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Small electron transfer proteins as mediators in enzymatic electrochemical biosensors

dc.contributor.authorSilveira, Célia M.
dc.contributor.authorAlmeida, M. Gabriela
dc.date.accessioned2014-04-24T08:53:36Z
dc.date.available2014-04-24T08:53:36Z
dc.date.issued2013-04
dc.descriptionThe final publication is available at Springer.
dc.description.abstract"Electrochemical mediators transfer redox equivalents between the active sites of enzymes and electrodes and, in this way, trigger bioelectrocatalytic redox processes. This has been very useful in the development of the so-called second generation biosensors, where they are able to transduce the catalytic event into an electrical signal. Among other pre-requisites, redox mediators must be readily oxidized/reduced at the electrode surface and easily interact with the biorecognition component. Small chemical compounds (e.g. ferrocene derivatives, ruthenium or osmium complexes and viologens) are frequently used for this purpose, but lately, small redox proteins (e.g. horse heart cytochrome c) have also played the role of redox partners in biosensing applications. In general, the docking between two complementary proteins introduces a second level of selectivity to the biosensor and enlarges the list of compounds targeted for analysis. Moreover, electrochemical interferences are frequently minimized owing to the small overpotentials achieved. This paper aims to provide an overview of enzyme biosensors that are mediated by electron transfer proteins. The article begins with a few considerations on mediated electrochemistry in biosensing 2 systems and proceeds with a detailed description of relevant works concerning the cooperative use of redox enzymes and biological electron donors/acceptors."por
dc.identifier.citationOriginal source: Analytical and Bioanalytical Chemistry. April 2013, Volume 405, Issue 11, pp 3619-3635por
dc.identifier.issn1618-2642
dc.identifier.issn1618-2650
dc.identifier.urihttp://hdl.handle.net/10400.26/6257
dc.language.isoengpor
dc.peerreviewedyespor
dc.publisherSpringerpor
dc.relationSTRUCTURAL AND MECHANISTIC FEATURES OF CYTOCHROME CD1 NITRITE REDUCTASE
dc.relation.publisherversionhttp://dx.doi.org/10.1007/s00216-013-6786-4por
dc.subjectElectrochemical biosensorspor
dc.subjectRedox partnerpor
dc.subjectElectron transfer proteinpor
dc.subjectMediated electrochemistrypor
dc.titleSmall electron transfer proteins as mediators in enzymatic electrochemical biosensorspor
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleSTRUCTURAL AND MECHANISTIC FEATURES OF CYTOCHROME CD1 NITRITE REDUCTASE
oaire.awardURIinfo:eu-repo/grantAgreement/FCT//SFRH%2FBPD%2F79566%2F2011/PT
oaire.citation.endPage3635por
oaire.citation.startPage3619por
oaire.citation.titleAnalytical and Bioanalytical Chemistrypor
oaire.citation.volume405 (11)por
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccess
rcaap.typearticlepor
relation.isProjectOfPublicationbd7e1740-39f4-4605-b0a6-5eaed8b50229
relation.isProjectOfPublication.latestForDiscoverybd7e1740-39f4-4605-b0a6-5eaed8b50229

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