Abstract
Nature has evolved through billions of years to achieve highly efficient biological processes and materials with properties that go, most of the time, far beyond the current human know-how. Not only to deeply understand these selective systems, but also to gain inspiration for the design of new processes and materials with similar behavior, the principles of biomimicry and bioinspiration have been applied by the scientific community and the industry. The general strategy for that is firstly, through scientific analysis, systematize the fundamental mechanisms that underlie a particular biological process, and then apply these concepts in the fabrication of novel biomimetic/bioinspired materials with enhanced performance. The inspiration coming from natural sources can be structure-wise and/or function-wise and, in the recent years, has had a significant impact on the bioelectrochemistry field, as most of the available electrochemical techniques are useful tools to investigate these systems. This chapter discusses the recent trends in biomimicry and bioinspiration in the bioelectrochemistry field, mainly focusing on biomimetic membranes, reconstituted membrane proteins, protein-based electrodes, biomimetic enzymes, genetic materials, and live cells.
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Naik, R.R., Singamaneni, S.: Introduction: bioinspired and biomimetic materials. Chem. Rev. 117, 12581–12583 (2017). https://doi.org/10.1021/acs.chemrev.7b00552
Suresh Kumar, N., Padma Suvarna, R., Chandra Babu Naidu, K., Banerjee, P., Ratnamala, A., Manjunatha, H.: A review on biological and biomimetic materials and their applications. Appl. Phys. A Mater. Sci. Process. 126 (2020). https://doi.org/10.1007/s00339-020-03633-z
Wegst, U.G.K., Bai, H., Saiz, E., Tomsia, A.P., Ritchie, R.O.: Bioinspired structural materials. Nat. Mater. 14, 23–36 (2015). https://doi.org/10.1038/nmat4089
Vullev, V.I.: From biomimesis to bioinspiration: what’s the benefit for solar energy conversion applications? J. Phys. Chem. Lett. 2, 503–508 (2011). https://doi.org/10.1021/jz1016069
Naleway, S.E., Porter, M.M., McKittrick, J., Meyers, M.A.: structural design elements in biological materials: application to bioinspiration. Adv. Mater. 27, 5455–5476 (2015). https://doi.org/10.1002/adma.201502403
Wang, Y., Naleway, S.E., Wang, B.: Biological and bioinspired materials: structure leading to functional and mechanical performance. Bioact. Mater. 5, 745–757 (2020). https://doi.org/10.1016/j.bioactmat.2020.06.003
Sharma, S., Sarkar, P.: Biomimicry: exploring research, challenges, gaps, and tools. In: Chakrabarti, A. (eds.) Research into Design for a Connected World. Smart Innovation, Systems and Technologies, vol. 134, pp 87–97. Springer, Singapore (2019)
Swiegers, G.F.: Bioinspiration and Biomimicry in Chemistry: Reverse-Engineering Nature. Wiley, Hoboken, NJ (2012)
Thanigaiarasu, P.: Biomimetics in the design of medical devices. In: Sahnmugam, P.S.T., Chokkalingam, L., Bakthavachalam, P. (eds.) Trends in Development of Medical Devices, 1st edn. Elsevier, London (2020)
Ricke, J.: Biomimetic chemistry at interfaces. In: Ball, V. (ed.) Self-Assembly Processes at Interfaces: Multiscale Phenomena, 1st edn. Elsevier, London (2017)
Martín-Palma, R.J., Lakhtakia, A.: Progress on bioinspired, biomimetic, and bioreplication routes to harvest solar energy. Appl. Phys. Rev. 4 (2017). https://doi.org/10.1063/1.4981792
Yin, X., Müller, R.: Integration of deep learning and soft robotics for a biomimetic approach to nonlinear sensing. Nat. Mach. Intell. 3, 507–512 (2021). https://doi.org/10.1038/s42256-021-00330-1
Pawlyn, M.: Biomimicry in Architecture, 2nd edn. RIBA Publishing, Newcastle (2016)
Park, E.-Y.: Body painting type analysis based on biomimicry camouflage. Int. J. Archit. Arts. Appl. 6, 1–11 (2020). https://doi.org/10.11648/j.ijaaa.20200601.11
Lepora, N.F., Verschure, P., Prescott, T.J.: The state of the art in biomimetics. Bioinspiration and Biomimetics 8 (2013). https://doi.org/10.1088/1748-3182/8/1/013001
de Souza, J.C.P., Macedo, L.J.A., Hassan, A., Sedenho, G.C., Modenez, I.A., Crespilho, F.N.: In situ and operando techniques for investigating electron transfer in biological systems. ChemElectroChem 8, 431–446 (2021). https://doi.org/10.1002/celc.202001327
Nieciecka, D., Królikowska, A., Krysinski, P.: Probing the interactions of mitoxantrone with biomimetic membranes with electrochemical and spectroscopic techniques. Electrochim. Acta 165, 430–442 (2015). https://doi.org/10.1016/j.electacta.2015.02.223
Guidelli, R.: Bioelectrochemistry of Biomembranes and Biomimetic Membranes, 1st edn. Wiley, Hoboken, NJ (2017)
Bondar, A.N., Lemieux, M.J.: Reactions at biomembrane interfaces. Chem. Rev. 119, 6162–6183 (2019). https://doi.org/10.1021/acs.chemrev.8b00596
Lipkowski, J.: Biomimetics: a new research opportunity for surface electrochemistry. J. Solid State Electrochem. 24, 2121–2123 (2020). https://doi.org/10.1007/s10008-020-04627-w
Luchini, A., Vitiello, G.: Mimicking the mammalian plasma membrane: an overview of lipid membrane models for biophysical studies. Biomimetics 6, 1–18 (2021). https://doi.org/10.3390/biomimetics6010003
Su, Z.F., Leitch, J.J., Lipkowski, J.: Electrode-supported biomimetic membranes: an electrochemical and surface science approach for characterizing biological cell membranes. Curr. Opin. Electrochem. 12, 60–72 (2018). https://doi.org/10.1016/j.coelec.2018.05.020
Blank, M., Miller, I.R.: Transport of ions across lipid monolayers. I. The structure of decylammonium monolayers at the polarized mercury-water interface. J. Colloid Interface Sci. 26, 26–33 (1968). https://doi.org/10.1016/0021-9797(68)90267-1
Sanver, D., Murray, B.S., Sadeghpour, A., Rappolt, M., Nelson, A.L.: Experimental modeling of flavonoid-biomembrane interactions. Langmuir 32, 13234–13243 (2016). https://doi.org/10.1021/acs.langmuir.6b02219
Rashid, A., Vakurov, A., Mohamadi, S., Sanver, D., Nelson, A.: Substituents modulate biphenyl penetration into lipid membranes. Biochim. Biophys. Acta – Biomembr. 1859, 712–721 (2017). https://doi.org/10.1016/j.bbamem.2017.01.023
Vakurov, A., Drummond-Brydson, R., Ugwumsinachi, O., Nelson, A.: Significance of particle size and charge capacity in TiO2 nanoparticle-lipid interactions. J. Colloid Interface Sci. 473, 75–83 (2016). https://doi.org/10.1016/j.jcis.2016.03.045
Levine, Z.A., Denardis, N.I., Vernier, P.T.: Phospholipid and hydrocarbon interactions with a charged electrode interface. Langmuir 32, 2808–2819 (2016). https://doi.org/10.1021/acs.langmuir.5b04090
Pawłowski, J., Juhaniewicz, J., Güzeloʇlu, A., Sek, S.: Mechanism of lipid vesicles spreading and bilayer formation on a Au(111) surface. Langmuir 31, 11012–11019 (2015). https://doi.org/10.1021/acs.langmuir.5b01331
Pawłowski, J., Dziubak, D., Sęk, S.: Potential-driven changes in hydration of chitosan-derived molecular films on gold electrodes. Electrochim. Acta 319, 606–614 (2019). https://doi.org/10.1016/j.electacta.2019.07.021
Prieto, F., Rueda, M., Naitlho, N., Vázquez-González, M., González-Rodríguez, M.L., Rabasco, A.M.: Electrochemical characterization of a mixed lipid monolayer supported on Au(111) electrodes with implications for doxorubicin delivery. J. Electroanal. Chem. 815, 246–254 (2018). https://doi.org/10.1016/j.jelechem.2018.02.056
Konarzewska, D., Juhaniewicz, J., Güzeloğlu, A., Sęk, S.: Characterization of planar biomimetic lipid films composed of phosphatidylethanolamines and phosphatidylglycerols from Escherichia coli. Biochim. Biophys. Acta – Biomembr. 1859, 475–483 (2017). https://doi.org/10.1016/j.bbamem.2017.01.010
Juhaniewicz-Dębińska, J., Tymecka, D., Sęk, S.: Lipopeptide-induced changes in permeability of solid supported bilayers composed of bacterial membrane lipids. J. Electroanal. Chem. 812, 227–234 (2018). https://doi.org/10.1016/j.jelechem.2017.12.065
Juhaniewicz, J., Szyk-Warszyńska, L., Warszyński, P., Sek, S.: Interaction of cecropin B with zwitterionic and negatively charged lipid bilayers immobilized at gold electrode surface. Electrochim. Acta 204, 206–217 (2016). https://doi.org/10.1016/j.electacta.2016.04.080
Pieta, P., Majewska, M., Su, Z., Grossutti, M., Wladyka, B., Piejko, M., Lipkowski, J., Mak, P.: Physicochemical studies on orientation and conformation of a new bacteriocin BacSp222 in a planar phospholipid bilayer. Langmuir 32, 5653–5662 (2016). https://doi.org/10.1021/acs.langmuir.5b04741
Su, H., Liu, H.Y., Pappa, A.M., Hidalgo, T.C., Cavassin, P., Inal, S., Owens, R.M., Daniel, S.: Facile generation of biomimetic-supported lipid bilayers on conducting polymer surfaces for membrane biosensing. ACS Appl. Mater. Interfaces 11, 43799–43810 (2019). https://doi.org/10.1021/acsami.9b10303
Alvarez-Malmagro, J., Jablonowska, E., Nazaruk, E., Szwedziak, P., Bilewicz, R.: How do lipid nanocarriers—cubosomes affect electrochemical properties of DMPC bilayers deposited on gold (111) electrodes? Bioelectrochemistry 134 (2020). https://doi.org/10.1016/j.bioelechem.2020.107516
Gao, T., Liu, F., Yang, D., Yu, Y., Wang, Z., Li, G.: Assembly of selective biomimetic surface on an electrode surface: a design of nano-bio interface for biosensing. Anal. Chem. 87, 5683–5689 (2015). https://doi.org/10.1021/acs.analchem.5b00816
Madrid, E., Horswell, S.L.: The electrochemical phase behaviour of chemically asymmetric lipid bilayers supported at Au(111) electrodes. J. Electroanal. Chem. 819, 338–346 (2018). https://doi.org/10.1016/j.jelechem.2017.11.006
Andersson, J., Köper, I.: Tethered and polymer supported bilayer lipid membranes: structure and function. Membranes (Basel) 6 (2016). https://doi.org/10.3390/membranes6020030
Wiebalck, S., Kozuch, J., Forbrig, E., Tzschucke, C.C., Jeuken, L.J.C., Hildebrandt, P.: Monitoring the transmembrane proton gradient generated by cytochrome bo3 in tethered bilayer lipid membranes using SEIRA spectroscopy. J. Phys. Chem. B 120, 2249–2256 (2016). https://doi.org/10.1021/acs.jpcb.6b01435
Andersson, J., Fuller, M.A., Wood, K., Holt, S.A., Köper, I.: A tethered bilayer lipid membrane that mimics microbial membranes. Phys. Chem. Chem. Phys. 20, 12958–12969 (2018). https://doi.org/10.1039/c8cp01346b
Zhou, W., Burke, P.J.: Versatile bottom-up synthesis of tethered bilayer lipid membranes on nanoelectronic biosensor devices. ACS Appl. Mater. Interfaces 9, 14618–14632 (2017). https://doi.org/10.1021/acsami.7b00268
Su, Z., Juhaniewicz-Debinska, J., Sek, S., Lipkowski, J.: Water structure in the submembrane region of a floating lipid bilayer: the effect of an ion channel formation and the channel blocker. Langmuir 36, 409–418 (2020). https://doi.org/10.1021/acs.langmuir.9b03271
Abbasi, F., Leitch, J.J., Su, Z.F., Szymanski, G., Lipkowski, J.: Direct visualization of alamethicin ion pores formed in a floating phospholipid membrane supported on a gold electrode surface. Electrochim. Acta 267, 195–205 (2018). https://doi.org/10.1016/j.electacta.2018.02.057
Abbasi, F., Su, Z.F., Alvarez-Malmagro, J., Leitch, J.J., Lipkowski, J.: Effects of amiloride, an ion channel blocker, on alamethicin pore formation in negatively charged, gold-supported, phospholipid bilayers: a molecular view. Langmuir 35, 5060–5068 (2019). https://doi.org/10.1021/acs.langmuir.9b00187
Ryu, H., Fuwad, A., Yoon, S., Jang, H., Lee, J.C., Kim, S.M., Jeon, T.J.: Biomimetic membranes with transmembrane proteins: state-of-the-art in transmembrane protein applications. Int. J. Mol. Sci. 20 (2019). https://doi.org/10.3390/ijms20061437
Kim, Y.H., Hang, L., Cifelli, J.L., Sept, D., Mayer, M., Yang, J.: Frequency-based analysis of gramicidin A nanopores enabling detection of small molecules with picomolar sensitivity. Anal. Chem. 90, 1635–1642 (2018). https://doi.org/10.1021/acs.analchem.7b02961
Park, J., Lim, M.C., Ryu, H., Shim, J., Kim, S.M., Kim, Y.R., Jeon, T.J.: Nanopore based detection of: Bacillus thuringiensis HD-73 spores using aptamers and versatile DNA hairpins. Nanoscale 10, 11955–11961 (2018). https://doi.org/10.1039/c8nr03168a
Zieleniecki, J.L., Nagarajan, Y., Waters, S., Rongala, J., Thompson, V., Hrmova, M., Köper, I.: Cell-free synthesis of a functional membrane transporter into a tethered bilayer lipid membrane. Langmuir 32, 2445–2449 (2016). https://doi.org/10.1021/acs.langmuir.5b04059
Steininger, C., Reiner-Rozman, C., Schwaighofer, A., Knoll, W., Naumann, R.L.C.: Kinetics of cytochrome c oxidase from R. sphaeroides initiated by direct electron transfer followed by tr-SEIRAS. Bioelectrochemistry 112, 1–8 (2016). https://doi.org/10.1016/j.bioelechem.2016.06.005
Karaballi, R.A., Merchant, S., Power, S.R., Brosseau, C.L.: Electrochemical surface-enhanced Raman spectroscopy (EC-SERS) study of the interaction between protein aggregates and biomimetic membranes. Phys. Chem. Chem. Phys. 20, 4513–4526 (2018). https://doi.org/10.1039/c7cp06838g
Gutiérrez-Sanz, Ó., Tapia, C., Marques, M.C., Zacarias, S., Vélez, M., Pereira, I.A.C., De Lacey, A.L.: Induction of a proton gradient across a gold-supported biomimetic membrane by electroenzymatic H2 oxidation. Angew. Chemie. Int. Ed. 54, 2684–2687 (2015). https://doi.org/10.1002/anie.201411182
Gutiérrez-Sanz, Ó., Natale, P., Márquez, I., Marques, M.C., Zacarias, S., Pita, M., Pereira, I.A.C., López-Montero, I., De Lacey, A.L., Vélez, M.: H2-fueled ATP synthesis on an electrode: mimicking cellular respiration. Angew. Chemie. Int. Ed. 55, 6216–6220 (2016). https://doi.org/10.1002/anie.201600752
García-Molina, G., Natale, P., Valenzuela, L., Alvarez-Malmagro, J., Gutiérrez-Sánchez, C., Iglesias-Juez, A., López-Montero, I., Vélez, M., Pita, M., De Lacey, A.L. Potentiometric detection of ATP based on the transmembrane proton gradient generated by ATPase reconstituted on a gold electrode. Bioelectrochemistry 133 (2020). https://doi.org/10.1016/j.bioelechem.2020.107490
Niroomand, H., Pamu, R., Mukherjee, D., Khomami, B.: Microenvironment alterations enhance photocurrents from photosystem i confined in supported lipid bilayers. J. Mater. Chem. A 6, 12281–12290 (2018). https://doi.org/10.1039/c8ta00898a
Heath, G.R., Li, M., Rong, H., Radu, V., Frielingsdorf, S., Lenz, O., Butt, J.N., Jeuken, L.J.C.: Multilayered lipid membrane stacks for biocatalysis using membrane enzymes. Adv. Funct. Mater. 27 (2017). https://doi.org/10.1002/adfm.201606265
Mazurenko, I., Hitaishi, V.P., Lojou, E.: Recent advances in surface chemistry of electrodes to promote direct enzymatic bioelectrocatalysis. Curr. Opin. Electrochem. 19, 113–121 (2020). https://doi.org/10.1016/j.coelec.2019.11.004
Milton, R.D., Minteer, S.D.: Direct enzymatic bioelectrocatalysis: differentiating between myth and reality. J. R. Soc. Interface 14 (2017). https://doi.org/10.1098/rsif.2017.0253
Saboe, P.O., Conte, E., Farell, M., Bazan, G.C., Kumar, M.: Biomimetic and bioinspired approaches for wiring enzymes to electrode interfaces. Energy Environ. Sci. 10, 14–42 (2017). https://doi.org/10.1039/c6ee02801b
Pereira, A.R., Sedenho, G.C., de Souza, J.C.P., Crespilho, F.N.: Advances in enzyme bioelectrochemistry. An. Acad. Bras. Cienc. 90, 825–857 (2018). https://doi.org/10.1590/0001-3765201820170514
Chowdhury, R., Stromer, B., Pokharel, B., Kumar, C.V.: Control of enzyme-solid interactions via chemical modification. Langmuir 28, 11881–11889 (2012). https://doi.org/10.1021/la3022003
Efrati, A., Lu, C.-H., Michaeli, D., Nechushtai, R., Alsaoub, S., Schuhmann, W., Willner, I.: Assembly of photo-bioelectrochemical cells using photosystem I-functionalized electrodes. Nat. Energy 1, 1–8 (2016). https://doi.org/10.1038/nenergy.2015.21
Zhang, J.Z., Sokol, K.P., Paul, N., Romero, E., Van Grondelle, R., Reisner, E.: Competing charge transfer pathways at the photosystem II-electrode interface. Nat. Chem. Biol. 12, 1046–1052 (2016). https://doi.org/10.1038/nchembio.2192
Herzallh, N.S., Cohen, Y., Mukha, D., Neumann, E., Michaeli, D., Nechushtai, R., Yehezkeli, O.: Photosynthesis Z-Scheme biomimicry: photosystem I/BiVO4 photo-bioelectrochemical cell for donor-free bias-free electrical power generation. Biosens. Bioelectron. 168, 112517 (2020). https://doi.org/10.1016/j.bios.2020.112517
Yu, W., Zhang, S., Chen, J., Xia, P., Richter, M.H., Chen, L., Xu, W., Jin, J., Chen, S., Peng, T.: Biomimetic Z-scheme photocatalyst with a tandem solid-state electron flow catalyzing H2 evolution. J. Mater. Chem. A 6, 15668–15674 (2018). https://doi.org/10.1039/c8ta02922a
Li, Z., Wang, W., Ding, C., Wang, Z., Liao, S., Li, C.: Biomimetic electron transport via multiredox shuttles from photosystem II to a photoelectrochemical cell for solar water splitting. Energy Environ. Sci. 10, 765–771 (2017). https://doi.org/10.1039/c6ee03401b
Sokol, K.P., Robinson, W.E., Warnan, J., Kornienko, N., Nowaczyk, M.M., Ruff, A., Zhang, J.Z., Reisner, E.: Bias-free photoelectrochemical water splitting with photosystem II on a dye-sensitized photoanode wired to hydrogenase. Nat Energy 3, 944–951 (2018). https://doi.org/10.1038/s41560-018-0232-y
Ing, N.L., Nusca, T.D., Hochbaum, A.I.: Geobacter sulfurreducens pili support ohmic electronic conduction in aqueous solution. Phys. Chem. Chem. Phys. 19, 21791–21799 (2017). https://doi.org/10.1039/c7cp03651e
Altamura, L., Horvath, C., Rengaraj, S., Rongier, A., Elouarzaki, K., Gondran, C., Maçon, A.L.B., Vendrely, C., Bouchiat, V., Fontecave, M., Mariolle, D., Rannou, P., Le Goff, A., Duraffourg, N., Holzinger, M., Forge, V.: A synthetic redox biofilm made from metalloprotein-prion domain chimera nanowires. Nat. Chem. 9, 157–163 (2017). https://doi.org/10.1038/NCHEM.2616
Ing, N.L., Spencer, R.K., Luong, S.H., Nguyen, H.D., Hochbaum, A.I.: Electronic conductivity in biomimetic α-helical peptide nanofibers and gels. ACS Nano 12, 2652–2661 (2018). https://doi.org/10.1021/acsnano.7b08756
Creasey, R.C.G., Mostert, A.B., Solemanifar, A., Nguyen, T.A.H., Virdis, B., Freguia, S., Laycock, B.: Biomimetic peptide nanowires designed for conductivity. ACS Omega 4, 1748–1756 (2019). https://doi.org/10.1021/acsomega.8b02231
Vázquez-González, M., Liao, W.C., Cazelles, R., Wang, S., Yu, X., Gutkin, V., Willner, I.: Mimicking horseradish peroxidase functions using Cu2+-modified carbon nitride nanoparticles or Cu2+-modified carbon dots as heterogeneous catalysts. ACS Nano 11, 3247–3253 (2017). https://doi.org/10.1021/acsnano.7b00352
Kluenker, M., Nawaz Tahir, M., Ragg, R., Korschelt, K., Simon, P., Gorelik, T.E., Barton, B., Shylin, S.I., Panthöfer, M., Herzberger, J., Frey, H., Ksenofontov, V., Möller, A., Kolb, U., Grin, J., Tremel, W.: Pd@Fe2O3 superparticles with enhanced peroxidase activity by solution phase epitaxial growth. Chem. Mater. 29, 1134–1146 (2017). https://doi.org/10.1021/acs.chemmater.6b04283
Sang, J., Wu, R., Guo, P., Du, J., Xu, S., Wang, J.: Affinity-tuned peroxidase-like activity of hydrogel-supported Fe3O4 nanozyme through alteration of crosslinking concentration. J. Appl. Polym. Sci. 133, 1–10 (2016). https://doi.org/10.1002/app.43065
Bhunia, S., Rana, A., Roy, P., Martin, D.J., Pegis, M.L., Roy, B., Dey, A.: Rational design of mononuclear iron porphyrins for facile and selective 4e-/4H+ O2 reduction: activation of O-O bond by 2nd sphere hydrogen bonding. J. Am. Chem. Soc. 140, 9444–9457 (2018). https://doi.org/10.1021/jacs.8b02983
Li, M., Zhao, M., Cao, X., Zhao, M.: Smart polymers for biomimetic catalysis and enzyme inhibition. In: Li, S., Lieberzeit, P.A., Piletsky, S.A., Turner, A.P.F. (eds.) Smart Polymer Catalysis and Tunable Catalysis, 1st edn. Elsevier, Amsterdam (2019)
Hötger, D., Etzkorn, M., Morchutt, C., Wurster, B., Dreiser, J., Stepanow, S., Grumelli, D., Gutzler, R., Kern, K.: Stability of metallo-porphyrin networks under oxygen reduction and evolution conditions in alkaline media. Phys. Chem. Chem. Phys. 21, 2587–2594 (2019). https://doi.org/10.1039/c8cp07463a
Lin, T., Qin, Y., Huang, Y., Yang, R., Hou, L., Ye, F., Zhao, S.: A label-free fluorescence assay for hydrogen peroxide and glucose based on the bifunctional MIL-53(Fe) nanozyme. Chem. Commun. 54, 1762–1765 (2018). https://doi.org/10.1039/c7cc09819g
Ortiz-Gómez, I., Salinas-Castillo, A., García, A.G., Álvarez-Bermejo, J.A., de Orbe-Payá, I., Rodríguez-Diéguez, A., Capitán-Vallvey, L.F.: Microfluidic paper-based device for colorimetric determination of glucose based on a metal-organic framework acting as peroxidase mimetic. Microchim. Acta 185 (2018). https://doi.org/10.1007/s00604-017-2575-7
Wei, H., Wang, E.: Nanomaterials with enzyme-like characteristics (nanozymes): next-generation artificial enzymes. Chem. Soc. Rev. 42, 6060–6093 (2013). https://doi.org/10.1039/c3cs35486e
Manea, F., Houillon, F.B., Pasquato, L., Scrimin, P.: Nanozymes: gold-nanoparticle-based transphosphorylation catalysts. Angew. Chemie. 116, 6291–6295 (2004). https://doi.org/10.1002/ange.200460649
Gao, L., Zhuang, J., Nie, L., Zhang, J., Zhang, Y., Gu, N., Wang, T., Feng, J., Yang, D., Perrett, S., Yan, X.: Intrinsic peroxidase-like activity of ferromagnetic nanoparticles. Nat. Nanotechnol. 2, 577 (2007). https://doi.org/10.1038/nnano.2007.260
Liang, M., Yan, X.: Nanozymes: from new concepts, mechanisms, and standards to applications. Acc. Chem. Res. 52, 2190–2200 (2019). https://doi.org/10.1021/acs.accounts.9b00140
Campuzano, S., Pedrero, M., Yáñez-Sedeño, P., Pingarrón, J.M.: Nanozymes in electrochemical affinity biosensing. Microchim. Acta 187 (2020). https://doi.org/10.1007/s00604-020-04390-9
Peng, F., Xu, T., Wu, F., Ma, C., Liu, Y., Li, J., Zhao, B., Mao, C.: Novel biomimetic enzyme for sensitive detection of superoxide anions. Talanta 174, 82–91 (2017). https://doi.org/10.1016/j.talanta.2017.05.028
Chatterjee, B., Das, S.J., Anand, A., Sharma, T.K.: Nanozymes and aptamer-based biosensing. Mater. Sci. Energy Technol. 3, 127–135 (2020). https://doi.org/10.1016/j.mset.2019.08.007
Komkova, M.A., Andreeva, K.D., Zarochintsev, A.A., Karyakin, A.A.: Nanozymes “artificial peroxidase”: enzyme oxidase mixtures for single-step fabrication of advanced electrochemical biosensors. ChemElectroChem 8, 1117–1122 (2021). https://doi.org/10.1002/celc.202100275
Niu, X., Cheng, N., Ruan, X., Du, D., Lin, Y.: Review—Nanozyme-based immunosensors and immunoassays: recent developments and future trends. J. Electrochem. Soc. 167, 037508 (2020). https://doi.org/10.1149/2.0082003jes
Mahmudunnabi, R.G., Farhana, F.Z., Kashaninejad, N., Firoz, S.H., Shim, Y.B., Shiddiky, M.J.A.: Nanozyme-based electrochemical biosensors for disease biomarker detection. Analyst 145, 4398–4420 (2020). https://doi.org/10.1039/d0an00558d
Wang, C., Liu, C., Luo, J., Tian, Y., Zhou, N.: Direct electrochemical detection of kanamycin based on peroxidase-like activity of gold nanoparticles. Anal. Chim. Acta 936, 75–82 (2016). https://doi.org/10.1016/j.aca.2016.07.013
Das, R., Dhiman, A., Kapil, A., Bansal, V., Sharma, T.K.: Aptamer-mediated colorimetric and electrochemical detection of Pseudomonas aeruginosa utilizing peroxidase-mimic activity of gold NanoZyme. Anal. Bioanal. Chem. 411, 1229–1238 (2019). https://doi.org/10.1007/s00216-018-1555-z
Modenez, I.A., Macedo, L.J.A., Melo, A.F.A.A., Pereira, A.R., Oliveira, O.N., Crespilho, F.N.: Nanosized non-proteinaceous complexes III and IV mimicking electron transfer of mitochondrial respiratory chain. J. Colloid Interface Sci. 599, 198–206 (2021). https://doi.org/10.1016/j.jcis.2021.04.072
Begum, S., Hassan, Z., Bräse, S., Wöll, C., Tsotsalas, M.: Metal-organic framework-templated biomaterials: recent progress in synthesis, functionalization, and applications. Acc. Chem. Res. 52, 1598–1610 (2019). https://doi.org/10.1021/acs.accounts.9b00039
Bour, J.R., Wright, A.M., He, X., Dincǎ, M.: Bioinspired chemistry at MOF secondary building units. Chem. Sci. 11, 1728–1737 (2020). https://doi.org/10.1039/c9sc06418d
Ling, P., Cheng, S., Chen, N., Qian, C., Gao, F.: Nanozyme-modified metal-organic frameworks with multienzymes activity as biomimetic catalysts and electrocatalytic interfaces. ACS Appl. Mater. Interfaces 12, 17185–17192 (2020). https://doi.org/10.1021/acsami.9b23147
Ling, P., Hao, Q., Lei, J., Ju, H.: Porphyrin functionalized porous carbon derived from metal-organic framework as a biomimetic catalyst for electrochemical biosensing. J. Mater. Chem. B 3, 1335–1341 (2015). https://doi.org/10.1039/c4tb01620c
Katz, M.J., Mondloch, J.E., Totten, R.K., Park, J.K., Nguyen, S.T., Farha, O.K., Hupp, J.T.: Simple and compelling biomimetic metal-organic framework catalyst for the degradation of nerve agent simulants. Angew. Chemie. 126, 507–511 (2014). https://doi.org/10.1002/ange.201307520
McGuirk, C.M., Katz, M.J., Stern, C.L., Sarjeant, A.A., Hupp, J.T., Farha, O.K., Mirkin, C.A.: Turning on catalysis: incorporation of a hydrogen-bond-donating squaramide moiety into a Zr metal-organic framework. J. Am. Chem. Soc. 137, 919–925 (2015). https://doi.org/10.1021/ja511403t
Sahoo, P.C., Jang, Y.N., Lee, S.W.: Enhanced biomimetic CO2 sequestration and CaCO3 crystallization using complex encapsulated metal organic framework. J. Cryst. Growth 373, 96–101 (2013). https://doi.org/10.1016/j.jcrysgro.2012.11.043
Sasan, K., Lin, Q., Mao, C.Y., Feng, P.: Incorporation of iron hydrogenase active sites into a highly stable metal–organic framework for photocatalytic hydrogen generation. Chem. Commun. 50, 10390–10393 (2014). https://doi.org/10.1039/c4cc03946g
Feng, Y., Chen, C., Liu, Z., Fei, B., Lin, P., Li, Q., Sun, S., Du, S.: Application of a Ni mercaptopyrimidine MOF as highly efficient catalyst for sunlight-driven hydrogen generation. J. Mater. Chem. A 3, 7163–7169 (2015). https://doi.org/10.1039/c5ta00136f
Nath, I., Chakraborty, J., Verpoort, F.: Metal organic frameworks mimicking natural enzymes: a structural and functional analogy. Chem. Soc. Rev. 45, 4127–4170 (2016). https://doi.org/10.1039/c6cs00047a
Li, Y., Xu, N., Zhu, W., Wang, L., Liu, B., Zhang, J., Xie, Z., Liu, W.: Nanoscale melittin@zeolitic imidazolate frameworks for enhanced anticancer activity and mechanism analysis. ACS Appl. Mater. Interfaces 10, 22974–22984 (2018). https://doi.org/10.1021/acsami.8b06125
Wang, Q., Zhang, X., Huang, L., Zhang, Z., Dong, S.: GOx@ZIF-8(NiPd) nanoflower: an artificial enzyme system for tandem catalysis. Angew. Chemie. 129, 16298–16301 (2017). https://doi.org/10.1002/ange.201710418
Wang, Y., Hou, C., Zhang, Y., He, F., Liu, M., Li, X.: Preparation of graphene nano-sheet bonded PDA/MOF microcapsules with immobilized glucose oxidase as a mimetic multi-enzyme system for electrochemical sensing of glucose. J. Mater. Chem. B 4, 3695–3702 (2016). https://doi.org/10.1039/c6tb00276e
Dey, S., Mondal, B., Chatterjee, S., Rana, A., Amanullah, S., Dey, A.: Molecular electrocatalysts for the oxygen reduction reaction. Nat. Rev. Chem. 1 (2017). https://doi.org/10.1038/s41570-017-0098
Zhang, B., Sun, L.: Artificial photosynthesis: opportunities and challenges of molecular catalysts. Chem. Soc. Rev. 48, 2216–2264 (2019). https://doi.org/10.1039/c8cs00897c
Zhao, Y.M., Yu, G.Q., Wang, F.F., Wei, P.J., Liu, J.G.: Bioinspired transition-metal complexes as electrocatalysts for the oxygen reduction reaction. Chem. - A Eur. J. 25, 3726–3739 (2019). https://doi.org/10.1002/chem.201803764
Mihara, N., Yamada, Y., Takaya, H., Kitagawa, Y., Aoyama, S., Igawa, K., Tomooka, K., Tanaka, K.: Oxygen reduction to water by a cofacial dimer of iron(III)–porphyrin and iron(III)–phthalocyanine linked through a highly flexible fourfold rotaxane. Chem. - A Eur. J. 23, 7508–7514 (2017). https://doi.org/10.1002/chem.201700082
Oliveira, R., Zouari, W., Herrero, C., Banse, F., Schöllhorn, B., Fave, C., Anxolabéhère-Mallart, E.: Characterization and subsequent reactivity of an Fe-peroxo porphyrin generated by electrochemical reductive activation of O2. Inorg. Chem. 55, 12204–12210 (2016). https://doi.org/10.1021/acs.inorgchem.6b01804
Liu, C., Lei, H., Zhang, Z., Chen, F., Cao, R.: Oxygen reduction catalyzed by a water-soluble binuclear copper(ii) complex from a neutral aqueous solution. Chem. Commun. 53, 3189–3192 (2017). https://doi.org/10.1039/c6cc09206c
Kotani, H., Yagi, T., Ishizuka, T., Kojima, T.: Enhancement of 4-electron O2 reduction by a Cu(II)-pyridylamine complex via protonation of a pendant pyridine in the second coordination sphere in water. Chem. Commun. 51, 13385–13388 (2015). https://doi.org/10.1039/c5cc03012a
Zhang, W., Lai, W., Cao, R.: Energy-related small molecule activation reactions: oxygen reduction and hydrogen and oxygen evolution reactions catalyzed by porphyrin- and corrole-based systems. Chem. Rev. 117, 3717–3797 (2017). https://doi.org/10.1021/acs.chemrev.6b00299
Sonkar, P.K., Prakash, K., Yadav, M., Ganesan, V., Sankar, M., Gupta, R., Yadav, D.K.: Co(II)-porphyrin-decorated carbon nanotubes as catalysts for oxygen reduction reactions: an approach for fuel cell improvement. J. Mater. Chem. A 5, 6263–6276 (2017). https://doi.org/10.1039/c6ta10482g
Brezny, A.C., Nedzbala, H.S., Mayer, J.M.: Multiple selectivity-determining mechanisms of H2O2 formation in iron porphyrin-catalysed oxygen reduction. Chem. Commun. 57, 1202–1205 (2021). https://doi.org/10.1039/d0cc06701f
Kostopoulos, N., Banse, F., Fave, C., Anxolabéhère-Mallart, E.: Modulating alkene reactivity from oxygenation to halogenationviaelectrochemical O2 activation by Mn porphyrin. Chem. Commun. 57, 1198–1201 (2021). https://doi.org/10.1039/d0cc07531k
Thiyagarajan, N., Janmanchi, D., Tsai, Y.-F., Wanna, W.H., Ramu, R., Chan, S.I., Zen, J.-M., Yu, S.S.-F.: A carbon electrode functionalized by a tricopper cluster complex: overcoming overpotential and production of hydrogen peroxide in the oxygen reduction reaction. Angew. Chemie. 130, 3674–3678 (2018). https://doi.org/10.1002/ange.201712226
Lu, Y., Wang, X., Wang, M., Kong, L., Zhao, J.: 1,10-phenanthroline metal complex covalently bonding to poly- (pyrrole-3-carboxylic acid)-coated carbon: an efficient electrocatalyst for oxygen reduction. Electrochim. Acta 180, 86–95 (2015). https://doi.org/10.1016/j.electacta.2015.08.104
Cunningham, D.W., Yang, J.Y.: Kinetic and mechanistic analysis of a synthetic reversible CO2/HCO2-electrocatalyst. Chem. Commun. 56, 12965–12968 (2020). https://doi.org/10.1039/d0cc05556e
Kaeffer, N., Chavarot-Kerlidou, M., Artero, V.: Hydrogen evolution catalyzed by cobalt diimine-dioxime complexes. Acc. Chem. Res. 48, 1286–1295 (2015). https://doi.org/10.1021/acs.accounts.5b00058
Xie, L., Tian, J., Ouyang, Y., Guo, X., Zhang, W., Apfel, U., Zhang, W., Cao, R.: Water-soluble polymers with appending porphyrins as bioinspired catalysts for the hydrogen evolution reaction. Angew. Chemie. 132, 15978–15982 (2020). https://doi.org/10.1002/ange.202003836
Rosser, T.E., Gross, M.A., Lai, Y.H., Reisner, E.: Precious-metal free photoelectrochemical water splitting with immobilised molecular Ni and Fe redox catalysts. Chem. Sci. 7, 4024–4035 (2016). https://doi.org/10.1039/c5sc04863j
Wu, H.L., Li, X.B., Tung, C.H., Wu, L.Z.: Bioinspired metal complexes for energy-related photocatalytic small molecule transformation. Chem. Commun. 56, 15496–15512 (2020). https://doi.org/10.1039/d0cc05870j
Stieger, K.R., Ciornii, D., Kölsch, A., Hejazi, M., Lokstein, H., Feifel, S.C., Zouni, A., Lisdat, F.: Engineering of supramolecular photoactive protein architectures: the defined co-assembly of photosystem i and cytochrome: C using a nanoscaled DNA-matrix. Nanoscale 8, 10695–10705 (2016). https://doi.org/10.1039/c6nr00097e
Guo, W., Hong, F., Liu, N., Huang, J., Wang, B., Duan, R., Lou, X., Xia, F.: Target-specific 3D DNA gatekeepers for biomimetic nanopores. Adv. Mater. 27, 2090–2095 (2015). https://doi.org/10.1002/adma.201405078
Kocsis, I., Sorci, M., Vanselous, H., Murail, S., Sanders, S.E., Licsandru, E., Legrand, Y.M., Van der Lee, A., Baaden, M., Petersen, P.B., Belfort, G., Barboiu, M.: Oriented chiral water wires in artificial transmembrane channels. Sci. Adv. 4 (2018). https://doi.org/10.1126/sciadv.aao5603
Zhao, X.P., Liu, F.F., Hu, W.C., Younis, M.R., Wang, C., Xia, X.H.: Biomimetic nanochannel-ionchannel hybrid for ultrasensitive and label-free detection of microRNA in cells. Anal. Chem. 91, 3582–3589 (2019). https://doi.org/10.1021/acs.analchem.8b05536
Burns, J.R., Seifert, A., Fertig, N., Howorka, S.: A biomimetic DNA-based channel for the ligand-controlled transport of charged molecular cargo across a biological membrane. Nat. Nanotechnol. 11, 152–156 (2016). https://doi.org/10.1038/nnano.2015.279
Lv, C., Gu, X., Li, H., Zhao, Y., Yang, D., Yu, W., Han, D., Li, J., Tan, W.: Molecular transport through a biomimetic DNA channel on live cell membranes. ACS Nano 14, 14616–14626 (2020). https://doi.org/10.1021/acsnano.0c03105
Hu, X.B., Liu, Y.L., Wang, W.J., Zhang, H.W., Qin, Y., Guo, S., Zhang, X.W., Fu, L., Huang, W.H.: Biomimetic graphene-based 3D scaffold for long-term cell culture and real-time electrochemical monitoring. Anal. Chem. 90, 1136–1141 (2018). https://doi.org/10.1021/acs.analchem.7b03324
Liu, Y., Li, L., Zhu, J., Xu, J., Liu, S., Wang, Y., Zhang, C., Liu, T.: A biomimetic: Setaria viridis-inspired electrode with polyaniline nanowire arrays aligned on MoO3@polypyrrole core-shell nanobelts. J. Mater. Chem. A 6, 13428–13437 (2018). https://doi.org/10.1039/c8ta04218g
Wickham, A., Vagin, M., Khalaf, H., Bertazzo, S., Hodder, P., Dånmark, S., Bengtsson, T., Altimiras, J., Aili, D.: Electroactive biomimetic collagen-silver nanowire composite scaffolds. Nanoscale 8, 14146–14155 (2016). https://doi.org/10.1039/c6nr02027e
Jiao, D., Lossada, F., Guo, J., Skarsetz, O., Hoenders, D., Liu, J., Walther, A.: Electrical switching of high-performance bioinspired nanocellulose nanocomposites. Nat. Commun. 12, 1–10 (2021). https://doi.org/10.1038/s41467-021-21599-1
Li, B.M., Lu, J.: Cobalt in lithium-ion batteries. Sci. 367, 970–980 (2020)
Shi, W., Shen, J., Shen, L., Hu, W., Xu, P., Baucom, J.A., Ma, S., Yang, S., Chen, X.M., Lu, Y.: Electrolyte membranes with biomimetic lithium-ion channels. Nano Lett. 20, 5435–5442 (2020). https://doi.org/10.1021/acs.nanolett.0c01910
Chen, N., Dai, Y., Xing, Y., Wang, L., Guo, C., Chen, R., Guo, S., Wu, F.: Biomimetic ant-nest ionogel electrolyte boosts the performance of dendrite-free lithium batteries. Energy Environ. Sci. 10, 1660–1667 (2017). https://doi.org/10.1039/c7ee00988g
Yabuuchi, N., Kajiyama, M., Iwatate, J., Nishikawa, H., Hitomi, S., Okuyama, R., Usui, R., Yamada, Y., Komaba, S.: P2-type Nax[Fe1/2Mn1/2]O2 made from earth-abundant elements for rechargeable Na batteries. Nat. Mater. 11, 512–517 (2012). https://doi.org/10.1038/nmat3309
Liu, W., Zhi, H., Yu, X.: Recent progress in phosphorus based anode materials for lithium/sodium ion batteries. Energy Storage Mater. 16, 290–322 (2019). https://doi.org/10.1016/j.ensm.2018.05.020
Ran, L., Luo, B., Gentle, I.R., Lin, T., Sun, Q., Li, M., Rana, M.M., Wang, L., Knibbe, R.: Biomimetic Sn4P3 anchored on carbon nanotubes as an anode for high-performance sodium-ion batteries. ACS Nano 14, 8826–8837 (2020). https://doi.org/10.1021/acsnano.0c03432
Orita, A., Verde, M.G., Sakai, M., Meng, Y.S.: A biomimetic redox flow battery based on flavin mononucleotide. Nat. Commun. 7, 1–8 (2016). https://doi.org/10.1038/ncomms13230
Soloveichik, G.L.: Flow batteries: current status and trends. Chem. Rev. 115, 11533–11558 (2015). https://doi.org/10.1021/cr500720t
Dai, K., Wang, X., Yi, F., Jiang, C., Li, R., You, Z.: Triboelectric nanogenerators as self-powered acceleration sensor under high-g impact. Nano Energy 45, 84–93 (2018). https://doi.org/10.1016/j.nanoen.2017.12.022
Liu, S., Liu, X., Zhou, G., Qin, F., Jing, M., Li, L., Song, W., Sun, Z.: A high-efficiency bioinspired photoelectric-electromechanical integrated nanogenerator. Nat. Commun. 11, 1–9 (2020). https://doi.org/10.1038/s41467-020-19987-0
Wakerley, D., Lamaison, S., Ozanam, F., Menguy, N., Mercier, D., Marcus, P., Fontecave, M., Mougel, V.: Bio-inspired hydrophobicity promotes CO2 reduction on a Cu surface. Nat. Mater. 18, 1222–1227 (2019). https://doi.org/10.1038/s41563-019-0445-x
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Modenez, I.A. (2022). Biomimetics Applied in Electrochemistry. In: Crespilho, F.N. (eds) Advances in Bioelectrochemistry Volume 2. Springer, Cham. https://doi.org/10.1007/978-3-030-95270-9_1
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