Nonlinear Optical Investigation of Microbial Chromoproteins

Krekic, Szilvia; Zakar, Tomáš; Gombos, Zoltán; Valkai, Sándor; Mero, Mark; Zimányi, László; Heiner, Zsuzsanna; Dér, András

doi:10.3389/fpls.2020.547818

Cited by 8 publications

(16 citation statements)

References 73 publications

(100 reference statements)

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“…The significant changes of the measuring light level between the light and dark periods indicate that all-optical switching works properly (Figure 3) and that the bias point at 4 V heating voltage suffered only negligible drift. According to a brief interpretation of the observed phenomena based on a simplified reaction scheme of the PYP photocycle (Figure 1b), a steady-state equilibrium between the ground state (pG) and the rate-limiting intermediate (pB) was formed about 2 s after excitation, in accordance with our earlier results [11], establishing a corresponding refractive index change of the protein-film adlayer (Figure S2c). After another 2 s of the dark period, most of the protein returned to the ground state, which, upon re-excitation, yielded the same signal as when exciting the sample for the first time (Figure 3), demonstrating the repeatability of switching.…”

Section: Demonstration Of All-optical Switchingsupporting

confidence: 88%

“…The preparation method for PYP has been discussed elsewhere [10,11], but a brief summary will be given here as well. To prevent the cracking of the PYP films, 87% glycerol solution was added to the protein solution at 1:49 ratio.…”

Section: Pyp Sample Preparationmentioning

confidence: 99%

“…To prevent the cracking of the PYP films, 87% glycerol solution was added to the protein solution at 1:49 ratio. It was then allowed to dry in a laboratory environment (33% RH, 20 • C) for at least 24 h. By using glycerol as a ballast material, we secured the relative humidity inside the sample at ~80%, still allowing for the photocycle to take place [10,11].…”

Section: Pyp Sample Preparationmentioning

confidence: 99%

“…The application of biological materials is appealing because of their easy availability and exceptional NLO properties [8]. Recently, another light-sensitive biomaterial, the photoactive yellow protein (PYP) [9,10], has garnered interest for IO applications because of its fast photocycle in solution and its large light-induced refractive index change in dried films [11]. PYP, being water-soluble and smaller than the bR membrane patches used previously, potentially enables its combination with special IO passive elements where the application of bR is not possible (e.g., in porous silicon structures).…”

Section: Introductionmentioning

confidence: 99%

“…PYP, being water-soluble and smaller than the bR membrane patches used previously, potentially enables its combination with special IO passive elements where the application of bR is not possible (e.g., in porous silicon structures). Based on our previous experiments, the PYP in film form could be a viable option for all-optical switching experiments, as adding glycerol to the protein solution before drying the film helps maintain the integrity of the photocycle even in low humidity environments, allowing for the formation of the intermediate states [12], which accompanies refractive index changes of the film [11]. The photocycle of PYP consists of two main intermediates, the redshifted pR and the blue-shifted pB (further distinguishing pR 1 , pR 2 , pB 1 and pB 2 ) [10].…”

Section: Introductionmentioning

confidence: 99%

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All-Optical Switching Demonstrated with Photoactive Yellow Protein Films

et al. 2021

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Integrated optics (IO) is a field of photonics which focuses on manufacturing circuits similar to those in integrated electronics, but that work on an optical basis to establish means of faster data transfer and processing. Currently, the biggest task in IO is finding or manufacturing materials with the proper nonlinear optical characteristics to implement as active components in IO circuits. Using biological materials in IO has recently been proposed, the first material to be investigated for this purpose being the protein bacteriorhodopsin; however, since then, other proteins have also been considered, such as the photoactive yellow protein (PYP). In our current work, we directly demonstrate the all-optical switching capabilities of PYP films combined with an IO Mach–Zehnder interferometer (MZI) for the first time. By exploiting photoreactions in the reaction cycle of PYP, we also show how a combination of exciting light beams can introduce an extra degree of freedom to control the operation of the device. Based on our results, we discuss how the special advantages of PYP can be utilized in future IO applications.

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Section: Demonstration Of All-optical Switchingsupporting

confidence: 88%

Section: Pyp Sample Preparationmentioning

confidence: 99%

Section: Pyp Sample Preparationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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All-Optical Switching Demonstrated with Photoactive Yellow Protein Films

et al. 2021

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Ultrafast All-Optical Switching Using Doped Chromoprotein Films

et al. 2023

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Next-generation communication networks require > Tbit/s single-channel data transfer and processing with subpicosecond switches and routers at network nodes. Materials enabling ultrafast all-optical switching have high potential to solve the speed limitations of current optoelectronic circuits. Chromoproteins exhibit a large light-controlled refractive index change alleviating the driving energy requirements for optical switching. Here, we report femtosecond transient grating experiments demonstrating the feasibility of < 200 fs all-optical switching by hydrated thin films of photoactive yellow protein and compare the results with those obtained using bacteriorhodopsin. Possibilities for the practical utilization of the scheme in extremely highspeed optical modulation and switching/routing with nominally infinite extinction contrast are discussed.

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Linear and thermo-optically generated nonlinear optical response of bovine serum albumin and its constituent amino acids in continuous wave z-scan

et al. 2023

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Proteins are large biomolecules in the form of polypeptide chains consisting of amino acid (AA) residues. Ultraviolet–visible absorption spectroscopy and continuous wave (CW) z-scan of bovine serum albumin (BSA) and some of its constituent AAs were examined to deduce the relationship between the optical properties of this protein molecule and its constituents. From the analysis of their optical spectra, the absorption at 278 nm by BSA is found to be the outcome of the cumulative effects of the absorptions by constituent aromatic AA residues, cysteine disulfide bonds, and methionine. Similarly, the closed aperture CW z-scan of BSA and those of the constituent AAs at 74–106 mW incident optical power at 655 nm indicate that thermally generated third-order optical effects arise in BSA and its aromatic AA residues due to multiphoton absorptions. The nonlinear optical (NLO) responses of BSA and those of the AA residues are compared in terms of their molar phase shift per unit power, which indicate a possible relationship between the NLO property of BSA and its AA residues.

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Nonlinear Optical Investigation of Microbial Chromoproteins

Cited by 8 publications

References 73 publications

All-Optical Switching Demonstrated with Photoactive Yellow Protein Films

All-Optical Switching Demonstrated with Photoactive Yellow Protein Films

Ultrafast All-Optical Switching Using Doped Chromoprotein Films

Linear and thermo-optically generated nonlinear optical response of bovine serum albumin and its constituent amino acids in continuous wave z-scan

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