Toward single-enzyme molecule electrochemistry: [NiFe]-hydrogenase protein film voltammetry at nanoelectrodes
| Authors |
|
|---|---|
| Publication date | 2008 |
| Journal | ACS Nano |
| Volume | Issue number | 2 | 12 |
| Pages (from-to) | 2497-2504 |
| Organisations |
|
| 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 x 70 nm(2). 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.
|
| Document type | Article |
| Language | English |
| Published at | https://doi.org/10.1021/nn800518d |
| Permalink to this page | |