Toward single-enzyme molecule electrochemistry: [NiFe] - Hydrogenase protein film voltammetry at nanoelectrodes

Freek J.M. Hoeben, F. Stefan Meijer, Cees Dekker, Simon P.J. Albracht, Hendrik A. Heering*, Serge G. Lemay

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

83 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)2497-2504
Number of pages8
JournalACS nano
Volume2
Issue number12
DOIs
Publication statusPublished - 23 Dec 2008
Externally publishedYes

Keywords

  • [NiFe]
  • Cyclic voltammetry
  • Finite-element
  • Hydrogenase
  • Modeling
  • Nanoelectrodes
  • Nanofabricatlon
  • Protein film voltammetry
  • Redox enzymes

Fingerprint Dive into the research topics of 'Toward single-enzyme molecule electrochemistry: [NiFe] - Hydrogenase protein film voltammetry at nanoelectrodes'. Together they form a unique fingerprint.

Cite this