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Toward Single-Enzyme Molecule Electrochemistry: [NiFe]-Hydrogenase Protein Film Voltammetry at Nanoelectrodes

We have scaled down electrochemical assays of redox-active enzymes enabling us to study small numbers of molecules. Our approach is based on lithographically fabricated Au nanoelectrodes with dimensions down to ca. 70 × 70 nm2. We first present a detailed characterization of the electrodes using a c...

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Bibliographic Details
Published in:ACS nano 2008-12, Vol.2 (12), p.2497-2504
Main Authors: Hoeben, Freek J. M, Meijer, F. Stefan, Dekker, Cees, Albracht, Simon P. J, Heering, Hendrik A, Lemay, Serge G
Format: Article
Language:English
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Summary:We have scaled down electrochemical assays of redox-active enzymes enabling us to study small numbers of molecules. Our approach is based on lithographically fabricated Au nanoelectrodes with dimensions down to ca. 70 × 70 nm2. We first present a detailed characterization of the electrodes using a combination of scanning electron microscopy, cyclic voltammetry, and finite-element modeling. We then demonstrate the viability of the approach by focusing on the highly active [NiFe]-hydrogenase from Allochromatium vinosum immobilized on polymyxin-pretreated Au. Using this system, we successfully demonstrate a distinct catalytic response from less than 50 enzyme molecules. These results strongly suggest the feasibility of using bioelectrochemistry as a new tool for studying redox enzymes at the single-molecule level.
ISSN:1936-0851
1936-086X
DOI:10.1021/nn800518d