Complete Oxidation of Methanol in Biobattery Devices Using a Hydrogel Created from Three Modified Dehydrogenases

Kim, Yang‐Hee; Campbell, Elliot; Yu, Jiang; Minteer, Shelley D.; Banta, Scott

doi:10.1002/anie.201207423

Cited by 87 publications

(73 citation statements)

References 30 publications

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“…Kim et al combined alcohol dehydrogenase from Bacillus stearothermophilus, human aldehyde dehydrogenase and the NAD-dependent FDH from Saccharomyces cerevisiae to produce a synthetic metabolic pathway capable of complete oxidation of methanol. 7 All of these enzymes were applied on stainless steel mesh current collectors after having been mixed with mediators (NAD + , methylene blue, Na 2 SO 4 ), carbon fibers and carbon black and were then subsequently used as the bioanode. Further, this study made use of a Prussian blue non-biological cathode, which was separated from the anode using a Nafion proton exchange membrane.…”

Section: -29mentioning

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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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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Section: -29mentioning

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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“…In addition, the power curve was recorded at high scan rate (50 mV/s) due to the fast consumption of fuel. 12 As shown in Figure 3, the enzymatic biobattery generates maximum power density of 1.5 ± 0.3 mA/cm 2 and maximum current density of 302 ± 21 µW/cm 2 . In a control battery without enzyme present, the values of 0.48 ± 0.12 mA/cm 2 and 46 ± 8 µW/cm 2 were observed.…”

Section: Page 1 Of 4 Chemcommmentioning

confidence: 95%

Investigating DNA hydrogels as a new biomaterial for enzyme immobilization in biobatteries

Nguyen

2015

Chem. Commun.

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“…For examples, this approach was successfully used to construct BFCs with an anode consisting of multi-enzyme cascades for complete oxidation of methanol, ethanol, glycerol, lactate, pyruvate and carbohydrates. [3][4][5][6][7] There is a growing interest in improving the bioelectrocatalysis of enzyme cascades, as it might help to increase the energy density of BFCs and potentially create more effective BFC devices.An important factor that affects the biocatalytic activity of an enzyme cascade is the diffusion efficiency of intermediate substrates from one enzyme to another. In nature, enzyme cascades utilized in various metabolic pathways are highly organized to form interenzyme complexes termed "metabolons" that can facilitate substrate channelling, which in turn increases the pathway efficiency.…”

mentioning

confidence: 99%

Improved Bioelectrocatalytic Oxidation of Sucrose in a Biofuel Cell with an Enzyme Cascade Assembled on a DNA Scaffold

Nguyen

Giroud

2014

J. Electrochem. Soc.

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The employment of multi-enzyme cascades as catalysts is a promising strategy to improve performance of enzymatic biofuel cells, as it allows for the conversion of more chemical energy stored in complex fuels. However, the performance of these enzyme systems is often limited by the mass transport of intermediate substrates between enzymes. Nature addresses this issue by organizing metabolic enzymes in a sequential and proximal manner to enhance the efficiency of metabolic pathways. In this work, we investigate the utilization of DNA as a structural scaffold for assembly of the invertase/glucose oxidase enzyme cascade to improve sucrose bioelectrocatalytic activity. It has been found that the DNA-assembled enzyme cascade has higher activity than the free cascade, both in solution and in the immobilized state on an electrode surface. The organization of the enzyme cascade on the DNA scaffold leads to a 100% increase in the current density in amperometric measurements and a 75% increase in the power density of the biofuel cell. This is the first evidence of the advantages of utilizing DNA scaffords for improved bioelectrocatalysis. The search for renewable energy sources has been an important focus in recent years. Among various solutions, enzymatic biofuel cells (BFCs) offer a cheap and environmentally friendly approach for energy conversion from renewable fuels.1,2 The operation of these devices is based on the biocatalysis of oxidoreductase enzymes incorporated on one or both electrodes. Although enzyme-based biofuel cells have shown great promise for energy conversion, they are limited by the low energy density due to the incomplete oxidation of fuels.1 Addressing this issue, enzyme cascades have been employed for deep or complete oxidation of fuels. For examples, this approach was successfully used to construct BFCs with an anode consisting of multi-enzyme cascades for complete oxidation of methanol, ethanol, glycerol, lactate, pyruvate and carbohydrates. [3][4][5][6][7] There is a growing interest in improving the bioelectrocatalysis of enzyme cascades, as it might help to increase the energy density of BFCs and potentially create more effective BFC devices.An important factor that affects the biocatalytic activity of an enzyme cascade is the diffusion efficiency of intermediate substrates from one enzyme to another. In nature, enzyme cascades utilized in various metabolic pathways are highly organized to form interenzyme complexes termed "metabolons" that can facilitate substrate channelling, which in turn increases the pathway efficiency.8 Inspired by this phenomenon, the Minteer research group used small crosslinkers such as dimethyl suberimidate, glutaraldehyde or bis-maleimides for synthesizing enzyme conjugates. 5,9 The utilization of these conjugates instead of free enzymes in the anode led to the improvement of BFC performance and biosensor sensitivity. However, the usage of small crosslinkers suffers from several drawbacks such as low conjugation yield, homo-crosslinking issues, and especially, no con...

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Complete Oxidation of Methanol in Biobattery Devices Using a Hydrogel Created from Three Modified Dehydrogenases

Cited by 87 publications

References 30 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

Investigating DNA hydrogels as a new biomaterial for enzyme immobilization in biobatteries

Improved Bioelectrocatalytic Oxidation of Sucrose in a Biofuel Cell with an Enzyme Cascade Assembled on a DNA Scaffold

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Complete Oxidation of Methanol in Biobattery Devices Using a Hydrogel Created from Three Modified Dehydrogenases

Cited by 87 publications

References 30 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

Investigating DNA hydrogels as a new biomaterial for enzyme immobilization in biobatteries

Improved Bioelectrocatalytic Oxidation of Sucrose in a Biofuel Cell with an Enzyme Cascade Assembled on a DNA Scaffold

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Product

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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