Biomaterial engineered electrodes for bioelectronics

DC FieldValueLanguage
dc.contributor.authorPardo-Yissar, V
dc.contributor.authorKatz, E
dc.contributor.authorWillner, I
dc.contributor.authorKotlyar, AB
dc.contributor.authorSanders, C
dc.contributor.authorLill, H
dc.date.accessioned2021-12-23T16:16:22Z-
dc.date.available2021-12-23T16:16:22Z-
dc.date.issued2000
dc.identifier.issn13596640
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/11835-
dc.description.abstractA series of single-cysteine-containing cytochrome c, Cyt c, heme proteins including the wild-type Cyt c (from Saccharomyces cerevisiae) and the mutants (V33C, Q21C, R18C, G1C, K9C and K4C) exhibit direct electrical contact with Au-electrodes upon covalent attachment to a maleimide monolayer associated with the electrode. With the G1C-Cyt c mutant, which includes the cysteine residue in the polypeptide chain at position 1, the potential-induced switchable control of the interfacial electron transfer was observed. This heme protein includes a positively charged protein periphery that surrounds the attachment site and faces the electrode surface. Biasing of the electrode at a negative potential (-0.3 V vs. SCE) attracts the reduced Fe(ii)-Cyt c heme protein to the electrode surface. Upon the application of a double-potential-step chronoamperometric signal onto the electrode, where the electrode potential is switched to 0.3 V and back to -0.3 V, the kinetics of the transient cathodic current, corresponding to the re-reduction of the Fe(iii)-Cyt c, is controlled by the time interval between the oxidative and reductive potential steps. While a short time interval results in a rapid interfacial electron-transfer, k(et)(1)=20 s(-1), long time intervals lead to a slow interfacial electron transfer to the Fe(iii)-Cyt c, k(et)(2)=1.5 s(-1). The fast interfacial electron-transfer rate-constant is attributed to the reduction of the surface-attracted Fe(iii)-Cyt c. The slow interfacial electron-transfer rate constant is attributed to the electrostatic repulsion of the positively charged Cyt c from the electrode surface, resulting in long-range electron transfer exhibiting a lower rate constant. At intermediate time intervals between the oxidative and reductive steps, two populations of Cyt c, consisting of surface-attracted and surface-repelled heme proteins, are observed. Crosslinking of a layered affinity complex between the Cyt c and cytochrome oxidase, COx, on an Au-electrode yields an electrically-contacted, integrated, electrode for the four-electron reduction of O-2 to water. Kinetic analysis reveals that the rate-limiting step in the bioelectrocatalytic reduction of O-2 by the integrated Cyt c/COx electrode is the primary electron transfer from the electrode support to the Cyt c units.
dc.language.isoen
dc.publisherROYAL SOC CHEMISTRY
dc.relation.ispartofFARADAY DISCUSSIONS
dc.subject4-ELECTRON REDUCTION
dc.subjectAU-ELECTRODES
dc.subjectChemistry
dc.subjectChemistry, Physical
dc.subjectCYTOCHROME-C
dc.subjectDIOXYGEN
dc.subjectELECTROCHEMICAL REDUCTION
dc.subjectENZYME ELECTRODES
dc.subjectGLUCOSE-OXIDASE
dc.subjectGOLD ELECTRODE
dc.subjectKINETIC SEPARATION
dc.subjectMONOLAYERS
dc.titleBiomaterial engineered electrodes for bioelectronics
dc.typejournal article
dc.identifier.doi10.1039/b001508n
dc.identifier.isiISI:000165249000010
dc.description.volume116
dc.description.startpage119
dc.description.endpage134
dc.contributor.orcid0000-0001-9336-5428
dc.contributor.orcid0000-0003-0713-6499
dc.contributor.researcheridH-7314-2016
dc.identifier.eissn13645498
dc.publisher.placeTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND
dcterms.isPartOf.abbreviationFaraday Discuss.
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