Hydrogen peroxide produced by glucose oxidase affects the performance of laccase cathodes in glucose/oxygen fuel cells: FAD-dependent glucose dehydrogenase as a replacement

Milton, Ross D.; Giroud, Françoise; Thumser, Alfred E.; Minteer, Shelley D.; Slade, Robert C. T.

doi:10.1039/c3cp53351d

Cited by 101 publications

(92 citation statements)

References 43 publications

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“…20 Most reported bioelectrodes employing ChOx are based on the electro-oxidation or electro-reduction of H 2 O 2 , which has been shown to act as an inhibitor to commonly-used O 2 -reducing cathodic enzymes (laccase and bilirubin oxidase). 12 Thereby, the production of H 2 O 2 can affect the performance and stability of EFCs. It is also important to note that biosensors using ChOx to quantify cholesterol as a function of H 2 O 2 are dependent on and limited by the availability of O 2 , which can affect the reproducibility of sample analysis.…”

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confidence: 99%

“…5,[9][10][11] Metalloenzymes, such as laccases, bilirubin oxidase and peroxidase, are generally used at the cathode of EFCs allowing the bioelectrocatalytic reduction of O 2 or peroxides to H 2 O. [12][13][14][15] In addition to carbohydrates, other types of enzyme substrates have been reported as fuels such as alkanes, carboxylic acids, and other organic molecules. 1,16,17 Cholesterol, a sterol lipid, is a potential fuel for EFCs that can be oxidized to cholest-4-ene-3-one by some oxidases and dehydrogenases.…”

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confidence: 99%

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Cholesterol as a Promising Alternative Energy Source: Bioelectrocatalytic Oxidation Using NAD-Dependent Cholesterol Dehydrogenase in Human Serum

Quah

Abdellaoui

Milton

et al. 2016

J. Electrochem. Soc.

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Cholesterol is an essential structural component of mammalian cells, although elevated concentrations of cholesterol in the human body are linked to atherosclerotic disease. In this context, monitoring physiological cholesterol concentrations is of great interest in medical fields and the concept of producing electrical energy from cholesterol is interesting. In this work, we report the bioelectrocatalytic oxidation of cholesterol with the use of nicotinamide adenine dinucleotide-(NAD) dependent cholesterol dehydrogenase (ChDH) as an alternative enzyme to the commonly-used cholesterol oxidase (ChOx) in bioelectronic applications. To achieve bioelectrocatalytic cholesterol oxidation, ChDH was combined with diaphorase (DH) in a bilayer fashion, whereby DH acts as an intermediary enzyme to facilitate NADH oxidation at a ferrocene redox polymer. Characterization of the resulting bioanode identifies a linear cholesterol response range from 5 μM to 200 μM, with an associated sensitivity of 60.12 mA cm −2 M −1 . Furthermore, an O 2 -reducing biocathode incorporating bilirubin oxidase (BOx) was combined with the cholesterol bioanode into a complete cholesterol/O 2 membrane-less enzymatic fuel cell (EFC).

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Cholesterol as a Promising Alternative Energy Source: Bioelectrocatalytic Oxidation Using NAD-Dependent Cholesterol Dehydrogenase in Human Serum

Quah

Abdellaoui

Milton

et al. 2016

J. Electrochem. Soc.

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“…AcMWCNTs have been shown to act as an efficient docking moiety for DET between laccase and an electrode. 4,[11][12][13][14] The onset potential for the direct bioelectrocatalytic reduction of O 2 to H 2 O by laccase was found to begin at approximately +670 mV (vs. SCE) at pH 4.5. In contrast, the onset potential for the mediated bioelectrocatalytic reduction of O 2 to H 2 O by laccase via MET was found to begin at approximately +640 mV (vs. SCE) at pH 4.5.…”

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confidence: 99%

“…While it appears evident that H 2 O 2 can significantly affect the catalytic/bioelectrocatalytic performance of laccase, the mechanism by which H 2 O 2 inhibits laccase remains unclear; a single study investigating the inhibition of laccase by F − previously proposed that H 2 O 2 binds to the T2 Cu of laccase. 22 Although the authors have previously demonstrated the reversible inhibition of laccase by H 2 O 2 on DET-type bioelectrodes (incorporating anthracene-modified multi-walled carbon nanotubes (AcMWCNTs)), 12,13 an inhibition mechanism for the reversible inhibition of laccase (by H 2 O 2 ) does not currently exist. Thus, this study investigates and reports the reversible inhibition mechanism by which H 2 O 2 inhibits laccase, in both an MET and DET context.…”

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confidence: 99%

“…z E-mail: minteer@chem.utah.edu (GOx)) which utilize O 2 as their natural electron acceptor can produce significant quantities of H 2 O 2 (taking place as a side-reaction at bioanodes) to rapidly inhibit laccase and its bioelectrocatalytic reduction of O 2 , in both MET and DET. 12,20,21 This loss in bioelectrocatalytic performance at the EFC biocathode can result in an overall loss-of-performance of the EFC. While it appears evident that H 2 O 2 can significantly affect the catalytic/bioelectrocatalytic performance of laccase, the mechanism by which H 2 O 2 inhibits laccase remains unclear; a single study investigating the inhibition of laccase by F − previously proposed that H 2 O 2 binds to the T2 Cu of laccase.…”

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Investigating the Reversible Inhibition Model of Laccase by Hydrogen Peroxide for Bioelectrocatalytic Applications

Milton¹

2014

J. Electrochem. Soc.

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The reversible inhibition of laccase by H 2 O 2 as a bioelectrocatalyst was studied in mediated-and direct electron transfer-based configurations to understand the differences in mechanism. The reversible inhibition of laccase follows a noncompetitive inhibition model when 2,2 -azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) is used as an electron mediator, whereas laccase is inhibited by an uncompetitive inhibition model when anthracene-moieties are used to intelligently "dock" laccase to electrodes (consisting of multi-walled carbon nanotubes, MWCNTs) which afford direct electron transfer (DET). This further confirms the efficient orientation of laccase onto suitably-designed docking moieties for bioelectrocatalysis applications. 1-5 Along with some other MCOs (such as bilirubin oxidase, BOx), laccase contains 3 different copper centers. A type-1 copper center (T1 Cu) is proximally located within the enzyme structure and is responsible for the single-electron oxidation of phenolic-type substrates, and a further type-2 copper center (T2 Cu) and 2 further type-3 copper centers (T3 Cu) are combined in a tri-nuclear cluster (TNC), which is responsible for the 4-electron reduction of O 2 to H 2 O. Following the oxidation of substrates at the T1 Cu site, electrons are quickly and individually transferred to the TNC via a His-Cys-His tripeptide chain.6,7 Although laccase (from Trametes versicolor) is reported to optimally reduce O 2 at acidic pH (which may limit its incorporation within implantable EFCs) further complications can be found within a physiological setting, where laccase can be inhibited by Cl − (approximately 150 mM physiological concentration) via a competitive inhibition model whereby Cl − can compete against certain electron mediators at the T1 Cu site of the enzyme. 8,9 Laccase can be intelligently orientated (or "docked") onto electrode architectures whereby moieties with structural similarities to the natural substrates of laccase (oxidized at the T1 site) are incorporated on specifically-designed electrode architectures, which subsequently allow direct electron transfer (DET).2,4,10-14 Efficient mediated electron transfer (MET) has also been demonstrated using mediators such as 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) or osmium-based complexes 1,[15][16][17] and comparison between orientationally-driven DET and MET of laccase (with ABTS) has been reported, contrasting catalytic current densities that can be achieved with both electron transfer methods.18 Such electrode architectures can be capable of demonstrating increased resistance to Cl − inhibition, since the moieties used for docking can efficiently out-compete Cl − at the T1 site and therefore permit electron transfer. 9,13,19 Recent studies, however, determined that certain membrane-less EFC configurations (favorable to lower overall device cost and size) can present further problems for laccase-based biocathodes, whereby oxidoreductases utilized at EFC bioanodes (such as glucose oxidase * Electrochemical Soc...

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Effect of Multi‐Walled Carbon Nanotubes on Glucose Oxidation by Glucose Oxidase or a Flavin‐Dependent Glucose Dehydrogenase in Redox‐Polymer‐Mediated Enzymatic Fuel Cell Anodes

Osadebe

Leech

2014

ChemElectroChem

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The addition of multi‐walled carbon nanotubes (MWCNTs) to enzymatic electrodes based on either glucose oxidase (GOx), or an oxygen‐insensitive flavin adenine dinucleotide‐dependent glucose dehydrogenase (FADGDH), increases the amount of {Os(4,4′‐dimethyl‐2,2′‐bipyridine)2[poly(vinylimidazole)]10Cl}Cl redox polymer at the electrode surface, indicating that MWCNTs provide a surface for the immobilisation of film components. Glucose oxidation is highest for films with 68 % (w/w) MWCNTs, and a decrease is observed with larger amounts; this decrease is related to a decrease in retained enzyme activity. Enzymatic electrodes provide 4.2 mA cm−2 current density at 0.12 V versus Ag/AgCl, for GOx‐based electrodes, compared to 2.7 mA cm−2 for FADGDH‐based electrodes in 50 mM phosphate‐buffered saline containing 150 mM NaCl at 37 °C. Current densities of 0.52 and 1.1 mA cm−2 are obtained for FADGDH and GOx‐based electrodes, respectively, operating at physiologically relevant 5 mM glucose concentrations. These enzymatic electrodes, thus, show promise for application as anodes in enzymatic fuel cells for in vivo or ex vivo power generation.

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Hydrogen peroxide produced by glucose oxidase affects the performance of laccase cathodes in glucose/oxygen fuel cells: FAD-dependent glucose dehydrogenase as a replacement

Cited by 101 publications

References 43 publications

Cholesterol as a Promising Alternative Energy Source: Bioelectrocatalytic Oxidation Using NAD-Dependent Cholesterol Dehydrogenase in Human Serum

Cholesterol as a Promising Alternative Energy Source: Bioelectrocatalytic Oxidation Using NAD-Dependent Cholesterol Dehydrogenase in Human Serum

Investigating the Reversible Inhibition Model of Laccase by Hydrogen Peroxide for Bioelectrocatalytic Applications

Effect of Multi‐Walled Carbon Nanotubes on Glucose Oxidation by Glucose Oxidase or a Flavin‐Dependent Glucose Dehydrogenase in Redox‐Polymer‐Mediated Enzymatic Fuel Cell Anodes

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