Direct electron transfer based enzymatic fuel cells

Falk, Magnus; Blum, Zoltan; Shleev, Sergey

doi:10.1016/j.electacta.2011.12.133

Cited by 241 publications

(185 citation statements)

References 97 publications

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“…1, left part). BOx has been widely used for a long time in clinical analysis [30,31] and biofuel cells [32][33][34][35][36], but the crystal structure was published only recently [37,38]. It is a highly similar to structures of other MCO and BOx contains a full complement of four copper ions per monomer, located in domains 1 and 3 [37,38].…”

Section: Introductionmentioning

confidence: 85%

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On the Possibility of Uphill Intramolecular Electron Transfer in Multicopper Oxidases: Electrochemical and Quantum Chemical Study of Bilirubin Oxidase

et al. 2012

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The catalytic cycle of multicopper oxidases (MCOs) involves intramolecular electron transfer (IET) from the Cu‐T1 copper ion, which is the primary site of the one‐electron oxidations of the substrate, to the trinuclear copper cluster (TNC), which is the site of the four‐electron reduction of dioxygen to water. In this study we report a detailed characterization of the kinetic and electrochemical properties of bilirubin oxidase (BOx) – a member of the MCO family. The experimental results strongly indicate that under certain conditions, e.g. in alkaline solutions, the IET can be the rate‐limiting step in the BOx catalytic cycle. The data also suggest that one of the catalytically relevant intermediates (most likely characterized by an intermediate oxidation state of the TNC) formed during the catalytic cycle of BOx has a redox potential close to 0.4 V, indicating an uphill IET process from the T1 copper site (0.7 V) to the Cu‐T23. These suggestions are supported by calculations of the IET rate, based on the experimentally observed Gibbs free energy change and theoretical estimates of reorganization energy obtained by combined quantum and molecular mechanical (QM/MM) calculations.

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Section: Introductionmentioning

confidence: 85%

“…[32][33][34][35][36]), as well as in homogeneous catalysis under certain conditions, e.g. at pH 7 and higher, the IET process might be the rate-limiting step determining the ultimate efficiency of BOx-based biocatalysis.…”

Section: Discussionmentioning

confidence: 99%

On the Possibility of Uphill Intramolecular Electron Transfer in Multicopper Oxidases: Electrochemical and Quantum Chemical Study of Bilirubin Oxidase

et al. 2012

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“…laccase and bilirubin oxidase (BOD)) modified electrodes have been extensively employed as cathodes of enzymatic biofuel cells (BFC) [94], which are of significant interest due to their potential applications as autonomous power suppliers [95,96].…”

Section: Multi-copper Oxidasesmentioning

confidence: 99%

An overview of dealloyed nanoporous gold in bioelectrochemistry

Xiao

Magner

2016

Bioelectrochemistry

113

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“…For our investigations, we chose a wellstudied enzyme, Myrothecium verrucaria bilirubin oxidase (MvBOx), which is widely used nowadays to design potentially implantable third-generation oxygen biosensors 22 and DETbased cathodes of biofuel cells. 4,17,23,24 Only AuNPs within the range of 20-80 nm were used to mitigate (i) quantum effects (electron coupling) in NPs (that are anticipated to be seen when employing metal particles with diameters below 5 nm) and (ii) to keep the dependence of van der Waals forces between metal and protein surfaces on NP radius negligible.…”

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confidence: 99%

The influence of nanoparticles on enzymatic bioelectrocatalysis

et al. 2014

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In nearly all papers concerning enzyme-nanoparticle based bioelectronic devices, it is stated that the presence of nanoparticles on electrode surfaces per se enhances bioelectrocatalysis, although the reasons for that enhancement are often unclear. Here, we report detailed experimental evidence that neither an overpotential of bioelectrocatalysis, nor direct electron transfer and bioelectrocatalytic reaction rates for an adsorbed enzyme depend on the size of nanoparticles within the range of 20-80 nm, i.e. for nanoparticles that are considerably larger than the enzyme molecules.Bioelectronics is a rapidly progressing interdisciplinary research eld 1 that aims to integrate biomaterials and electronic elements into functional devices which, among many other applications, can be used in high-tech, environmental, pharmaceutical and biomedical industries for sensing and power-generation purposes. High-performance direct electron transfer (DET)-based bioelectrocatalytic reactions at low overpotentials are needed to design sensitive, selective, and efficient third-generation (DET-based) bioelectronic devices, e.g. biosensors 2,3 and biofuel cells, 4,5 since third-generation bioelectronics are simple, non-toxic, and potentially miniaturisable down to nm scale. Nanostructuring electrode surfaces for enzyme-based bioelectronics is important because, in most cases, "planar" biodevices, i.e. designed without articial nanodecoration of electrodes, show very little or no electron transfer (ET) between immobilised redox enzymes and unmodied surfaces. The commonly offered explanation for "enzyme nanowiring" is an appropriate orientation of proteins on nanomaterials for ET reactions. Facile and effective bioelectrocatalysis has been shown in many papers, where different mono-and multi-centre redox enzymes, such as horseradish peroxidase, 6 glucose oxidase, 7-10 superoxide dismutase, 11 and cellobiose dehydrogenase, 12 with blue multicopper oxidases (MCOs), 13-18 respectively, are immobilised on different nanomaterials, e.g. metal and carbon nanoparticles (NPs) and nanotubes, graphene, nanoporous materials, etc. As a major proof for the enhancement of bioelectrocatalytic reactions, large bioelectrocatalytic currents that originate from nanostructured electrodes modied with oxidoreductases are usually presented. However, it should be emphasised that electrocatalysis is not actually related to the current increase, but should result in the decrease of an overpotential, which is quite rarely addressed in the case of bioelectrocatalytic reactions. Moreover, even for a particular enzyme, e.g. Trametes hirsuta laccase (ThLc), and a particular material, e.g. gold (Au), contradictory situations for different nanostructures can be found in the literature: the use of gold NPs (AuNPs) and nanoporous Au was shown to facilitate the DET-based bioelectrocatalytic reduction of oxygen (O 2 ), 13,18 whereas Aumodied nano-/microstructured silicon chips with the immobilised enzyme displayed very limited DET-based activity. 19Furthermore, two op...

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Direct electron transfer based enzymatic fuel cells

Cited by 241 publications

References 97 publications

On the Possibility of Uphill Intramolecular Electron Transfer in Multicopper Oxidases: Electrochemical and Quantum Chemical Study of Bilirubin Oxidase

On the Possibility of Uphill Intramolecular Electron Transfer in Multicopper Oxidases: Electrochemical and Quantum Chemical Study of Bilirubin Oxidase

An overview of dealloyed nanoporous gold in bioelectrochemistry

The influence of nanoparticles on enzymatic bioelectrocatalysis

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