High-Power Formate/Dioxygen Biofuel Cell Based on Mediated Electron Transfer Type Bioelectrocatalysis

Sakai, Kyosuke; Kitazumi, Yuki; Shirai, Osamu; Takagi, Kazuyoshi; Kano, Kenji

doi:10.1021/acscatal.7b01918

Cited by 54 publications

(44 citation statements)

References 60 publications

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“…1 Additionally, the theoretical potential difference of a HCOO − /O 2 enzymatic biofuel cell (EFC) (∼1.47 V) is attractive, being higher than that of a glucose/oxygen EFC (∼1.2 V). 2 Formic acid is also highly soluble in water and is liquid at room temperature. 2 Formate dehydrogenase (FDH) is an enzyme which can catalyze the reversible oxidation of formate to CO 2 according to the reaction: [3][4][5][6] HCOO − ← → CO 2 + 2e − + H + and different FDHs are classified into two major classes: metalindependent (nicotinamide adenine dinucleotide (NAD)-dependent enzymes) and metal-dependent enzymes.…”

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confidence: 99%

“…2 Formic acid is also highly soluble in water and is liquid at room temperature. 2 Formate dehydrogenase (FDH) is an enzyme which can catalyze the reversible oxidation of formate to CO 2 according to the reaction: [3][4][5][6] HCOO − ← → CO 2 + 2e − + H + and different FDHs are classified into two major classes: metalindependent (nicotinamide adenine dinucleotide (NAD)-dependent enzymes) and metal-dependent enzymes. NAD-dependent FDHs have been used in the past for formic acid/formate EFCs, but they have been plagued by the poor electrooxidation of NADH and poor stability of NAD + .…”

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confidence: 99%

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Molybdenum-Dependent Formate Dehydrogenase for Formate Bioelectrocatalysis in a Formate/O₂Enzymatic Fuel Cell

Şahin

Cai

Milton

et al. 2018

J. Electrochem. Soc.

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Formate/formic acid has been an intriguing fuel for fuel cells and biofuel cells over the last two decades. The common challenge with formate/formic acid biofuel cells has been the use of NAD-dependent formate dehydrogenase, which requires a diffusive cofactor and problematic cofactor regeneration systems. In this paper, we explore the bioelectro-oxidation of formate using Mo-containing formate dehydrogenase from E. coli (Mo-FDH) for development of a new HCOO − /O 2 enzymatic fuel cell (EFC). Mo-FDH was coupled with a benzylpropylviologen-based linear polyethylenimine (BPV-LPEI) redox polymer to fabricate a formate bioanode and laccase incorporated with anthracene-modified multi-walled carbon nanotubes (Ac-MWCNTs) to promote direct electron transfer was used for the O 2 biocathode. The resulting Mo-FDH/laccase EFC has an open-circuit potential of 1.28 ± 0.05 V, with corresponding maximum current and power densities of 17 ± 7 μA cm −2 and 18 ± 6 μW cm −2 , respectively. This FDH contains a molybdenum-coordinated selenocysteine (SeCys) residue, essential for catalytic activity, and two molybdopterin guanine dinucleotides (MGDs), with just one [4Fe-4S] cluster for electron transfer to and from the active site.13,14 Bassegoda et al. 13and Robinson et al. 15 showed that Mo-FDH from E.coli adsorbed on the surface of a graphite-epoxy rotating disk working electrode can catalyze the reversible interconversion of CO 2 and formate with direct electron transfer at ∼ −0.4 V vs. SHE (pH 6.8).16 However, the current densities of DET electrodes are lower than what is necessary for biofuel cell applications.In this study, we constructed a MET-type bioanode with Mo-FDH by employing a viologen-based redox polymer (benzylpropylviologen-modified linear poly(ethylenimine), BPV-LPEI) which is able to facilitate the bioelectrocatalytic oxidation of formate at low potentials. While a DET approach could theoretically offer improved open-circuit potentials of a resulting EFC, the current densities obtained from DET-based bioelectrodes is almost always dwarfed by those obtained from appropriately designed MET bioanodes, due to a combination of increased enzyme loading, the ability of redox polymers to undergo "self-exchange" (creating an expanded 3D network of electronically-connected yet immobilized enzyme) and increased interfacial electron transfer rates (k ET ) which are commonly poor for DET-based bioelectrodes.17,18 Therefore, we investigated a redox polymer with low oxidation potentials to ensure near theoretical OCPs for the EFC. Several different mechanisms for FDH-catalyzed formate oxidation have been proposed. 5,9,14,19,20 It was shown by Maia et al. that FDH requires an activation step by its reduction using viologen or an artificial reducer.9 Robinson et al. have proposed a reductive activation to create a stabilized form of the SeCys dissociated state and it was mentioned that this state is also possible upon incubation of the protein with reducing agents (such as sodium dithionite (DT)). 15,19 Thus, we evaluated the activat...

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confidence: 99%

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confidence: 99%

Molybdenum-Dependent Formate Dehydrogenase for Formate Bioelectrocatalysis in a Formate/O₂Enzymatic Fuel Cell

Şahin

Cai

Milton

et al. 2018

J. Electrochem. Soc.

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“…KB was used to construct mesoporous structures suitable for physically trapping the mediator and enzyme for METbioelectrocatalysis. 33 In addition, a large surface area is convenient to increase the enzymatic reaction rate on the electrode surface. Note here that the diffusion layers in the close vicinity of the mesoporous surface overlap with each other with time, resulting in a simple diffusion layer on the projected surface area.…”

Section: Resultsmentioning

confidence: 99%

Simultaneous Detection of Lactate Enantiomers Based on Diffusion-controlled Bioelectrocatalysis

et al. 2018

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Amperometric biosensors were constructed for the simultaneous detection of lactate enantiomers. The enantioselectivity of the sensor is based on NAD-dependent l- and d-lactate dehydrogenases that, respectively, oxidize l- and d-lactates into pyruvate. The NADH formed during the enzymatic reduction was catalytically oxidized at Meldola's blue-adsorbed mesoporous electrodes. Stable amperometric measurements were performed in a two-electrode system using Ag|AgCl|sat. KCl as a counter electrode via a salt bridge. The response of the sensor reached a pseudo-steady state within 60 s. The agreement of the sensitivities for l- and d-lactates and the pseudo-steady-state characteristics of the sensors demonstrate that the current is strongly influenced by the diffusion of lactates at the edge of the electrode, enabling reproducible measurements. The pseudo steady-state characteristics are also realized at the chip-type electrode. The sensor was successfully applied for the detection of d- and l-lactates in horse serum.

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“…In most cases, a bioanode utilizes an oxidase or dehydrogenase enzyme,, to catalytically oxidize monosaccharides, and a biocathode utilizes a multicopper oxidase enzyme to reduce molecular oxygen into water. Compared to conventional fuel cells, one of the most outstanding advantages of EFCs is wide variety of available fuels, by designing the bioelectrodes with consideration of proper and optimum enzymatic reactions. However, an enzyme immobilized in bioanode can oxidize only its specific fuel material due to its high specific selectivity, resulting in limitation of fuel choice of the EFC.…”

Section: Introductionmentioning

confidence: 85%

Multi‐Enzyme Immobilized Anodes Utilizing Maltose Fuel for Biofuel Cell Applications

et al. 2018

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Multi‐enzyme immobilized carbon‐felt electrodes are fabricated for application as a bioanode in biofuel cells to utilize both maltose and glucose as the fuel. The unique combination of three enzymes (maltase, mutarotase, and glucose oxidase) enables us to utilize maltose as the fuel for the bioanode. The new electrode based on carbon felt (CF) demonstrates a high oxidation current density of 6.5 mA cm−2 at 0.34 V vs. Ag/AgCl in a neutral phosphate buffer solution containing 0.025 mol dm−3 (≡M) maltose in a half‐cell configuration. Furthermore, we improve the bioanode performance by changing the surfactant from cetyltrimethylammonium bromide (CTAB) to Triton X‐100® (TX), which is used as a carbon nanotube (CNT) dispersant in the bioanode preparation process. A superior current density of 17 mA cm−2 at 0.34 V vs. Ag/AgCl is demonstrated with the multi‐enzyme bioanode by using TX as the CNT dispersant, owing to the good dispersion of CNTs attached to CF and the reduced deactivation and leakage of the enzymes. A maltose/O2 biofuel cell, composed of the multi‐enzyme immobilized bioanode and a biocathode based on bilirubin oxidase and mediator, delivers a maximum power density of 2.3 mW cm−2 and an open‐circuit voltage of 0.69 V in 0.2 M phosphate buffer solution containing 50 mM maltose.

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High-Power Formate/Dioxygen Biofuel Cell Based on Mediated Electron Transfer Type Bioelectrocatalysis

Cited by 54 publications

References 60 publications

Molybdenum-Dependent Formate Dehydrogenase for Formate Bioelectrocatalysis in a Formate/O₂Enzymatic Fuel Cell

Molybdenum-Dependent Formate Dehydrogenase for Formate Bioelectrocatalysis in a Formate/O₂Enzymatic Fuel Cell

Simultaneous Detection of Lactate Enantiomers Based on Diffusion-controlled Bioelectrocatalysis

Multi‐Enzyme Immobilized Anodes Utilizing Maltose Fuel for Biofuel Cell Applications

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High-Power Formate/Dioxygen Biofuel Cell Based on Mediated Electron Transfer Type Bioelectrocatalysis

Cited by 54 publications

References 60 publications

Molybdenum-Dependent Formate Dehydrogenase for Formate Bioelectrocatalysis in a Formate/O2Enzymatic Fuel Cell

Molybdenum-Dependent Formate Dehydrogenase for Formate Bioelectrocatalysis in a Formate/O2Enzymatic Fuel Cell

Simultaneous Detection of Lactate Enantiomers Based on Diffusion-controlled Bioelectrocatalysis

Multi‐Enzyme Immobilized Anodes Utilizing Maltose Fuel for Biofuel Cell Applications

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Molybdenum-Dependent Formate Dehydrogenase for Formate Bioelectrocatalysis in a Formate/O₂Enzymatic Fuel Cell

Molybdenum-Dependent Formate Dehydrogenase for Formate Bioelectrocatalysis in a Formate/O₂Enzymatic Fuel Cell