Interconversion between formate and hydrogen carbonate by tungsten-containing formate dehydrogenase-catalyzed mediated bioelectrocatalysis

Sakai, Kyosuke; Hsieh, Bo-Chuan; Maruyama, Akihiro; Kitazumi, Yuki; Shirai, Osamu; Kano, Kenji

doi:10.1016/j.sbsr.2015.07.008

Cited by 34 publications

(39 citation statements)

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“…However, several problems still exist, such as low current densities and low stability. We have electrochemically studied tungsten (W)-containing formate dehydrogenase (FoDH1) from Methylobacterium extorquens AM1 [21]. It has been shown that FoDH1 produces mediated electron transfer (MET)-type bioelectrocatalytic currents for both of the HCOO − oxidation and the CO 2 reduction.…”

Section: Introductionmentioning

confidence: 99%

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Efficient bioelectrocatalytic CO2 reduction on gas-diffusion-type biocathode with tungsten-containing formate dehydrogenase

Sakai

Kitazumi

Shirai

et al. 2016

Electrochemistry Communications

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A new gas-diffusion-type biocathode was constructed for carbon dioxide (CO 2) reduction. In this work, tungsten-containing formate dehydrogenase (FoDH1), which is a promising enzyme for interconversion of formate and CO 2 , was used as a catalyst and was absorbed on a Ketjen Black (KB)-modified electrode. We used 1,1'-trimethylene-2,2'-bipyridinium dibromide as a mediator, and the hydrophobicity of the FoDH1-absorbed electrode was optimized according to the weight ratio of the polytetrafluoroethylene binder to KB. We achieved cathodic current densities of about 20 mA cm −2 under mild and quiescent conditions (neutral pH, atmospheric pressure, and room temperature).

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Section: Introductionmentioning

confidence: 99%

“…We focused on the introduction of a gas-diffusion-type electrode into an FoDH1-based bioelectrocatalytic system. From the viewpoints of the kinetics and the thermodynamics between FoDH1 and mediators [21], we used 1,1'-trimethylene-2,2'-bipyridinium dibromide (TQ; Fig. 1, inset) as a mediator.…”

Section: Introductionmentioning

confidence: 99%

Efficient bioelectrocatalytic CO2 reduction on gas-diffusion-type biocathode with tungsten-containing formate dehydrogenase

Sakai

Kitazumi

Shirai

et al. 2016

Electrochemistry Communications

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“…This FDH is a heterodimer and catalyzes the oxidation of formate to CO 2 in the coupled reduction of NAD + to NADH. 11 It has been shown, however, that Methylobacterium extorquens AM can indirectly produce W-FDH when tungsten is present in the growth medium. 12 The Mo-FDH is a component of the anaerobic formate hydrogen lyase complex of E. coli and is one of the most characterized FDHs.…”

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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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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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“…[8] In nature, evolutionary processes have generated biocatalysts capable of CO 2 reduction to specific molecules with high efficiency under mild, ambientc onditions of pH, temperature, and pressure. [9] While the exact catalytic mechanisms of many such biocatalysts remain unclear,C O 2 reduction by biocatalysts (whole cells or enzymes) have been considered as ap otential technique in future industrial CO 2 utilization. [10] Typically,i n vivo, catalytic reactions occur when coenzymes such as heme, transition metals,n icotinamidea denine dinucleotide (NADH), flavin adenine dinucleotide (FAD), or flavin mononucleotide (FMN) associate with the enzymee ither temporarily or permanently and serve as the reducing equivalent for the reaction.…”

Section: Introductionmentioning

confidence: 99%

“…[10] Kano and colleagues utilized W-FDH from Methylobacterium extorquens AM1 with both DET-a nd MET-based system designs. [9,22] FDH was adsorbed onto am esoporous carbone lectrode to achieve improved FDH orientation and efficient electrochemical communicationb etween the iron sulfur cluster andt he electrode. [21] In another DET design, ag old nanoparticleembedded Ketjenblack-modified glassy carbone lectrode treated with 4-mercaptopyridine facilitated the correcto rientation of W-FDH, improving interfacial electron transfer kinetics.…”

Section: Introductionmentioning

confidence: 99%

Strategies for Bioelectrochemical CO₂ Reduction

Yuan

Kummer

2019

Chemistry A European J

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Atmospheric CO 2 is ac heap and abundants ource of carbonf or synthetic applications. However, the stability of CO 2 makes its conversion to other carbon compounds difficult and has prompted the extensive developmento fC O 2 reduction catalysts. Bioelectrocatalystsa re generally more selective, highly efficient, can operate under mild conditions, and use electricity as the sole reducing agent.I mproving the communication between an electrode and ab ioelectrocatalyst remains as ignificant area of development. Through the examples of CO 2 reduction catalyzed by electroactivee nzymesa nd whole cells, recent advancements in this area are compared and contrasted. Figure 5. (A) MWCNT-coated RVCs used to produce acetate by am ixed bacterial culture. Reproduced with permission from American Chemical Societyfrom Reference [50].(B) Agraphite felt electrode serves as artificial pilifor microbial electrosynthesis. Reproducedw ith permission from Elsevier from Reference [55].

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Interconversion between formate and hydrogen carbonate by tungsten-containing formate dehydrogenase-catalyzed mediated bioelectrocatalysis

Cited by 34 publications

References 43 publications

Efficient bioelectrocatalytic CO2 reduction on gas-diffusion-type biocathode with tungsten-containing formate dehydrogenase

Efficient bioelectrocatalytic CO2 reduction on gas-diffusion-type biocathode with tungsten-containing formate dehydrogenase

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

Strategies for Bioelectrochemical CO₂ Reduction

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Interconversion between formate and hydrogen carbonate by tungsten-containing formate dehydrogenase-catalyzed mediated bioelectrocatalysis

Cited by 34 publications

References 43 publications

Efficient bioelectrocatalytic CO2 reduction on gas-diffusion-type biocathode with tungsten-containing formate dehydrogenase

Efficient bioelectrocatalytic CO2 reduction on gas-diffusion-type biocathode with tungsten-containing formate dehydrogenase

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

Strategies for Bioelectrochemical CO2 Reduction

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

Strategies for Bioelectrochemical CO₂ Reduction