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Direct Electrochemistry of Cytochrome c at Modified Si(100) Electrodes
Author(s) -
Ciampi Simone,
Gooding J. Justin
Publication year - 2010
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.200903316
Subject(s) - isonicotinic acid , chemistry , monolayer , moiety , cyclic voltammetry , electrochemistry , redox , alkyl , dielectric spectroscopy , electron transfer , self assembled monolayer , combinatorial chemistry , photochemistry , polymer chemistry , electrode , stereochemistry , inorganic chemistry , organic chemistry , hydrazide , biochemistry
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 para ‐ester 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.