Mechanism of Bilirubin Oxidase : Fabrication and Characterization of Efficient Biocathode

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Mechanism of Bilirubin Oxidase : Fabrication and Characterization of Efficient Biocathode

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dc.contributor.author Falk, Magnus en_US
dc.contributor.author Andoralov, Viktor en_US
dc.contributor.author Reimann, Curt en_US
dc.contributor.author Ruzgas, Tautgirdas en_US
dc.contributor.author Srnec, Martin en_US
dc.contributor.author Ryde, Ulf en_US
dc.contributor.author Rulíšek, Lubomír en_US
dc.contributor.author Shleev, Sergey en_US
dc.contributor.editor Chaitanya, Desai
dc.contributor.editor Subramanian, V.
dc.date.accessioned 2010-12-21T19:21:01Z
dc.date.available 2010-12-21T19:21:01Z
dc.date.issued 2010
dc.identifier.issn 1091-8213
dc.identifier.issn 2151-2043
dc.identifier.uri http://hdl.handle.net/2043/11241
dc.description.abstract To elucidate the mechanism of bilirubin oxidase (BOx) function in order to design efficient and stable biocathodes working at different conditions, the enzyme was studied thoroughly. BOx is a copper-containing redox enzyme that catalyzes the oxidation of a variety of different organic and inorganic compounds with concomitant reduction of O2 directly to H2O. en
dc.format.extent 1
dc.language.iso eng en
dc.publisher ECS en
dc.subject bilirubin oxidase en
dc.subject biocathode en
dc.subject.classification Sciences en
dc.title Mechanism of Bilirubin Oxidase : Fabrication and Characterization of Efficient Biocathode en_US
dc.type Conference Abstract en_US
dc.relation.url http://www.ecsdl.org/browse/ecs/symp.jsp?Coden=MAECES&Volume=1002 en
dc.contributor.department Malmö University. Faculty of Health and Society en
dc.subject.srsc Research Subject Categories::NATURAL SCIENCES::Chemistry::Biochemistry en
dc.subject.srsc Research Subject Categories::TECHNOLOGY::Bioengineering::Enzyme engineering en
dc.relation.ispartofpublication Meeting abstracts en
dcterms.description.conferenceName ECS Meeting
dcterms.description.conferencePlace Las Vegas, NV
dcterms.description.conferenceYear 2010
dc.format.artNo 60
mahlocal.rights.oaType green
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