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dc.contributor.authorCiampi, Simone
dc.contributor.authorGooding, J.
dc.identifier.citationCiampi, S. and Gooding, J. 2010. Direct electrochemistry of cytochrome c at modified Si(100) electrodes. Chemistry - A European Journal. 16 (20): pp. 5961-5968.

This paper demonstrates the direct electron transfer between the heme moiety of horse hearth cytochrome c and a pyridinyl group on self-assembled-monolayer-modified Si(100) electrodes. Self-assembled monolayers (SAMs) containing the putative receptor ligand were prepared by a step-wise procedure using "click" reactions of acetylene-terminated alkyl monolayers and isonicotinic acid azide derivatives. Unoxidized Si(100) electrodes, possessing either isonicotinate or isonicotinamide receptor ligands, were characterized using X-ray photoelectron spectroscopy, contact-angle goniometry, cyclic voltammetry, and electrochemical impedance spectroscopy. The ability of isonicotinic acid terminated layers to coordinatively bind the redox center of cytochrome c was found to be restricted to pyridinyl assemblies with a paraester linkage present. The protocol detailed here offers an experimentally simple modular approach to producing chemically well-defined SAMs on silicon surfaces for direct electrochemistry of a well-studied model redox protein. © 2010 Wiley-VCH Verlag GmbH & Co. KGaA.

dc.publisherWiley - V C H Verlag GmbH & Co. KGaA
dc.titleDirect electrochemistry of cytochrome c at modified Si(100) electrodes
dc.typeJournal Article
dcterms.source.titleChemistry - A European Journal
curtin.departmentNanochemistry Research Institute
curtin.accessStatusFulltext not available

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