Direct electron transfer-type dual gas diffusion H2/O2biofuel cells

2016 ◽  
Vol 4 (22) ◽  
pp. 8742-8749 ◽  
Author(s):  
Keisei So ◽  
Yuki Kitazumi ◽  
Osamu Shirai ◽  
Koji Nishikawa ◽  
Yoshiki Higuchi ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Direct Electron Transfer ◽  
Environmentally Friendly ◽  
Gas Diffusion ◽  
Biofuel Cells ◽  
Multicopper Oxidases ◽  
Power Devices

H2/O2biofuel cells utilizing hydrogenases and multicopper oxidases as bioelectrocatalysts are clean, sustainable, and environmentally friendly power devices.

scholarly journals Nanocatalysts Containing Direct Electron Transfer-Capable Oxidoreductases: Recent Advances and Applications

Catalysts ◽  
2019 ◽  
Vol 10 (1) ◽  
pp. 9 ◽  
Author(s):  
Dalius Ratautas ◽  
Marius Dagys
Keyword(s):  
Electron Transfer ◽  
State Of The Art ◽  
Direct Electron Transfer ◽  
Biofuel Cells ◽  
Solid Surfaces ◽  
Electron Mediator ◽  
Research Directions ◽  
Catalytic Systems ◽  
Nanoparticle Catalysts ◽  
Nanoparticle Surface

Direct electron transfer (DET)-capable oxidoreductases are enzymes that have the ability to transfer/receive electrons directly to/from solid surfaces or nanomaterials, bypassing the need for an additional electron mediator. More than 100 enzymes are known to be capable of working in DET conditions; however, to this day, DET-capable enzymes have been mainly used in designing biofuel cells and biosensors. The rapid advance in (semi) conductive nanomaterial development provided new possibilities to create enzyme-nanoparticle catalysts utilizing properties of DET-capable enzymes and demonstrating catalytic processes never observed before. Briefly, such nanocatalysts combine several cathodic and anodic catalysis performing oxidoreductases into a single nanoparticle surface. Hereby, to the best of our knowledge, we present the first review concerning such nanocatalytic systems involving DET-capable oxidoreductases. We outlook the contemporary applications of DET-capable enzymes, present a principle of operation of nanocatalysts based on DET-capable oxidoreductases, provide a review of state-of-the-art (nano) catalytic systems that have been demonstrated using DET-capable oxidoreductases, and highlight common strategies and challenges that are usually associated with those type catalytic systems. Finally, we end this paper with the concluding discussion, where we present future perspectives and possible research directions.

Direct electron transfer-based bioanodes for ethanol biofuel cells using PQQ-dependent alcohol and aldehyde dehydrogenases

2013 ◽  
Vol 87 ◽  
pp. 323-329 ◽  
Author(s):  
Sidney Aquino Neto ◽  
Emily L. Suda ◽  
Shuai Xu ◽  
Matthew T. Meredith ◽  
Adalgisa R. De Andrade ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Direct Electron Transfer ◽  
Biofuel Cells ◽  
Aldehyde Dehydrogenases

Gold-Coated M13 Bacteriophage as a Template for Glucose Oxidase Biofuel Cells with Direct Electron Transfer

ACS Nano ◽  
2015 ◽  
Vol 10 (1) ◽  
pp. 324-332 ◽  
Author(s):  
Rita A. Blaik ◽  
Esther Lan ◽  
Yu Huang ◽  
Bruce Dunn
Keyword(s):  
Electron Transfer ◽  
Glucose Oxidase ◽  
Direct Electron Transfer ◽  
Biofuel Cells ◽  
M13 Bacteriophage

Direct Electron Transfer at Cellobiose Dehydrogenase Modified Anodes for Biofuel Cells

2008 ◽  
Vol 112 (26) ◽  
pp. 9956-9961 ◽  
Author(s):  
Federico Tasca ◽  
Lo Gorton ◽  
Wolfgang Harreither ◽  
Dietmar Haltrich ◽  
Roland Ludwig ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Direct Electron Transfer ◽  
Biofuel Cells ◽  
Cellobiose Dehydrogenase

scholarly journals Enhancement of Electrochemical Performance of Bilirubin Oxidase Modified Gas Diffusion Biocathode by Porphyrin Precursor

2018 ◽  
Vol 2018 ◽  
pp. 1-9 ◽  
Author(s):  
Erica Pinchon ◽  
Mary Arugula ◽  
Kapil Pant ◽  
Sameer Singhal
Keyword(s):  
Electron Transfer ◽  
Oxygen Reduction ◽  
Power Density ◽  
Current Density ◽  
Direct Electron Transfer ◽  
Glucose Dehydrogenase ◽  
Phosphate Buffer Solution ◽  
Gas Diffusion ◽  
Biofuel Cell ◽  
Bilirubin Oxidase

Recent studies have focused on tailoring the catalytic currents of multicopper oxidase (MCO) enzymes-based biocathodes to enhance oxygen reduction. Biocathodes modified with natural substrates specific for MCO enzymes demonstrated drastic improvement for oxygen reduction. Performance of 1-pyrenebutanoic acid, succinimidyl ester (PBSE), and 2,5-dimethyl-1-phenyl-1H-pyrrole-3-carbaldehyde (Di-Carb) oriented bilirubin oxidase (BOx) modified gas diffusion biocathode has been highly improved by incorporating hematin, a porphyrin precursor as electron transfer enhancement moiety. Hematin modified electrodes demonstrated direct electron transfer reaction of BOx exhibiting larger O2 reduction in current density in phosphate buffer solution (pH 7.0) without the need of a mediator. A remarkable improvement in the catalytic currents with 2.5-fold increase compared to non-hematin modified oriented BOx electrodes was achieved. Moreover, a mediatorless and compartmentless glucose/O2 biofuel cell based on DET-type bioelectrocatalysis via the BOx cathode and the glucose dehydrogenase (GDH) anode demonstrated peak power densities of 1 mW/cm2 at pH 7.0 with 100 mM glucose/10 mM NAD fuel. The maximum current density of 1.6 mA/cm2 and the maximum power density of 0.4 mW/cm2 were achieved at 300 mV with nonmodified BOx cathode, while 3.5 mA/cm2 and 1.1 mW/cm2 of current and power density were achieved with hematin modified cathode. The performance improved 2.4 times which attributes to the hematin acting as a natural precursor and activator for BOx activity enhancement.

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