Fully Oriented Bilirubin Oxidase on Porphyrin‐Functionalized Carbon Nanotube Electrodes for Electrocatalytic Oxygen Reduction

Lalaoui, Noémie; Goff, Alan Le; Holzinger, Michael; Cosnier, Serge

doi:10.1002/chem.201502377

Cited by 93 publications

(118 citation statements)

References 42 publications

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“…Typically, polyaromatic hydrocarbons (anthracene, naphthalene and derivatives thereof ) are the most commonly employed orientational agents [40 -44]. In the case of BOx, efficient DET can be afforded by immobilization onto multi-walled carbon nanotubes, using charged multi-walled carbon nanotubes, immobilized polyaromatic hydrocarbons and even natural substrates (bilirubin and its metabolites) [33,[45][46][47][48][49].…”

Section: Direct Bioelectrocatalysis Of Metalloenzymesmentioning

confidence: 99%

Direct enzymatic bioelectrocatalysis: differentiating between myth and reality

Milton

Minteer

2017

J. R. Soc. Interface.

165

148

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Enzymatic bioelectrocatalysis is being increasingly exploited to better understand oxidoreductase enzymes, to develop minimalistic yet specific biosensor platforms, and to develop alternative energy conversion devices and bioelectrosynthetic devices for the production of energy and/or important chemical commodities. In some cases, these enzymes are able to electronically communicate with an appropriately designed electrode surface without the requirement of an electron mediator to shuttle electrons between the enzyme and electrode. This phenomenon has been termed direct electron transfer or direct bioelectrocatalysis. While many thorough studies have extensively investigated this fascinating feat, it is sometimes difficult to differentiate desirable enzymatic bioelectrocatalysis from electrocatalysis deriving from inactivated enzyme that may have also released its catalytic cofactor. This article will review direct bioelectrocatalysis of several oxidoreductases, with an emphasis on experiments that provide support for direct bioelectrocatalysis versus denatured enzyme or dissociated cofactor. Finally, this review will conclude with a series of proposed control experiments that could be adopted to discern successful direct electronic communication of an enzyme from its denatured counterpart.

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Section: Direct Bioelectrocatalysis Of Metalloenzymesmentioning

confidence: 99%

Direct enzymatic bioelectrocatalysis: differentiating between myth and reality

Milton

Minteer

2017

J. R. Soc. Interface.

165

148

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“…[21] The bioelectrodes were placed in an electrochemical cell containing 200 mmol L À 1 glucose in oxygen saturated buffer solution Figure 6A shows the obtained power profile of the resulting glucose biofuel cell. [21] The bioelectrodes were placed in an electrochemical cell containing 200 mmol L À 1 glucose in oxygen saturated buffer solution Figure 6A shows the obtained power profile of the resulting glucose biofuel cell.…”

Section: Performance Of the Bioanode In A Glucose/oxygen Biofuel Cellmentioning

confidence: 99%

Electrosynthesis of Pyrenediones on Carbon Nanotube Electrodes for Efficient Electron Transfer with FAD‐dependent Glucose Dehydrogenase in Biofuel Cell Anodes

et al. 2019

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A particularly efficient redox mediator for electron transfer between FAD-dependent glucose dehydrogenase (FAD-GDH) and carbon nanotube (CNT) based electrodes can be obtained via electrosynthetic oxidation of pyrene in aqueous buffer solution. 1 H-NMR spectroscopic studies reveal the formation of a 2 : 1 mixture of 1,6-pyrenedione and 1,8-pyrenedione at the electrode. The formed pyrenedione exhibits a well-defined surface-bound redox system at À 0.1 V vs. SCE and provides excellent electron transfer kinetics with this enzyme. Further-more, the π-system of pyrenedione allows improved stacking behavior with the CNT walls, leading to enhanced stabilities compared to commonly used mediators like naphthoquinone. The electrosynthesis of pyrenedione for catalytic glucose oxidation is optimal at pH 2 using cyclic voltammetry or chronoamerometry. It is envisioned that the electrosynthetic methodology can be expanded to form different redox mediators for a series of enzymes.[a] Dr.

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“…Catechol, hydroquinone, pyrogallol, and bilirubin which are catalytically oxidized by BOx were employed in modification of biocathodes [28]. Recent studies have focused on incorporating specific substrates of BOx such as bilirubin, quinones, syringaldazine, and protoporphyrin derivatives such as protoporphyrin IX iron (III) (PPFeIII), protoporphyrin IX dimethyl ester (PPDE), and octaethylporphyrin (OEP) towards appropriate orientation that can be convenient for DET-type electrocatalysis [36]. However no study has been previously done on hematin as substrate for BOx.…”

Section: Electrochemical Testing and Characterization Of Hemin/mentioning

confidence: 99%

“…Several literature studies show that hemin modified electrodes were extended in the catalysis and reduction of hydrogen peroxide [32][33][34], oxygen [35], and superoxide [31]. Utilization of hemin, protoporphyrin derivatives as pretreatment of the surface for improving the activity of BOx on cathode electrode has also been reported [36].…”

Section: Introductionmentioning

confidence: 99%

Enhancement of Electrochemical Performance of Bilirubin Oxidase Modified Gas Diffusion Biocathode by Porphyrin Precursor

Pinchon

Arugula

Pant

et al. 2018

Advances in Physical Chemistry

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Recent studies have focused on tailoring the catalytic currents of multicopper oxidase (MCO) enzymes-based biocathodes to enhance oxygen reduction. Biocathodes modified with natural substrates specific for MCO enzymes demonstrated drastic improvement for oxygen reduction. Performance of 1-pyrenebutanoic acid, succinimidyl ester (PBSE), and 2,5-dimethyl-1-phenyl-1H-pyrrole-3-carbaldehyde (Di-Carb) oriented bilirubin oxidase (BOx) modified gas diffusion biocathode has been highly improved by incorporating hematin, a porphyrin precursor as electron transfer enhancement moiety. Hematin modified electrodes demonstrated direct electron transfer reaction of BOx exhibiting larger O 2 reduction in current density in phosphate buffer solution (pH 7.0) without the need of a mediator. A remarkable improvement in the catalytic currents with 2.5-fold increase compared to non-hematin modified oriented BOx electrodes was achieved. Moreover, a mediatorless and compartmentless glucose/O 2 biofuel cell based on DET-type bioelectrocatalysis via the BOx cathode and the glucose dehydrogenase (GDH) anode demonstrated peak power densities of 1 mW/cm 2 at pH 7.0 with 100 mM glucose/10 mM NAD fuel. The maximum current density of 1.6 mA/cm 2 and the maximum power density of 0.4 mW/cm 2 were achieved at 300 mV with nonmodified BOx cathode, while 3.5 mA/cm 2 and 1.1 mW/cm 2 of current and power density were achieved with hematin modified cathode. The performance improved 2.4 times which attributes to the hematin acting as a natural precursor and activator for BOx activity enhancement.

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Fully Oriented Bilirubin Oxidase on Porphyrin‐Functionalized Carbon Nanotube Electrodes for Electrocatalytic Oxygen Reduction

Cited by 93 publications

References 42 publications

Direct enzymatic bioelectrocatalysis: differentiating between myth and reality

Direct enzymatic bioelectrocatalysis: differentiating between myth and reality

Electrosynthesis of Pyrenediones on Carbon Nanotube Electrodes for Efficient Electron Transfer with FAD‐dependent Glucose Dehydrogenase in Biofuel Cell Anodes

Enhancement of Electrochemical Performance of Bilirubin Oxidase Modified Gas Diffusion Biocathode by Porphyrin Precursor

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