title: Biomaterial engineered electrodes for bioelectronics.
abstract: A 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, ket1 = 20 s-1, long time intervals lead to a slow interfacial electron transfer to the Fe(III)-Cyt c, ket2 = 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 O2 to water. Kinetic analysis reveals that the rate-limiting step in the bioelectrocatalytic reduction of O2 by the integrated Cyt c/COx electrode is the primary electron transfer from the electrode support to the Cyt c units.
authors.affiliation: Institute of Chemistry, Hebrew University of Jerusalem, Givat Ram, Jerusalem 91904, Israel.
authors.forename: V
authors.initials: V
authors.lastname: Pardo-Yissar
authors.forename: E
authors.initials: E
authors.lastname: Katz
authors.forename: I
authors.initials: I
authors.lastname: Willner
authors.forename: A B
authors.initials: AB
authors.lastname: Kotlyar
authors.forename: C
authors.initials: C
authors.lastname: Sanders
authors.forename: H
authors.initials: H
authors.lastname: Lill
mesh_terms: D001672:Biocompatible Materials / Q000737:chemistry*; D015374:Biosensing Techniques; D003574:Cytochrome c Group / Q000737:chemistry*; D004563:Electrochemistry; D004566:Electrodes; D004581:Electronics; D004800:Enzymes, Immobilized
chemical_list: D001672:Biocompatible Materials; D003574:Cytochrome c Group; D004800:Enzymes, Immobilized