Relevant bibliographies by topics / Electrochemistry of enzymes

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'Electrochemistry of enzymes'

Author: Grafiati
Published: 4 June 2021
Last updated: 8 February 2022

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Journal articles on the topic "Electrochemistry of enzymes"

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Bernhardt, Paul V. "Enzyme Electrochemistry — Biocatalysis on an Electrode." Australian Journal of Chemistry 59, no. 4 (2006): 233. http://dx.doi.org/10.1071/ch05340.

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Oxidoreductase enzymes catalyze single- or multi-electron reduction/oxidation reactions of small molecule inorganic or organic substrates, and they are integral to a wide variety of biological processes including respiration, energy production, biosynthesis, metabolism, and detoxification. All redox enzymes require a natural redox partner such as an electron-transfer protein (e.g. cytochrome, ferredoxin, flavoprotein) or a small molecule cosubstrate (e.g. NAD(P)H, dioxygen) to sustain catalysis, in effect to balance the substrate/product redox half-reaction. In principle, the natural electron-transfer partner may be replaced by an electrochemical working electrode. One of the great strengths of this approach is that the rate of catalysis (equivalent to the observed electrochemical current) may be probed as a function of applied potential through linear sweep and cyclic voltammetry, and insight to the overall catalytic mechanism may be gained by a systematic electrochemical study coupled with theoretical analysis. In this review, the various approaches to enzyme electrochemistry will be discussed, including direct and indirect (mediated) experiments, and a brief coverage of the theory relevant to these techniques will be presented. The importance of immobilizing enzymes on the electrode surface will be presented and the variety of ways that this may be done will be reviewed. The importance of chemical modification of the electrode surface in ensuring an environment conducive to a stable and active enzyme capable of functioning natively will be illustrated. Fundamental research into electrochemically driven enzyme catalysis has led to some remarkable practical applications. The glucose oxidase enzyme electrode is a spectacularly successful application of enzyme electrochemistry. Biosensors based on this technology are used worldwide by sufferers of diabetes to provide rapid and accurate analysis of blood glucose concentrations. Other applications of enzyme electrochemistry are in the sensing of macromolecular complexation events such as antigen–antibody binding and DNA hybridization. The review will include a selection of enzymes that have been successfully investigated by electrochemistry and, where appropriate, discuss their development towards practical biotechnological applications.
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Lin, Chuhong, Lior Sepunaru, Enno Kätelhön, and Richard G. Compton. "Electrochemistry of Single Enzymes: Fluctuations of Catalase Activities." Journal of Physical Chemistry Letters 9, no. 11 (May 11, 2018): 2814–17. http://dx.doi.org/10.1021/acs.jpclett.8b01199.

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GUO, L. H., and H. A. O. HILL. "ChemInform Abstract: Direct Electrochemistry of Proteins and Enzymes." ChemInform 22, no. 50 (August 22, 2010): no. http://dx.doi.org/10.1002/chin.199150345.

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Hill, H. A. O. "Making Use of the Direct Electrochemistry of Enzymes." Portugaliae Electrochimica Acta 19, no. 3 (2001): 165–70. http://dx.doi.org/10.4152/pea.200103165.

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Peterbauer, Clemens K. "Pyranose dehydrogenases: Rare enzymes for electrochemistry and biocatalysis." Bioelectrochemistry 132 (April 2020): 107399. http://dx.doi.org/10.1016/j.bioelechem.2019.107399.

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Davis, Connor, Stephanie X. Wang, and Lior Sepunaru. "What can electrochemistry tell us about individual enzymes?" Current Opinion in Electrochemistry 25 (February 2021): 100643. http://dx.doi.org/10.1016/j.coelec.2020.100643.

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Gulaboski, Rubin, and Valentin Mirceski. "Application of voltammetry in biomedicine - Recent achievements in enzymatic voltammetry." Macedonian Journal of Chemistry and Chemical Engineering 39, no. 2 (November 12, 2020): 153. http://dx.doi.org/10.20450/mjcce.2020.2152.

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Protein-film voltammetry (PFV) is considered the simplest methodology to study the electrochemistry of lipophilic redox enzymes in an aqueous environment. By anchoring particular redox enzymes on the working electrode surface, it is possible to get an insight into the mechanism of enzyme action. The PFV methodology enables access to the relevant thermodynamic and kinetic parameters of the enzyme-electrode reaction and enzyme-substrate interactions, which is important to better understand many metabolic pathways in living systems and to delineate the physiological role of enzymes. PFV additionally provides important information which is useful for designing specific biosensors, simple medical devices and bio-fuel cells. In the current review, we focus on some recent achievements of PFV, while presenting some novel protocols that contribute to a better communication between redox enzymes and the working electrode. Insights to several new theoretical models that provide a simple strategy for studying electrode reactions of immobilized enzymes and that enable both kinetic and thermodynamic characterization of enzyme-substrate interactions are also provided. In addition, we give a short overview to several novel voltammetric techniques, derived from the perspective of square-wave voltammetry, which seem to be promising tools for application in PFV.
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KASAI, Nahoko, Yasuhiko JIMBO, Osamu NIWA, Tomokazu MATSUE, and Keiichi TORIMITSU. "Multichannel Glutamate Monitoring by Electrode Array Electrochemically Immobilized with Enzymes." Electrochemistry 68, no. 11 (November 5, 2000): 886–89. http://dx.doi.org/10.5796/electrochemistry.68.886.

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Schachinger, Franziska, Hucheng Chang, Stefan Scheiblbrandner, and Roland Ludwig. "Amperometric Biosensors Based on Direct Electron Transfer Enzymes." Molecules 26, no. 15 (July 27, 2021): 4525. http://dx.doi.org/10.3390/molecules26154525.

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The accurate determination of analyte concentrations with selective, fast, and robust methods is the key for process control, product analysis, environmental compliance, and medical applications. Enzyme-based biosensors meet these requirements to a high degree and can be operated with simple, cost efficient, and easy to use devices. This review focuses on enzymes capable of direct electron transfer (DET) to electrodes and also the electrode materials which can enable or enhance the DET type bioelectrocatalysis. It presents amperometric biosensors for the quantification of important medical, technical, and environmental analytes and it carves out the requirements for enzymes and electrode materials in DET-based third generation biosensors. This review critically surveys enzymes and biosensors for which DET has been reported. Single- or multi-cofactor enzymes featuring copper centers, hemes, FAD, FMN, or PQQ as prosthetic groups as well as fusion enzymes are presented. Nanomaterials, nanostructured electrodes, chemical surface modifications, and protein immobilization strategies are reviewed for their ability to support direct electrochemistry of enzymes. The combination of both biosensor elements—enzymes and electrodes—is evaluated by comparison of substrate specificity, current density, sensitivity, and the range of detection.
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Shukla, Alka, Elizabeth M. Gillam, Deanne J. Mitchell, and Paul V. Bernhardt. "Direct electrochemistry of enzymes from the cytochrome P450 2C family." Electrochemistry Communications 7, no. 4 (April 2005): 437–42. http://dx.doi.org/10.1016/j.elecom.2005.02.021.

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Dissertations / Theses on the topic "Electrochemistry of enzymes"

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Whitaker, Richard George. "The electrochemistry of redox enzymes." Thesis, University of Warwick, 1989. http://wrap.warwick.ac.uk/4235/.

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The work presented in this thesis is of two types. Firstly methods for the electrochemical immobilisation of redox enzymes in organic polymers are described. The electrochemical monitoring of the immobilised enzyme reaction by detection of one of the enzyme's products is discussed, and the results obtained for such a system under a variety of experimental conditions are presented. A good understanding of the way in which such a system operates' was obtained by using a specially developed kinetic model., This model is explained fully in the theory chapter of this thesis. A variety of organic polymers were used in the electrochemical immobilisation process, with varying degrees of success. The flexibility of this approach is demonstrated by the use of a variety of immobilisation matrices and also by the development of bienzyme and bilayer devices. The final experimental chapter presents work on the covalent modification of redox enzymes with a variety of, redox centres based. on ferrocene. Although attempts to electrochemically immobilise a modified enzyme were not successful, some interesting information about the kinetic behaviour and stability of a series Of modified enzymes was obtained. An indication of possible work forming an extension to this thesis is given in the final part of this thesis. The electrochemical immobilisation techniques and the procedure for covalently modifying, enzymes using electroactive, groups are relatively recent ideas. Much work remains to be done before a better understanding of these systems is gained.
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Hunt, Nicholas Imber. "Biological electrochemistry." Thesis, University of Oxford, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.386592.

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De, Oliveira Pedro M. A. "Studies of enzymes by electrochemistry and atomic force microscopy." Thesis, University of Oxford, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.298717.

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Xu, Lang. "Investigating the current/voltage/power/stability capabilities of enzyme-based membrane-less hydrogen fuel cells." Thesis, University of Oxford, 2014. http://ora.ox.ac.uk/objects/uuid:efef7124-3444-4531-872b-2ee8868e0aa0.

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Fuel cell is a device that can directly convert chemical energy into electrical energy. For low-temperature fuel cells, catalysts are required. Fuel cells using Pt-based or other non-biological materials as catalysts are known as conventional fuel cells. Inspired from Nature, enzymes can be used as catalysts in fuel cells known as enzyme-based fuel cells. The conventional and enzymatic fuel cells share the same underlying electrochemical principles, while enzyme-based fuel cells have their intrinsic advantages and disadvantages due to enzyme properties. The objective of this thesis is to investigate the current/voltage/ power/stability capabilities of enzyme-based membrane-less H2 fuel cells in order to design the enzymatic fuel cells with improved performance. This thesis presents a facile, effective method for the construction of 3D porous carbon electrodes. The 3D porous carbon electrodes are constructed by compacting suitable carbon nanomaterials into discs. The 3D porous carbon electrodes, with large roughness, high specific surface area, and optimized pore size distribution, are able to increase the loading density of enzymes, that is, reaction sites per unit geometric electrode area. The high loading density of enzymes can result in the high current/power density of the enzyme-based membrane-less H2 fuel cells. Moreover, the large enzyme loading can bring about the improvement in fuel cell stability because current becomes limited by mass transport of dissolved gases rather than enzyme immobilization so that neither inactivation nor desorption of enzymes would influence the current output. Based on one type of 3D porous carbon electrodes, the maximum power density of enzyme-based membrane-less H2 fuel cells has increased to the mW•cm2 level by at least one order of magnitude and the half-life has also increased from several hours to one week. This thesis presents a method for the increase in power density otherwise limited by low cathodic currents due to meagre O2 in non-explosive H2-rich H2-air mixtures. The power density of enzyme-based membrane-less H2 fuel cells can be increased by re-proportioning cathode/anode geometric area ratio to balance the cathodic and anodic currents under such an unusual H2-air mixture. This thesis also demonstrates that the 3D porous carbon electrode can improve the apparent O2 tolerance of anodic catalysts – hydrogenases, which are very important for the fuel cell performance. The degrees of apparent O2 tolerance for both O2-tolerant and O2-sensitive [NiFe]-hydrogenases are greatly increased based on the 3D porous carbon electrodes, so that even an O2-sensitive [NiFe]-hydrogenase can be used as an anodic catalyst in the enzyme-based membrane-less H2 fuel cell under a non-explosive H2-rich H2-air mixture. This thesis presents a design of a test bed in which series and parallel connections of sandwich-like electrode stacks can be varied. The fuel cell test bed has demonstrated low-loss interconnects and efficient stack configuration. Operated under a non-explosive H2-air mixture containing only 4.6% O2 at 20 °C, the maximum volume power density of the fuel cell test bed exceeds 2 mW•cm3, capable of powering electronic gadgets, which is a good demonstration of electricity that originates from the buried active sites of enzymes and is transmitted by long-range electron hopping in accordance with Marcus theory.
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Owens, Zachary J. "The purification and electrochemistry of his-tagged photosystem II." [Denver, Colo.] : Regis University, 2009. http://165.236.235.140/lib/ZOwens2009.pdf.

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Goldet, Gabrielle. "Electrochemical investigations of H2-producing enzymes." Thesis, University of Oxford, 2009. http://ora.ox.ac.uk/objects/uuid:696e5b9d-a80f-493e-85d4-0954be499b72.

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Hydrogenases are a family of enzyme that catalyses the bidirectional interconversion of H+ and H2. There are two major classes of hydrogenases: the [NiFe(Se)]- and [FeFe]-hydrogenases. Both of these benefit from characteristics which would be advantageous to their use in technological devices for H2 evolution and the generation of energy. These features are explored in detail in this thesis, with a particular emphasis placed on defining the conditions that limit the activity of hydrogenases when reducing H+ to produce H2. Electrochemistry can be used as a direct measure of enzymatic activity; thus, Protein Film Electrochemistry, in which the protein is adsorbed directly onto the electrode, has been employed to probe catalysis by hydrogenases. Various characteristics of hydrogenases were probed. The catalytic bias for H2 production was interrogated and the inhibition of H2 evolution by H2 itself (a major drawback to the use of some hydrogenases in technological devices to produce H2) was quantified for a number of different hydrogenase. Aerobic inactivation of hydrogenases is also a substantial technological limitation; thus, inactivation of both H2 production and H2 oxidation by O2 was studied in detail. This was compared to inhibition of hydrogenases by CO so as to elucidate the mechanism of binding of diatomic molecules and determine the factors limiting inactivation. This allows for a preliminary proposal for the genetic redesigning of hydrogenases for biotechnological purposes to be made. Finally, preliminary investigation of the binding of formaldehyde, potentially at a site integral to proton transfer, opens the field for further research into proton transfer pathways, the structural implications thereof and their importance in catalysis.
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Yorke, Jake. "Engineering cytochrome P450BM3 into a drug metabolising enzyme." Thesis, University of Oxford, 2012. http://ora.ox.ac.uk/objects/uuid:92dcddfe-b3fc-46e8-9e5e-77910fb03783.

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Directed evolution studies by Whitehouse et al. identified several variants of P450BM3 (CYP102A1) with enhanced substrate oxidation rates across a range of substrates. This thesis describes the use of these ‘generic accelerator’ variants, in combination with selectivity altering mutations to engineer P450BM3¬ for the oxidation of pharmaceuticals. Using engineered variants the non-steroidal anti-inflammatory drug diclofenac was metabolised to the primary human metabolites 4′- and 5-hydroxydiclofenac, with total conversion of 2 mM substrate by 5 μM enzyme. The local-anaesthetic lidocaine and the steroid testosterone were similarly metabolised to human metabolites. This is the first report of a drug compound being totally converted to the human metabolites by a P450BM3 variant, and is also the first report of lidocaine metabolism by a P450¬BM3 variant. The engineered variants are akin to CYP3A4, the primary human drug metabolising enzyme, as they show activity towards a range of compounds including anionic, cationic and neutral drugs. This range of activity is at the expense of NADPH coupling, which remains low with these substrates. In order to more fully understand the origin of the rate enhancing properties of the generic accelerator variants, spectroelectrochemical, stopped-flow and kinetic studies were performed. A custom optically transparent thin layer electrode system was designed and fabricated for use in spectroelectrochemical titrations. A spectroelectrochemical cell and gold mesh electrode were designed and used in spectroelectrochemical investigations of P450BM3 variants, as well as other P450s and their redox partners. These spectroelectrochemical, stopped-flow and kinetic studies, in combination with X-ray crystal structures provided insight into the origin of the rate enhancing properties of these enzymes and supplied the first example of the complete characterization of the thermodynamic and kinetic properties of WT and mutant P450BM3 for the oxidation of a non-natural substrate. The generic accelerator variants are, in the resting state, in a more catalytically ready conformation than the WT enzyme, and reorganization energy barriers appear to be lowered, so that fewer substrate-induced structural changes are required to promote electron transfer and initiate the catalytic cycle.
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Jarrar, Haytem. "Bioélectrodes enzymatiques pour des applications en biocapteurs et en biopiles." Thesis, Montpellier, Ecole nationale supérieure de chimie, 2011. http://www.theses.fr/2011ENCM0017/document.

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La principale originalité de ce travail est la mise en œuvre de deux voies d'immobilisation du biorécepteur sur différents matériaux d'électrodes. Dans un premier temps, nous avons démontré que le polyneutral red (PNR) représente une bonne matrice de rétention pour les enzymes. De plus, de part ses propriétés de médiation vis-à-vis des enzymes et principalement de leur cofacteur (NAD/FAD), ce polymère permet une connexion intime entre le site actif de l'enzyme et l'électrode. L'ensemble de ces caractéristiques nous a permis de mettre en œuvre une bioélectrode applicable en tant qu'anode d'un biocapteur à glucose et d'une cellule de biopile à combustible. Dans un second temps, la glocose oxydase a été immobilisée de façon covalente sur une électrode. L'électro-oxydation de l'éthylène a été menée sur les électrodes de carbone vitreux pour obtenir des fonctions amines. La voie proposée est simple, rapide et efficace. Puis, la glucose oxydase a été greffée avec succès par la méthode EDC / NHS sur les fonctions amines après optimisation des conditions de pH. Ces bioélectrodes ont ensuite été testées en tant que biocapteur à glucose montrant une bonne sensibilité de glucose avec une bonne stabilité sur une période de 4 semaines ce qui prouve l'efficacité de la méthode de greffage pour des applications de détection et dosage
The main originality of this work is the development of two-way to immobilize a bioreceptor on different electrode materials. Initially, we demonstrated that the polyneutral red (PNR) is a good matrix for retaining enzymes. In addition, its properties of mediation towards enzymes and mainly their cofactor (NAD / FAD), this polymer provides an intimate connection between the active site of the enzyme and the electrode. All these features allowed us to develop an bioelectrodes as the anode of a biosensor for glucose and a fuel cell biopile. In a second step, the glocose oxidase was covalently immobilized on an electrode. The electro-oxidation of ethylene diamine was carried out on glassy carbon electrodes to obtain amine functions. This proposed way is simple, fast and efficient. Then, glucose oxidase was successfully grafted by the method EDC / NHS on amine functions after the optimization of pH conditions. These bioelectrodes were then tested as glucose biosensor and showed good sensitivity with good stability over a period of 4 weeks which proves the effectiveness of the grafting method for detection and assay applications
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Wang, Vincent Cho-Chien. "New insights into enzymatic CO₂ reduction using protein film electrochemistry." Thesis, University of Oxford, 2013. http://ora.ox.ac.uk/objects/uuid:f1061854-f6b8-4562-81e0-968c80e1da3a.

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Carbon monoxide dehydrogenase (CODH) is known to catalyze CO oxidation and CO₂ reduction reversibly with the minimal overpotential. A great advantage of protein film electrochemistry (PFE) is its ability to probe catalysis over a wide range of potentials, especially in the low potential region required for CO₂ reduction. CODH I and CODH II from Carboxydothermus hydrogenoformans(Ch) and the composite enzyme acetyl-CoA synthase/carbon monoxide dehydrogenase (ACS/CODH) from Moorella thermoacetica(Mt) are intensively studied throughout this thesis. The different catalytic redox-states in CODH, Cox (inactive state), Cred1 (for CO oxidation) and Cred2 (for CO₂ reduction) as characterized by spectroscopy, are studied by PFE in the presence of substrate-mimic inhibitors. Cyanide, isoelectronic with CO, mainly inhibits CO oxidation, whereas cyanate, isoelectronic with CO₂, mainly targets CO₂ reduction. Sulfide inhibits CODH rapidly when the potential is more positive than −50 mV, which suggests that sulfide reacts to form a state at the oxidation level of Cox in CODH and is not an activator for CODH catalysis as suggested before. Thiocyanate only partially inhibits CO oxidation. No inhibition of CODH by azide is detected, which is in contrast with previous studies with ACS/CODHMt. The main differences between CODH ICh and CODH IICh are the stronger CO product inhibition and inhibition of CODH IICh by cyanide. These discoveries might shed light on the possible role of CODH IICh,/sub> in biological systems. In comparison with bidirectional (reversible) electrocatalysis by CODH ICh and CODH IICh, only unidirectional electrocatalysis for CO oxidation by ACS/CODHMt is observed with an overpotential of 0.1 V and the electrocatalytic current is much smaller. In order to identify whether ACS influences the performance of CODH, several chemical reagents, such as sodium dodecyl sulfate (which separates CODH and ACS partially), 1, 10-phenanthroline, (which inhibits the active site in ACS) and acetyl-CoA (the product of the reaction carried out by ACS/CODHMt) are added. However, we have yet to observe any electrocatalytic current from CO₂ reduction. Inhibition of ACS/CODHMt by cyanide, cyanate and azide is consistent with previous studies by spectroscopy. Oxygen attack toward the active site in CODH is proved by cyanide protection. The inactive state, Cox can prevent oxygen attack and reductive reactivation restores CODH activity. In contrast, oxygen damages the active site irreversibly when CODH is in the Cred1 state. The new substrate, nitrous oxide (N₂O), isoelectronic with CO₂, is reduced by CODH and acts as the suicide substrate. Finally, hydrogen formation in the direction of CO oxidation and formate formation in the direction of CO₂ reduction by CODH are detected. The small solvent kinetic isotope effect is observed in CO oxidation. These findings suggest metal-hydride should play a role in CODH catalysis, which might provide a new direction to design better catalysts for CO₂ reduction.
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Maerten, Clément. "Bio-inspired self-construction and self-assembly of organic films triggered by electrochemistry." Thesis, Strasbourg, 2016. http://www.theses.fr/2016STRAE045.

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Les architectures moléculaires qui se forment exclusivement sur une surface sont encore rares. L’électrodéposition est un procédé exploitant des « signaux » électriques afin de déclencher et contrôler l’assemblage de films. Récemment, une nouvelle méthode : l’autoconstruction de films en « une étape » par l’utilisation d’un morphogène (un gradient de catalyseur généré depuis une électrode), a attiré l’attention de la communauté scientifique. En effet, elle permet l’auto-assemblage rapide de films polymériques robustes. Cependant, cette technique était limitée à des systèmes basés sur la chimie click du Cu (I). Le but de ce travail était d’étendre cette stratégie à d’autres systèmes en utilisant une approche bio-inspirée. Le concept du morphogène a été appliqué pour développer deux nouveaux systèmes d’autoconstruction déclenchées par électrochimie. Le premier système est basé sur l’autoconstruction covalente de films polymériques induite par l’oxydation d’une molécule organique, inspirée de la moule. Le deuxième est basé sur l’auto-assemblage de films de polyphénols par électro-assemblage par liaisons de coordinations. Enfin, nous avons appliqué ces deux concepts pour immobiliser électrochimiquement une enzyme sur une électrode afin de créer un biosenseur
Molecular architectures that spontaneously grow exclusively near a surface are rare. Electrodeposition is a process in which imposed electrical « signals » are employed to direct the assembly of thin films. Recently, a new method based on the one-pot self-construction of films by means of a morphogen (a catalyst gradient generated from a surface) has attracted attention since it allows the quick self-assembly of robust films. Nevertheless, this technique was quite limited to systems based on click chemistry.The purpose of this work was to extend this strategy to other systems using a bio-inspired approach. The one-pot morphogen concept was applied to design two new electro-triggered self-construction concepts. The first one is based on the self-construction of covalent polymer films triggered by mussel-inspired molecule oxidation. The second one is based on the electro-self-assembly of polyphenols films based on ionic bonds coordination. Finally, we tried to apply these concepts in order to electrochemically immobilize an enzyme on an electrode to create a biosensor
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Books on the topic "Electrochemistry of enzymes"

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Whitaker, Richard George. The electrochemistry of redox enzymes. [s.l.]: typescript, 1989.

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Volk, Kevin John. Electrochemistry and enzymes on-line with mass spectrometry. 1989.

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Book chapters on the topic "Electrochemistry of enzymes"

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Ludwig, Roland. "Direct Electron Transfer to Enzymes." In Encyclopedia of Applied Electrochemistry, 330–35. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4419-6996-5_258.

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Kalimuthu, Palraj, and Paul V. Bernhardt. "CHAPTER 5. Electrochemistry of Molybdenum and Tungsten Enzymes." In Molybdenum and Tungsten Enzymes, 168–222. Cambridge: Royal Society of Chemistry, 2016. http://dx.doi.org/10.1039/9781782628842-00168.

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Magnusson, Anders O., and Dirk Holtmann. "Cofactor Substitution, Mediated Electron Transfer to Enzymes." In Encyclopedia of Applied Electrochemistry, 221–25. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4419-6996-5_256.

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Weidinger, Inez M. "Plasmonic Nanostructured Supports for Spectro-Electrochemistry of Enzymes on Electrodes." In Handbook of Nanoelectrochemistry, 1–16. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-15207-3_43-1.

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Weidinger, Inez M. "Plasmonic Nanostructured Supports for Spectro-Electrochemistry of Enzymes on Electrodes." In Handbook of Nanoelectrochemistry, 1013–32. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-15266-0_43.

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Shumyantseva, Victoria V., Tatiana Bulko, Evgeniya Shich, Anna Makhova, Alexey Kuzikov, and Alexander Archakov. "Cytochrome P450 Enzymes and Electrochemistry: Crosstalk with Electrodes as Redox Partners and Electron Sources." In Advances in Experimental Medicine and Biology, 229–46. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-16009-2_9.

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Butt, Julea N., Andrew J. Gates, Sophie J. Marritt, and David J. Richardson. "Enzyme Film Electrochemistry." In Electrochemical Processes in Biological Systems, 105–19. Hoboken, NJ: John Wiley & Sons, Inc, 2015. http://dx.doi.org/10.1002/9781118899076.ch5.

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Bachmeier, Andreas S. J. L. "The Direct Electrochemistry of Fuel-Forming Enzymes on Semiconducting Electrodes: How Light-Harvesting Semiconductors Can Alter the Bias of Reversible Electrocatalysts in Favour of H2 Production and CO2 Reduction." In Metalloenzymes as Inspirational Electrocatalysts for Artificial Photosynthesis, 157–77. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-47069-6_4.

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Brett, Christopher, and Ana Maria Oliveira-Brett. "DNA and Enzyme-Based Electrochemical Biosensors: Electrochemistry and AFM Surface Characterization." In Nanobioelectrochemistry, 105–25. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-642-29250-7_6.

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Guo, Liang-Hong, H. Allen, and O. Hill. "Direct Electrochemistry of Proteins and Enzymes." In Advances in Inorganic Chemistry, 341–75. Elsevier, 1991. http://dx.doi.org/10.1016/s0898-8838(08)60043-4.

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Conference papers on the topic "Electrochemistry of enzymes"

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Mazrouei, Roya, Bryan Kier, and Mohammad Shavezipur. "Development of Three-Dimensional MEMS Biochemical Sensors for Low Concentration Aqueous Solutions." In ASME 2019 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. American Society of Mechanical Engineers, 2019. http://dx.doi.org/10.1115/detc2019-98071.

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Abstract Three-dimensional biochemical sensors are developed that can be used for chemical and biological detection in aqueous solutions and suspensions. The sensors are fabricated using a standard polycrystalline silicon process, PolyMUMPs, and can detect chemicals and biomarkers in low concentrations in near real time. The sensors made of a stack of electrodes allowing the solution to occupy the space between the layers of electrodes and have a larger interface with the electrodes. The sensors use electrochemistry impedance spectroscopy (EIS) for detection and therefore increasing the solution-electrode interface improves the sensitivity of the sensor. To demonstrate the applicability of the proposed sensor design, experimental measurements are used to characterize and compare the 3D sensors with conventional 2D interdigitated sensors. Diethylhexyl phthalate (DEHP) solution is used as the target chemical, and the 2D and 3D biochemical sensors are exposed to different concentrations of DEHP solution. An LCR meter is used to sweep the frequency and determine the impedance of the sensor-solution combination. The test results show that the three-dimensional sensors have higher sensitivity than 2D interdigitated ones verifying the advantage of the new sensor design over existing conventional sensors. The proposed sensors can also be used for detection of biological markers such as cells, proteins and enzymes in aqueous solutions.
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