Bioelectrocatalysis at electrodes coated with alcohol dehydrogenase, a quinohemoprotein with heme c serving as a built-in mediator

Ikeda, Tokuji; Kobayashi, Daisuke; Matsushita, Fumio; Sagara, Takamasa; Niki, Katsumi

doi:10.1016/0022-0728(93)87058-4

Cited by 138 publications

(75 citation statements)

References 25 publications

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“…6 The exact structure of PQQ-PDH is unknown except for the fact there are large subunits at approximately 80 kDa and 60 kDa that are most likely heme-c containing moieties similar to that of those found in PQQ-ADH and PQQ-AldDH (which are known). In addition PQQ-PDH contains two smaller subunits at approximately 40 kDa and 18 kDa.…”

Section: Resultsmentioning

confidence: 99%

Bioelectrocatalysis of Pyruvate with PQQ-dependent Pyruvate Dehydrogenase

Treu

Sokic-Lazic

2010

ECS Trans.

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Although pyruvate has not been considered as a fuel for an enzymatic biofuel cell, there are dehydrogenase enzyme capable of oxidizing pyruvate. This paper details the discovery of a pyrroloquinoline quinone-dependent pyruvate dehydrogenase (PQQ-PDH) in Gluconobacter species. A method was developed to isolate and purify PQQ-PDH from Gluconobacter, along with the characterization of the purified enzyme. It was found that the purified enzyme can undergo direct electron transfer at carbon electrodes surfaces, which allowed for its incorporation into a pyruvate biofuel cell. It was also found that PQQ-PDH lacks substrate specificity, which minimizes its usefulness in many sensor applications, but is advantageous for deep oxidation in biofuel cell anodes.

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Section: Resultsmentioning

confidence: 99%

Bioelectrocatalysis of Pyruvate with PQQ-dependent Pyruvate Dehydrogenase

Treu

Sokic-Lazic

2010

ECS Trans.

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“…The anodic steady-state catalytic current density caused by DETtype bioelectrocatalytic oxidation current (i s ) under conditions without the concentration polarization of the substrate near a given electrode is given by 22,23 …”

Section: Steady-state Current At a Planar Electrodementioning

confidence: 99%

Effects of Mesoporous Structures on Direct Electron Transfer-Type Bioelectrocatalysis: Facts and Simulation on a Three-Dimensional Model of Random Orientation of Enzymes

et al. 2017

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Direct electron transfer (DET)-type bioelectrocatalytic waves of bilirubin oxidase (BOD)-catalyzed O 2 reduction and [NiFe] hydrogenase (H 2 ase)-catalyzed H 2 oxidation are very small and un-detectable using glassy carbon (GC) electrodes, respectively; however, clear catalytic waves are observed when the enzymes are adsorbed on Ketjen black-modified GC (KB-GC) electrodes, in which KB provides mesopores for DET-type bioelectocatalysis. To explain the phenomena, we focus on the curvature effect of mesoporous structures on long range electron transfer kinetics and simulate steady-state voltammograms catalyzed by model redox enzymes adsorbed with a random orientation on planar and mesoporous electrodes based on a three-dimensional model. In the simulation, we assume a spherical enzyme with a radius of r, an active site located at a certain distance from the center of the enzyme, and a spherical pore with a radius of R p in mesoporous electrodes in which the enzyme is trapped and adsorbed. The simulation reveals that mesoporous electrodes provide platforms suitable for DET-type bioelectrocatalysis of enzymes when R p becomes close to r. Such curvature effects of mesoporous electrodes become especially notable for larger sized enzymes. Furthermore, the simulation reproduces the experimental data of BOD-and H 2 asecatalyzed DET-type waves by considering the crystal structures of the enzymes. This work will open a route to improve the kinetic performance of the DET-type bioelectrocatalysis that has become very important in its practical application to a variety of bioelectrochemical devices.

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“…[16] The catalytic domain is a flavin adenine dinucleotide (FAD)-dependent dehydrogenase domain (DH CDH ) that catalyzes the oxidation of a variety of saccharides depending on the fungal source of the enzyme. The other domain, a cytochrome (CYT CDH ), which contains an exposed heme b, acts as a built-in mediator, [17] transferring the electrons from the reduced DH CDH to the final electron acceptor, recently found to be a copper-dependent monooxygenase participating in the breakdown of wood.…”

Section: Introductionmentioning

confidence: 99%

Highly Efficient Membraneless Glucose Bioanode Based on Corynascus thermophilus Cellobiose Dehydrogenase on Aryl Diazonium‐Activated Single‐Walled Carbon Nanotubes

2014

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We present an approach for electrode modification by using the oxidoreductase cellobiose dehydrogenase from the ascomycete Corynascus thermophilus (CtCDH). CtCDH is a two‐domain enzyme, in which the catalytic dehydrogenase domain (DHCDH) hosts flavin adenine dinucleotide (FAD) as cofactor and is connected through a flexible linker to a small cytochrome domain with a heme b cofactor (CYTCDH). This domain is responsible for the electron transfer from DHCDH to macromolecular electron acceptors, and is capable of direct electron transfer (DET) with electrode surfaces. CtCDH is optimal at pH values between 7 and 9 and exhibits one of the lowest apparent KM values for glucose (2.4×104 μM) in contrast to the majority of other CDHs, which have acidic optimal pH values and have very low or no activity for glucose. Glassy carbon (GC) electrodes were modified by drop‐casting single‐walled carbon nanotubes (SWCTs) and further modifying with aryl diazonium salts (DS). When adsorbed on such GC‐SWCT‐DS electrodes, CYTCDH showed efficient DET in the presence of a substrate. Six different functional groups for the aryl amines were studied and compared to non‐DS modified GC‐SWCT electrodes. The charge of the grafted aryl amines was investigated and it was found that surfaces modified with aniline, 4‐aminophenol, and 4‐aminobenzoic acid (ABA) contain negative charges at pH 7.4. On the other hand, surfaces modified with p‐phenylenediamine (PD), N,N‐dimethyl‐p‐phenylenediamine, and N,N‐diethyl‐p‐phenylenediamine remain uncharged. To date, the highest DET current density (JMAX=32.5 μA cm−2 for lactose and JMAX=16.2 μA cm−2 for glucose) for a CDH‐modified electrode at human physiological pH can be obtained by using a GC‐SWCT‐ABA CtCDH modified electrode. The use of glutaraldehyde (GA) in GC‐SWCT‐PD‐modified electrodes increases the JMAX twofold. The modified electrodes with DS showed a more negative onset potential for the catalytic current. For GC‐SWCT‐ABA modified electrodes and GC‐SWCT‐PD with GA, a change in the onset potential of −62 and −66 mV, respectively, was found compared with non‐DS modified electrodes. The prepared bioanodes show a loss in response current of 15 % after 9 days of continuous measurements from the original signal in 5 mM glucose, using 50 mM phosphate buffer solution at pH 7.40 at 37 °C.

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Bioelectrocatalysis at electrodes coated with alcohol dehydrogenase, a quinohemoprotein with heme c serving as a built-in mediator

Cited by 138 publications

References 25 publications

Bioelectrocatalysis of Pyruvate with PQQ-dependent Pyruvate Dehydrogenase

Bioelectrocatalysis of Pyruvate with PQQ-dependent Pyruvate Dehydrogenase

Effects of Mesoporous Structures on Direct Electron Transfer-Type Bioelectrocatalysis: Facts and Simulation on a Three-Dimensional Model of Random Orientation of Enzymes

Highly Efficient Membraneless Glucose Bioanode Based on Corynascus thermophilus Cellobiose Dehydrogenase on Aryl Diazonium‐Activated Single‐Walled Carbon Nanotubes

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