Abstract
Electron transfer kinetic parameters of site-specifically wired copper oxidase were investigated. The enzyme's orientation towards the electrode was controlled by incorporation of propargyl-l-lysine as a site-specific anchoring point. Herein, we demonstrate the importance of immobilization orientation and how it affects electron transfer efficiency and kinetics to each of the enzyme's two active sites.
| Original language | American English |
|---|---|
| Pages (from-to) | 6159-6166 |
| Number of pages | 8 |
| Journal | Physical Chemistry Chemical Physics |
| Volume | 20 |
| Issue number | 9 |
| DOIs | |
| State | Published - 1 Jan 2018 |
All Science Journal Classification (ASJC) codes
- General Physics and Astronomy
- Physical and Theoretical Chemistry
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