Direct Electrochemistry of Cytochrome c at Modified Si(100) Electrodes |
| |
Authors: | Simone Ciampi J?Justin Gooding Prof?Dr |
| |
Institution: | School of Chemistry, The University of New South Wales, Sydney, NSW, 2052 (Australia), Fax: (+61)?2‐93855384 |
| |
Abstract: | 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. |
| |
Keywords: | bioelectrochemistry cytochromes hydrosilylation monolayers silicon |
|
|