A Direct Electron Transfer‐Based Glucose/Oxygen Biofuel Cell Operating in Human Serum

Coman, Virginia; Ludwig, Roland; Harreither, Wolfgang; Haltrich, Dietmar; Gorton, Lo; Ruzgas, Tautgirdas; Shleev, Sergey

doi:10.1002/fuce.200900121

Cited by 131 publications

(127 citation statements)

References 37 publications

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“…For the purposes of this review and in the light of the wildtype CDH being comprised of the FAD dehydrogenase domain alongside the haem domain, we consider CDH to undergo direct bioelectrocatalysis. For the last 20 years or so, researchers have investigated the nature of DET between CDH and electrode surfaces, which has been concluded to be largely afforded via the haem domain (figure 8a) [73][74][75][76][77].…”

Section: Direct Bioelectrocatalysis Of Metalloenzymesmentioning

confidence: 99%

Direct enzymatic bioelectrocatalysis: differentiating between myth and reality

Milton

Minteer

2017

J. R. Soc. Interface.

158

148

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Enzymatic bioelectrocatalysis is being increasingly exploited to better understand oxidoreductase enzymes, to develop minimalistic yet specific biosensor platforms, and to develop alternative energy conversion devices and bioelectrosynthetic devices for the production of energy and/or important chemical commodities. In some cases, these enzymes are able to electronically communicate with an appropriately designed electrode surface without the requirement of an electron mediator to shuttle electrons between the enzyme and electrode. This phenomenon has been termed direct electron transfer or direct bioelectrocatalysis. While many thorough studies have extensively investigated this fascinating feat, it is sometimes difficult to differentiate desirable enzymatic bioelectrocatalysis from electrocatalysis deriving from inactivated enzyme that may have also released its catalytic cofactor. This article will review direct bioelectrocatalysis of several oxidoreductases, with an emphasis on experiments that provide support for direct bioelectrocatalysis versus denatured enzyme or dissociated cofactor. Finally, this review will conclude with a series of proposed control experiments that could be adopted to discern successful direct electronic communication of an enzyme from its denatured counterpart.

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Section: Direct Bioelectrocatalysis Of Metalloenzymesmentioning

confidence: 99%

Direct enzymatic bioelectrocatalysis: differentiating between myth and reality

Milton

Minteer

2017

J. R. Soc. Interface.

158

148

View full text Add to dashboard Cite

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“…In the present context of biofuel cell development intensive efforts are gathered [1,2] towards fulfilling of key limiting parameters [3], not only in terms of current densities and extended cell potential, but also regarding the adaptation to physiological conditions [4]. From an implantable biocathode point of view that catalyzes the oxygen reduction to water, the maximum output that can be feasibly obtained is limited by both the oxygen concentration and the potential provided by the biocathode.…”

Section: Introductionmentioning

confidence: 99%

Enhanced direct electron transfer between laccase and hierarchical carbon microfibers/carbon nanotubes composite electrodes. Comparison of three enzyme immobilization methods

Gutiérrez-Sánchez

Jia

Beyl

et al. 2012

Electrochimica Acta

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“…Corynascus thermophilus cellobiose dehydrogenase (CtCDH) was purified to homogeneity [18] and had a volumetric activity of 276 U/ml (2,6-dichloroindophenol assay at pH 7.5) [33].…”

Section: Methodsmentioning

confidence: 99%

“…The majority of enzymatic fuel cells utilise O 2 and glucose as oxidant and fuel, respectively, both of which are available in body fluids. The most frequently used enzymes in biofuel cells are blue multi-copper oxidases (bilirubin oxidase [15] and laccase [16]) at the cathode and glucose oxidase [15], glucose dehydrogenase [17] or cellobiose dehydrogenase [18] at the anode. GOx is a dimeric glycosylated protein composed of two identical monomers.…”

Section: Introductionmentioning

confidence: 99%

Mediated electron transfer of cellobiose dehydrogenase and glucose oxidase at osmium polymer-modified nanoporous gold electrodes

et al. 2012

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Abstract:Nanoporous and planar gold electrodes were utilised as supports for the redox enzymes Aspergillus niger glucose oxidase (GOx) and Corynascus thermophilus cellobiose dehydrogenase (CtCDH). Electrodes modified with hydrogels containing enzyme, Os-redox polymers and the cross-linking agent poly(ethylene glycol)diglycidyl ether (PEGDGE) were used as biosensors for the determination of glucose and lactose. Limits of detection of 6.0 (± 0.4), 16.0 (± 0.1) and 2.0 (± 0.1) µM were obtained for CtCDH modified lactose and glucose biosensors and GOx modified glucose biosensors, respectively, at nanoporous gold electrodes. Biofuel cells comprised of GOx and CtCDH modified gold electrodes were utilised as anodes, together with Myrothecium verrucaria bilirubin oxidase (MvBOD) or Melanocarpus albomyces laccase (rMaLc) as cathodes, in biofuel cells. A maximum power density of 41 µW/cm 2 was obtained for a CtCDH/MvBOD biofuel cell in 5 mM lactose and O 2 saturated buffer (pH 7.4, 0.1 M phosphate, 150 mM NaCl).2

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A Direct Electron Transfer‐Based Glucose/Oxygen Biofuel Cell Operating in Human Serum

Cited by 131 publications

References 37 publications

Direct enzymatic bioelectrocatalysis: differentiating between myth and reality

Direct enzymatic bioelectrocatalysis: differentiating between myth and reality

Enhanced direct electron transfer between laccase and hierarchical carbon microfibers/carbon nanotubes composite electrodes. Comparison of three enzyme immobilization methods

Mediated electron transfer of cellobiose dehydrogenase and glucose oxidase at osmium polymer-modified nanoporous gold electrodes

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