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Enzyme-Based (Bio)Fuel Cells—Bilirubin Oxidase Use
Malmö University, Biofilms Research Center for Biointerfaces. Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Sensor Realisation Center (SRC), Malmö, Sweden.ORCID iD: 0000-0003-0304-7528
2018 (English)In: Encyclopedia of Interfacial Chemistry: Surface Science and Electrochemistry / [ed] Klaus Wandelt, Oxford: Elsevier , 2018, p. 209-216Chapter in book (Other academic)
Abstract [en]

Discovered in 1981, bilirubin oxidase (BOD) became an important cathode enzyme in design of biofuel cells (BFCs). Substantial catalytic activity at neutral pH, minor inhibition by chloride ions and high-redox potential of the T1 copper site, being close to the redox potential of oxygen reduction to water, are the advantageous characteristics that distinguish this enzyme from other multicopper oxidases, for example, laccases, used in design of BFC cathodes. This article discusses the basic concept of BFCs and summarizes the achievements and limits which are reached by BFCs with focus on cathodes modified by BOD. Enzymatic cycle in homogeneous media and direct and mediated heterogeneous electron transfer of BOD are briefly summarized.

Place, publisher, year, edition, pages
Oxford: Elsevier , 2018. p. 209-216
Keywords [en]
Bilirubin oxidase, Bioelectrocatalysis, Biofuel cell, Cathode, Direct electron transfer, Enzymatic fuel cell, Enzyme modified electrode, Mediated electron transfer, Multicopper oxidase, Oxygen reduction reaction
National Category
Analytical Chemistry
Identifiers
URN: urn:nbn:se:mau:diva-44440DOI: 10.1016/B978-0-12-409547-2.13587-5Scopus ID: 2-s2.0-85054660057ISBN: 978-0-12-809894-3 (electronic)OAI: oai:DiVA.org:mau-44440DiVA, id: diva2:1575912
Available from: 2021-06-30 Created: 2021-06-30 Last updated: 2024-06-17Bibliographically approved

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Ruzgas, Tautgirdas

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Biofilms Research Center for BiointerfacesDepartment of Biomedical Science (BMV)
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