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      Nonlinear Optical Investigation of Microbial Chromoproteins

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          Abstract

          Membrane-bound or cytosolic light-sensitive proteins, playing a crucial role in energy- and signal-transduction processes of various photosynthetic microorganisms, have been optimized for sensing or harvesting light by myriads of years of evolution. Upon absorption of a photon, they undergo a usually cyclic reaction series of conformations, and the accompanying spectro-kinetic events assign robust nonlinear optical (NLO) properties for these chromoproteins. During recent years, they have attracted a considerable interest among researchers of the applied optics community as well, where finding the appropriate NLO material for a particular application is a pivotal task. Potential applications have emerged in various branches of photonics, including optical information storage and processing, higher-harmonic and white-light continuum generation, or biosensorics. In our earlier work, we also raised the possibility of using chromoproteins, such as bacteriorhodopsin (bR), as building blocks for the active elements of integrated optical (IO) circuits, where several organic and inorganic photonic materials have been considered as active components, but so far none of them has been deemed ideal for the purpose. In the current study, we investigate the linear and NLO properties of biofilms made of photoactive yellow protein (PYP) and bR. The kinetics of the photoreactions are monitored by time-resolved absorption experiments, while the refractive index of the films and its light-induced changes are measured using the Optical Waveguide Lightmode Spectroscopy (OWLS) and Z-scan techniques, respectively. The nonlinear refractive index and the refractive index change of both protein films were determined in the green spectral range in a wide range of intensities and at various laser repetition rates. The nonlinear refractive index and refractive index change of PYP were compared to those of bR, with respect to photonics applications. Our results imply that the NLO properties of these proteins make them promising candidates for utilization in applied photonics, and they should be considered as valid alternatives for active components of IO circuits.

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          Sensitive measurement of optical nonlinearities using a single beam

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            Time-resolved serial crystallography captures high-resolution intermediates of photoactive yellow protein.

            Serial femtosecond crystallography using ultrashort pulses from x-ray free electron lasers (XFELs) enables studies of the light-triggered dynamics of biomolecules. We used microcrystals of photoactive yellow protein (a bacterial blue light photoreceptor) as a model system and obtained high-resolution, time-resolved difference electron density maps of excellent quality with strong features; these allowed the determination of structures of reaction intermediates to a resolution of 1.6 angstroms. Our results open the way to the study of reversible and nonreversible biological reactions on time scales as short as femtoseconds under conditions that maximize the extent of reaction initiation throughout the crystal.
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              On-chip signal processing

              Rachel Won (2011)
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                Author and article information

                Contributors
                Journal
                Front Plant Sci
                Front Plant Sci
                Front. Plant Sci.
                Frontiers in Plant Science
                Frontiers Media S.A.
                1664-462X
                21 October 2020
                2020
                : 11
                : 547818
                Affiliations
                [1] 1Institute of Biophysics, Biological Research Centre , Szeged, Hungary
                [2] 2Doctoral School of Multidisciplinary Medical Sciences, University of Szeged , Szeged, Hungary
                [3] 3Institute of Plant Biology, Biological Research Centre , Szeged, Hungary
                [4] 4Max Born Institute for Nonlinear Optics and Short Pulse Spectroscopy , Berlin, Germany
                [5] 5School of Analytical Sciences Adlershof, Humboldt-Universität zu Berlin , Berlin, Germany
                Author notes

                Edited by: Michael Hippler, University of Münster, Germany

                Reviewed by: Heiko Lokstein, Charles University, Czechia; Dimitris Petroutsos, UMR 5168 Laboratoire de Physiologie Cellulaire Vegetale (LPCV), France

                *Correspondence: Zsuzsanna Heiner, heinerzs@ 123456hu-berlin.de

                Present address: Tomás Zakar, Institute of Photonics and Electronics, The Czech Academy of Sciences, Prague, Czechia

                Deceased

                This article was submitted to Plant Physiology, a section of the journal Frontiers in Plant Science

                Article
                10.3389/fpls.2020.547818
                7609429
                d707bfc3-a730-4d1e-a6f5-107df28aaa6c
                Copyright © 2020 Krekic, Zakar, Gombos, Valkai, Mero, Zimányi, Heiner and Dér.

                This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

                History
                : 31 March 2020
                : 22 September 2020
                Page count
                Figures: 10, Tables: 1, Equations: 4, References: 78, Pages: 14, Words: 0
                Funding
                Funded by: Nemzeti Kutatási Fejlesztési és Innovációs Hivatal 10.13039/501100011019
                Categories
                Plant Science
                Original Research

                Plant science & Botany
                z-scan,bacteriorhodopsin,photoactive yellow protein,nonlinear refractive index,saturable absorption,photo-induced refractive index change

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