechnologies, which had first elicited a holographic processor based on BR thin films through the project, Biochrome [80,81]. In the subsequent decades of research, BR has emerged as one of the most rigorously investigated biomaterial for use in electronic applications, culminating in the development of numerous prototypes of devices that include Fouriertransform holographic associative processors [25,42,[82][83][84], three-dimensional optical memories [25,82,85,86], biosensors [87,88], photovoltaic cells [89][90][91] and protein-based retinal prostheses [28,92]. Recent advances in genetic engineering and directed evolution have further invigorated the pursuit of optimizing these protein-based devices, thereby increasing the potential of introducing a commercial BR-based technology in the near future [38,41,76].…”

Section: Biophotonic Device Applications Of Bacteriorhodopsinmentioning

confidence: 99%

“…Because of this functional paradigm, associative processors are often considered a target design for the development of true artificial intelligence [95]. Fourier-transform holographic optical loops, which were first proposed by Paek and Psaltis, have long been considered an optimal architecture necessary to realize the implementation of this memory class [84,[96][97][98]. Bunkin et al [80] had first proposed thin films of BR as a viable medium for the technology owing to the inherent holographic and photochromic properties of the photoactive protein.…”

Section: Holographic Associative Processorsmentioning

confidence: 99%

Directed evolution of bacteriorhodopsin for applications in bioelectronics

Wagner

Greco

Ranaghan

et al. 2013

J. R. Soc. Interface.

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In nature, biological systems gradually evolve through complex, algorithmic processes involving mutation and differential selection. Evolution has optimized biological macromolecules for a variety of functions to provide a comparative advantage. However, nature does not optimize molecules for use in human-made devices, as it would gain no survival advantage in such cooperation. Recent advancements in genetic engineering, most notably directed evolution, have allowed for the stepwise manipulation of the properties of living organisms, promoting the expansion of protein-based devices in nanotechnology. In this review, we highlight the use of directed evolution to optimize photoactive proteins, with an emphasis on bacteriorhodopsin (BR), for device applications. BR, a highly stable light-activated proton pump, has shown great promise in three-dimensional optical memories, real-time holographic processors and artificial retinas.

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“…BR can remain in the Q state for 7 to 12 years and then returns to its normal bR state upon red photon illumination (Stuart et al ., , ). These unique features coupled with high stability make BR a versatile biological material with numerous potential attractive applications in photovoltaic cells (Hong, ; Xu et al ., ; Chellamuthu et al ., ), artificial retina (Chen and Birge, ; Cutsuridis and Wennekers, ), biosensors (Boucher et al ., ; Lanyi and Luecke, ), optical memory storage devices (Birge et al ., , ; Stuart et al ., , ) and optogenetics (Lindvold and Lausen, ; Fábián et al ., ). Several attempts to recombinantly express H. salinarum BR using E. coli as a host have been reported.…”

Section: Introductionmentioning

confidence: 99%

Discovery of bacteriorhodopsins in Haloarchaeal species isolated from Indian solar salterns: deciphering the role of the N‐terminal residues in protein folding and functional expression

Verma

Baral

Kumar

et al. 2019

Microbial Biotechnology

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Summary Interesting optical and photochemical properties make microbial rhodopsin a promising biological material suitable for various applications, but the cost‐prohibitive nature of production has limited its commercialization. The aim of this study was to explore the natural biodiversity of Indian solar salterns to isolate natural bacteriorhodopsin ( BR ) variants that can be functionally expressed in Escherichia coli . In this study, we report the isolation, functional expression and purification of BR s from three pigmented haloarchaea, wsp3 (water sample Pondicherry), wsp5 and K1 T isolated from two Indian solar salterns. The results of the 16S rRNA data analysis suggest that wsp3, wsp5 and K1 T are novel strains belonging to the genera Halogeometricum, Haloferax and Haloarcula respectively. Overall, the results of our study suggest that 17 N‐terminal residues, that were not included in the gene annotation of the close sequence homologues, are essential for functional expression of BR s. The primary sequence, secondary structural content, thermal stability and absorbance spectral properties of these recombinant BR s are similar to those of the previously reported Haloarcula marismortui Hm BRI . This study demonstrates the cost‐effective, functional expression of BR s isolated from haloarchaeal species using E. coli as an expression host and paves the way for feasibility studies for future applications.

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Spatial Light Modulators And Optical Associative Memories Based On Bacteriorhodopsin

Cited by 8 publications

References 10 publications

Photochemical and Thermal Stability of Green and Blue Proteorhodopsins: Implications for Protein-Based Bioelectronic Devices

Photochemical and Thermal Stability of Green and Blue Proteorhodopsins: Implications for Protein-Based Bioelectronic Devices

Directed evolution of bacteriorhodopsin for applications in bioelectronics

Discovery of bacteriorhodopsins in Haloarchaeal species isolated from Indian solar salterns: deciphering the role of the N‐terminal residues in protein folding and functional expression

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