Induced-fit binding of laccase to gold and carbon electrodes for the biological fuel cell applications

Karaskiewicz, Maciej; Majdecka, Dominika; Więckowska, Agnieszka; Biernat, Jan F.; Rogalski, Jerzy; Bilewicz, Renata

doi:10.1016/j.electacta.2013.08.024

Cited by 19 publications

(14 citation statements)

References 29 publications

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“…If the C FDH(FAD) and C FDH(FADH2) are kept constant, the above equation can be simplified to [Eqs. (5), (6)]:…”

Section: Resultsmentioning

confidence: 99%

“…The very first reports on DET with a redox active protein were published as far back as 1977, when Eddowes and Hill [3] and Yeh and Kuwana [4] independently showed that cytochrome c on bipyridyl-modified gold and tindoped indium oxide electrodes, respectively, showed virtually reversible electrochemistry. After that, DET was reported for peroxidases, [5] laccases, [6] and ferredoxins; [7] however, it is worth mentioning that no solid evidence could be provided to support the DET mechanism in the case of the most common enzyme in bioelectrochemistry -native glucose oxidase. [8] Although DET is observed only for a number of redox enzymes, it is one of the most important and interesting subjects in this field.…”

Section: Introductionmentioning

confidence: 99%

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Fructose Dehydrogenase Electron Transfer Pathway in Bioelectrocatalytic Reactions

Kizling

Bilewicz

2017

ChemElectroChem

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We present kinetic and mechanistic studies of fructose oxidation by fructose dehydrogenase (FDH) using the electrochemical methods of stationary and rotating disk voltammetry. FDH was physically adsorbed on unmodified multiwalled carbon nanotubes (MWCNT) to study direct electron transfer (DET) parameters, and for comparison an MWCNT with an adsorbed pyrene derivative of naphthoquinone employed as the mediator in mediated electron transfer, MET, was also examined. Kinetic parameters, such as the number of electrons transferred, the turnover number, and the electron transfer rate constant, were calculated. Comparison of the non-turnover and catalytic behaviour revealed the role of the heme c active site in the electron transfer of FDH. It was also shown that a mediator with a sufficiently low formal potential, such as the naphthoquinone, substitutes for the heme c site in the electron transfer to the electrode. The kinetic parameters of the processes proved that the application of the mediator results in an increase in the rate of fructose catalytic oxidation compared to that of the DET oxidation process.

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“…If the C FDH(FAD) and C FDH(FADH2) are kept constant, the above equation can be simplified to [Eqs. (5), (6)]:…”

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Fructose Dehydrogenase Electron Transfer Pathway in Bioelectrocatalytic Reactions

Kizling

Bilewicz

2017

ChemElectroChem

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“…They are widely used in a variety of industrial branches including paper, textile, food, cosmetics, but also as recognition element in biosensors for phenolic compounds . Since they were the first enzymes which effectively catalyze the cathodic reduction of dissolved oxygen at (carbon) electrodes they have been frequently applied as biocatalyst for oxygen reduction in biofuel cells …”

Section: Introductionmentioning

confidence: 99%

Electrosynthesized Molecularly Imprinted Polymer for Laccase Using the Inactivated Enzyme as the Target

Yarman

2018

Bulletin Korean Chem Soc

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The first molecularly imprinted polymer (MIP) for the recognition of the copper‐enzyme laccase was successfully prepared by electropolymerizing scopoletin in the presence of alkaline‐inactivated enzyme. Laccase‐MIP and the control polymer without laccase (nonimprinted polymer, NIP) were characterized by voltammetry using the redox marker ferricyanide. After electropolymerization, the signals for ferricyanide for both the MIP and the NIP were almost completely suppressed and increased after removal of the target from the polymer layer. Rebinding of both inactivated and active laccase decreased the ferricyanide peak currents to almost equal extent. The relative decrease of signal suppression approached saturation above 10 nM. Furthermore, the surface activity of rebound laccase toward the oxidation of catechol was investigated. The surface activity approached saturation above 10 nM, a value close to the value of the measurements with ferricyanide. Interaction of NIP with laccase brought about a six times smaller signal of catechol oxidation.

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“…Mediators may lead to unwanted reactions or leach to the solution, and if coimmobilized with the enzyme, they may not be sufficiently active anymore. To remove the need of mediators and to find the optimal way of enzyme immobilization at the electrode surface have been major goals of recent work in this area [19][20][21][22][23]. The carbon nanoparticles, e.g.…”

Section: Introductionmentioning

confidence: 99%

Nanostructuring carbon supports for optimal electrode performance in biofuel cells and hybrid fuel cells

Majdecka

Bilewicz

2015

J Solid State Electrochem

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The efficiencies of dioxygen reduction on common carbonaceous materials were compared using voltammetry and fuel cell measurements. Carbon paper (CP), carbon fibre (CF) or carbon cloth (CC) conducting supports were covered under water pump pressure with multiwalled carbon nanotubes (MWCNTs) to increase the working surface of the electrode, improve connectivity with enzyme molecules and provide direct electron transfer. Laccase was the biocathode catalyst catalyzing 4-electron reduction of oxygen to water on the nanostructured electrode. CP carbon paper was selected as the favourable electrode substrate, since it provided best durability holding firmly the carbon nanotubes together with the enzyme at the electrode surface. Zinc disc or fructose dehydrogenase was used as anode in the hybrid fuel cell and biofuel cell, respectively. The characteristics under externally applied resistances and potential-time dependencies under flowing solution conditions were evaluated. The hybrid fuel cell based on Zn anode and CP supported laccase cathode gave the best results in terms of power and open circuit potential (OCP). The full biofuel cell based on laccase and fructose dehydrogenase shows lower OCP but the power-time dependencies were similar to those of the hybrid biofuel cell. The nanostructured surfaces show good supercapacitor properties due to the presence of carbon nanotubes at the electrode surface. The fuel cells undergo self-charging/discharging and, therefore, can be conveniently employed in pulsed-work regime to power external devices.

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Induced-fit binding of laccase to gold and carbon electrodes for the biological fuel cell applications

Cited by 19 publications

References 29 publications

Fructose Dehydrogenase Electron Transfer Pathway in Bioelectrocatalytic Reactions

Fructose Dehydrogenase Electron Transfer Pathway in Bioelectrocatalytic Reactions

Electrosynthesized Molecularly Imprinted Polymer for Laccase Using the Inactivated Enzyme as the Target

Nanostructuring carbon supports for optimal electrode performance in biofuel cells and hybrid fuel cells

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