Direct electrochemistry of cytochrome c at modified Si(100) electrodes

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 usi...

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Main Authors: Ciampi, Simone, Gooding, J.
Format: Journal Article
Published: Wiley - V C H Verlag GmbH & Co. KGaA 2010
Online Access:http://hdl.handle.net/20.500.11937/31721
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author Ciampi, Simone
Gooding, J.
author_facet Ciampi, Simone
Gooding, J.
author_sort Ciampi, Simone
building Curtin Institutional Repository
collection Online Access
description 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.
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spelling curtin-20.500.11937-317212017-09-13T15:20:01Z Direct electrochemistry of cytochrome c at modified Si(100) electrodes Ciampi, Simone Gooding, J. 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. 2010 Journal Article http://hdl.handle.net/20.500.11937/31721 10.1002/chem.200903316 Wiley - V C H Verlag GmbH & Co. KGaA restricted
spellingShingle Ciampi, Simone
Gooding, J.
Direct electrochemistry of cytochrome c at modified Si(100) electrodes
title Direct electrochemistry of cytochrome c at modified Si(100) electrodes
title_full Direct electrochemistry of cytochrome c at modified Si(100) electrodes
title_fullStr Direct electrochemistry of cytochrome c at modified Si(100) electrodes
title_full_unstemmed Direct electrochemistry of cytochrome c at modified Si(100) electrodes
title_short Direct electrochemistry of cytochrome c at modified Si(100) electrodes
title_sort direct electrochemistry of cytochrome c at modified si(100) electrodes
url http://hdl.handle.net/20.500.11937/31721