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Oxygen Electroreduction Versus Bioelectroreduction: Direct Electron Transfer Approach
Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).ORCID iD: 0000-0001-6421-2158
Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
Malmö högskola, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
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2016 (English)In: Electroanalysis, ISSN 1040-0397, E-ISSN 1521-4109, Vol. 28, no 10, p. 2270-2287Article, review/survey (Refereed)
Abstract [en]

A review. Being inspired by a very recent review entitled: "Electrocatalysis and bioelectrocatalysis - Distinction without a difference" and following the general approach employed by Prof. Dr. Schuhmann, in the current work we point to the similarities and differences between oxygen electroredn. and bioelectroredn. processes. To addnl. distinguish our paper from the recent review we touch on different bioelements, such as redox proteins and living cells, but we still keep a special emphasis on oxidoreductases, biocatalysts par excellence. Moreover, we also exclusively focus on oxygen electroredn. based on direct electron transfer reactions. On the one hand, we corroborate the previously made conclusion regarding intrinsically high activity of the active sites of biol. catalysts, esp. redox enzymes, which results in mass transfer and heterogeneous electron transfer limited currents from oxygen reducing bioelectrodes. On the other hand, we disagree with the statements regarding the exceptionality of precious metal catalysts, and the notion of a huge trade-​off between high activity and stability of non-​precious metal catalysts and bioelements. We show that the activity and stability of noble metal based cathodes is very far from perfect, esp. when these electrodes operate in complex electrolytes, such as physiol. fluids, e.g. human blood.

Place, publisher, year, edition, pages
John Wiley & Sons, 2016. Vol. 28, no 10, p. 2270-2287
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:mau:diva-16179DOI: 10.1002/elan.201600280ISI: 000387886500003Scopus ID: 2-s2.0-84981333058Local ID: 21937OAI: oai:DiVA.org:mau-16179DiVA, id: diva2:1419695
Available from: 2020-03-30 Created: 2020-03-30 Last updated: 2024-02-05Bibliographically approved
In thesis
1. Blue copper proteins as bioelements for bioelectronic devices
Open this publication in new window or tab >>Blue copper proteins as bioelements for bioelectronic devices
2019 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

This thesis is focused on bioelements for biological electric power sources,specifically, on blue copper proteins with and without an intrinsic biocatalyticactivity, i.e. ability to reduce oxygen directly to water. These proteins, viz. differentlaccases, ceruloplasmin, and rusticyanin, were characterised in detailand employed for the construction of both self-charging and conventional biosupercapacitors.First, similarities and particularities of oxygen electroreductionvs. bioelectroreduction were reviewed. Moreover, being a promising candidatefor the construction of autotolerant implantable biocathodes, the electrochemistryof human ceruloplasmin was revisited. For the first time, a clearbioelectrocatalytic reduction of oxygen on ceruloplasmin modified electrodeswas shown. Second, computational design combined with directed evolutionresulted in a high redox potential mutated laccase, GreeDo, with increased redoxpotential of the T1 site, increased activity towards high redox potentialmediators, as well as enhanced stability. Third, GreeDo was electrochemicallycharacterised in detail. The mutant exhibited higher open circuit potentialvalues and onset potentials for oxygen bioelectroreduction compared to the parental laccase, OB-1. Moreover, the operational stability of GreeDo modifiedgraphite electrodes was found to be more than 2 h in a decidedly acidicelectrolyte, in agreement with the extended operational and storage stabilitiesof the enzyme in acidic solutions. Fourth, multi-cell single-electrolyte glucose/oxygen biodevices with adjustable open-circuit and operating voltages,which are independent on the difference in equilibrium redox potentials of thetwo redox couples, gluconolactone/glucose and oxygen/water, viz. 1.18 V, butdependent on the number of half-cells in the biodevice construction, were designedand tested. The biodevices were made from tubular graphite electrodeswith electropolymerised poly(3,4-ethylenedioxythiophene) modified withTrametes hirsuta laccase and Neurospora crassa cellobiose dehydrogenase as the cathodic and anodic biocatalysts, respectively. Due to the interplay betweenfaradaic and non-faradaic electrochemical processes, as well as betweenionic and electronic conductivities, the open-circuit voltage of the self-chargedbiodevice is extraordinarily high, reaching 3 V, when seven biosupercapacitorsoperating in a common electrolyte were connected in series. Moreover,glucose/oxygen biodevices could be externally discharged at an operatingvoltage exceeding the maximal limiting open-circuit value of 1.24 V for thecomplete glucose oxidation. Last but not least, a conventional biosupercapacitor,i.e. a biodevice lacking self-charging ability, was composed of Acidithiobacillusferrooxidans rusticyanin modified gold electrodes. The complete biodevicesas well as separate electrodes were thoroughly characterised electrochemically.The symmetrical biosupercapacitor based on two identical goldelectrodes modified with rusticyanin is able to capacitively store electricityand deliver electric power, accumulated mostly in the form of biopseudocapacitance,when charged and discharged externally.

Place, publisher, year, edition, pages
Malmö university, 2019. p. 77
Series
Malmö University Health and Society Dissertations, ISSN 1653-5383 ; 2
Keywords
Blue copper protein, Multicopper oxidase, Direct electron transfer, Oxygen bioelectroreduction, Enzymatic fuel cell, Biosupercapacitor
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:mau:diva-7341 (URN)10.24834/9789178770014 (DOI)28677 (Local ID)9789178770007 (ISBN)9789178770014 (ISBN)28677 (Archive number)28677 (OAI)
Note

Contribution:Paper I. Performed electrochemical investigations of human ceruloplasmin,purified from human blood, on nanostructured graphite electrodes. Took partin literature review, writing of the section 2.3 and preparation of graphicaldata.

Available from: 2020-02-28 Created: 2020-02-28 Last updated: 2022-02-24Bibliographically approved

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Shleev, SergeyPankratov, DmitryFalk, MagnusAleksejeva, OlgaBlum, Zoltan

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