Direct bioelectrocatalysis at electrodes modified with D-gluconate dehydrogenase.

Ikeda, Tokuji; Fushimi, Fumiyoshi; Miki, Koujiro; Senda, Mitsugi

doi:10.1271/bbb1961.52.2655

Cited by 33 publications

(5 citation statements)

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“…Therefore, the deviation from the straight line at increased x 1/2 is ascribed to the interfacial electron transfer kinetic limitation in part. Such behavior has been frequently observed in enzyme-catalyzed electrochemical systems without mediators [36][37][38][39][40][41] and has been explained by a model that there exists a wide distribution in the standard interfacial electron transfer rate constant due to the random orientation of adsorbed enzyme on the electrode surface and that large overpotential is needed to exceed the enzymatic turnover rate constant for disordered enzyme molecules exhibiting longer electron tunneling distance between active site in enzyme and electrode surface, where the current is expressed by the summation of the contribution from the catalytic reactions of all enzymes on the electrode surface [38,41]. The interfacial electron transfer rate (tunneling distance) would also depend on the microscopic surface structures such as crevices and asperities.…”

Section: Laccase-catalyzed Electrochemical Reduction Of Oxygenmentioning

confidence: 70%

Diffusion‐Controlled Oxygen Reduction on Multi‐Copper Oxidase‐Adsorbed Carbon Aerogel Electrodes without Mediator

2007

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Bioelectrocatalytic reduction of O2 into water was archived at diffusion‐controlled rate by using enzymes (laccase from Trametes sp. and bilirubin oxidase from Myrothecium verrucaria, which belong to the family of multi‐copper oxidase) adsorbed on mesoporous carbon aerogel particle without a mediator. The current density was predominantly controlled by the diffusion of dissolved O2 in rotating‐disk electrode experiments, and reached a value as large as 10 mA cm–2 at 1 atm O2, 25 °C, and 8,000 rpm on the laccase‐adsorbed electrode. The overpotential of the bioelectrocatalytic reduction of O2 was 0.4–0.55 V smaller than that observed on a Pt disk electrode. Without any optimization, the laccase‐adsorbed biocathode showed stable current intensity of the O2 reduction in an air‐saturated buffer at least for 10 days under continuous flow system.

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Section: Laccase-catalyzed Electrochemical Reduction Of Oxygenmentioning

confidence: 70%

Diffusion‐Controlled Oxygen Reduction on Multi‐Copper Oxidase‐Adsorbed Carbon Aerogel Electrodes without Mediator

2007

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“…The current appeared to increase with the electrode potential. Such situations have been reported in the literature on DET bioelectrocatalysis [11,12,[52][53][54][55], and the potential-dependent linear increase in the catalytic current is ascribed to the wide spectrum of surface electrode kinetics due to random orientation of the adsorbed enzymes [54][55][56]. Differences in orientation cause the differences in the distance between the redox site of adsorbed enzymes and electrodes.…”

Section: Catalytic Activity Of M510l and M510q Cueosmentioning

confidence: 81%

Direct Electrochemistry of CueO and Its Mutants at Residues to and Near Type I Cu for Oxygen‐Reducing Biocathode

et al. 2009

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CueO, a multi‐copper oxidase (MCO) occurring in Escherichia coli, catalyses a four‐electron reduction of O2 in a direct electron transfer (DET) mechanism with very high electrocatalytic activity on carbon aerogel electrodes. However, the overpotential of CueO is greater than that in other MCOs. By understanding the redox properties of CueO, we attempted to reduce this overpotential. Direct electrochemistry of CueO on carbon aerogel electrodes showed a pair of redox waves derived from the type I (T1) Cu site with a redox potential ($E {^{\circ \prime} \atop {\rm T1}} $) of 0.28 V versus Ag|AgCl at pH 5.0. Dependence of $E {^{\circ \prime} \atop {\rm T1}} $ on pH suggests the participation of proton transfer and acid–base equilibrium of some amino acid residue. The shape of the catalytic current is consistent with the T1 site being an inlet of electrons in the DET bioelectrocatalysis of O2, in which case the overpotential could be reduced by shifting $E {^{\circ \prime} \atop {\rm T1}} $ towards the positive potential. To achieve this, we created mutants of CueO at M510, which is the axial ligand of the T1 Cu, and at D439, which forms a hydrogen bond with His443 coordinated with the T1 Cu. Two mutants, M510L and D439A, successfully reduced the overpotential.

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“…The experimental evidence of DET has been reported in the literature for both low molecular weight electrontransfer proteins and enzymes with large, more complicated structures such as laccase, peroxidase, and glucose oxidase [1, 9 -11, 18, 24]. The DET has been observed with multicofactor redox enzymes, such as flavohemeprotein gluconate dehydrogenase [12] and quinohemoproteins [13]. For alcohol dehydrogenase and fructose dehydrogenase the DET between the electrode and active site of the enzyme has been reported [14 -17].…”

Section: Introductionmentioning

confidence: 99%

Direct Bioelectrocatalysis of PQQ‐Dependent Glucose Dehydrogenase

2007

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The direct bioelectrocatalysis was demonstrated for pyrroloquinoline quinone-dependent glucose dehydrogenase (PQQ-dependent GDH) covalently attached to single-walled carbon nanotubes (SWNTs). The homogeneous ink-like SWNT suspension was used for both creating the SWNT network on the microelectrode carbon surface and for enzyme immobilization. Functionalization of the SWNT surface by forming active ester groups was found to considerably enhance SWNT solubility in water with a range from 0.1 to 1.0 mg/mL. The PQQ-dependent GDH immobilized on the surface of the SWNTs exhibited fast heterogeneous electron transfer with a rate constant of 3.6 s À1 . Moreover, the immobilized PQQ-dependent GDH retained its enzymatic activity for glucose oxidation. A fusion of PQQ-dependent GDH with SWNTs has a great potential for the development of low-cost and reagentless glucose sensors and biofuel cells.

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Direct bioelectrocatalysis at electrodes modified with D-gluconate dehydrogenase.

Abstract: D-Gluconate dehydrogenase isolated from Pseudomonas fluorescens was immobilized on the surfaces of carbon and gold electrodes by irreversible adsorption. The electrodes with the adsorbed enzyme produced anodic currents in solutions containing D-gluconate. The currents were at

Cited by 33 publications

References 1 publication

Diffusion‐Controlled Oxygen Reduction on Multi‐Copper Oxidase‐Adsorbed Carbon Aerogel Electrodes without Mediator

Diffusion‐Controlled Oxygen Reduction on Multi‐Copper Oxidase‐Adsorbed Carbon Aerogel Electrodes without Mediator

Direct Electrochemistry of CueO and Its Mutants at Residues to and Near Type I Cu for Oxygen‐Reducing Biocathode

Direct Bioelectrocatalysis of PQQ‐Dependent Glucose Dehydrogenase

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