Rational design of quinones for high power density biofuel cells

Milton, Ross D.; Hickey, David P.; Abdellaoui, Sofiène; Lim, Koun; Wu, Fei; Tan, Bo‐Xuan; Minteer, Shelley D.

doi:10.1039/c5sc01538c

Cited by 183 publications

(173 citation statements)

References 51 publications

Supporting

Mentioning

163

Contrasting

Unclassified

Order By: Relevance

“…Once a series of electron mediators with suitable electronic properties has been selected, they must next be screened for their ability to interact with the enzyme in a similar fashion to a substrate; this has greater importance in cases where the redox cofactor is deeply buried within the protein structure. We recently demonstrated that naphthoquinone derivatives were able to undergo efficient MET with one type of glucose oxidizing enzyme, while another species did not exhibit any activity even though the enzymes possess the same redox cofactor where their potentials are expected to have negligible effect on the required overpotential of MET, reemphasizing the importance of cofactor accessibility by the electron mediator [27].…”

Section: Electron Transfer Mechanisms 21 Mediated Electron Transfermentioning

confidence: 99%

Direct enzymatic bioelectrocatalysis: differentiating between myth and reality

Milton

Minteer

2017

J. R. Soc. Interface.

Self Cite

162

148

View full text Add to dashboard Cite

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.

show abstract

Section: Electron Transfer Mechanisms 21 Mediated Electron Transfermentioning

confidence: 99%

Direct enzymatic bioelectrocatalysis: differentiating between myth and reality

Milton

Minteer

2017

J. R. Soc. Interface.

Self Cite

162

148

View full text Add to dashboard Cite

show abstract

“…6 In EFCs, the fuels undergo bioelectrocatalytic oxidation at the anode operating commonly with flavin adenine dinucleotide-dependent (FAD) oxidases and dehydrogenases as well as nicotinamide adenine dinucleotidedependent (NAD) dehydrogenases. 5,[9][10][11] Metalloenzymes, such as laccases, bilirubin oxidase and peroxidase, are generally used at the cathode of EFCs allowing the bioelectrocatalytic reduction of O 2 or peroxides to H 2 O. [12][13][14][15] In addition to carbohydrates, other types of enzyme substrates have been reported as fuels such as alkanes, carboxylic acids, and other organic molecules.…”

mentioning

confidence: 99%

Cholesterol as a Promising Alternative Energy Source: Bioelectrocatalytic Oxidation Using NAD-Dependent Cholesterol Dehydrogenase in Human Serum

Quah

Abdellaoui

Milton

et al. 2016

J. Electrochem. Soc.

Self Cite

View full text Add to dashboard Cite

Cholesterol is an essential structural component of mammalian cells, although elevated concentrations of cholesterol in the human body are linked to atherosclerotic disease. In this context, monitoring physiological cholesterol concentrations is of great interest in medical fields and the concept of producing electrical energy from cholesterol is interesting. In this work, we report the bioelectrocatalytic oxidation of cholesterol with the use of nicotinamide adenine dinucleotide-(NAD) dependent cholesterol dehydrogenase (ChDH) as an alternative enzyme to the commonly-used cholesterol oxidase (ChOx) in bioelectronic applications. To achieve bioelectrocatalytic cholesterol oxidation, ChDH was combined with diaphorase (DH) in a bilayer fashion, whereby DH acts as an intermediary enzyme to facilitate NADH oxidation at a ferrocene redox polymer. Characterization of the resulting bioanode identifies a linear cholesterol response range from 5 μM to 200 μM, with an associated sensitivity of 60.12 mA cm −2 M −1 . Furthermore, an O 2 -reducing biocathode incorporating bilirubin oxidase (BOx) was combined with the cholesterol bioanode into a complete cholesterol/O 2 membrane-less enzymatic fuel cell (EFC).

show abstract

“…Furthermore, the EET efficiency of this strain could be improved by utilization of the currently known conductive pili (Holmes et al ., 2016) by, for instance, coproduction of conductive and adhesive pili in the same cell or by replacing the Fim pili with novel rationally designed hybrid pili that consist of a long conductive fibre and a terminal carbohydrate‐binding adhesin. Alternatively, the EET of E. coli cymA ‐ mtr ‐ fim could be promoted through penetration of the pili layer with electrode‐tethered conductive polymers such as linear naphtoquinone‐modified polyethylenimine hydrogels through which electrons can be transferred by shuttling between the covalently bound redox centres (Milton et al ., 2015). …”

Section: Resultsmentioning

confidence: 99%

Towards patterned bioelectronics: facilitated immobilization of exoelectrogenic Escherichia coli with heterologous pili

Lienemann

TerAvest

Pitkänen

et al. 2018

Microbial Biotechnology

View full text Add to dashboard Cite

SummaryBiosensors detect signals using biological sensing components such as redox enzymes and biological cells. Although cellular versatility can be beneficial for different applications, limited stability and efficiency in signal transduction at electrode surfaces represent a challenge. Recent studies have shown that the Mtr electron conduit from Shewanella oneidensis MR‐1 can be produced in Escherichia coli to generate an exoelectrogenic model system with well‐characterized genetic tools. However, means to specifically immobilize this organism at solid substrates as electroactive biofilms have not been tested previously. Here, we show that mannose‐binding Fim pili can be produced in exoelectrogenic E. coli and can be used to selectively attach cells to a mannose‐coated material. Importantly, cells expressing fim genes retained current production by the heterologous Mtr electron conduit. Our results demonstrate the versatility of the exoelectrogenic E. coli system and motivate future work that aims to produce patterned biofilms for bioelectronic devices that can respond to various biochemical signals.

show abstract

Rational design of quinones for high power density biofuel cells

Abstract: Rationally designing quinones to label GDH and create a redox hydrogel that delivers high OCP, current and power densities.

Cited by 183 publications

References 51 publications

Direct enzymatic bioelectrocatalysis: differentiating between myth and reality

Direct enzymatic bioelectrocatalysis: differentiating between myth and reality

Cholesterol as a Promising Alternative Energy Source: Bioelectrocatalytic Oxidation Using NAD-Dependent Cholesterol Dehydrogenase in Human Serum

Towards patterned bioelectronics: facilitated immobilization of exoelectrogenic Escherichia coli with heterologous pili

Contact Info

Product

Resources

About