Abstract
By simultaneous analysis of the on-time distribution and autocorrelation function of a single working cholesterol oxidase enzyme, a diffusional model reveals the coupling of conformation change with enzyme action. Active-site oxidation induces a conformational change-that opens the path for substrate entry. Its binding, in turn, induces the reverse protein relaxation process, which tightens the active site, thereby reducing the rate of product release.
| Original language | English |
|---|---|
| Pages (from-to) | 7830-7834 |
| Number of pages | 5 |
| Journal | Journal of Physical Chemistry B |
| Volume | 104 |
| Issue number | 32 |
| DOIs | |
| State | Published - 17 Aug 2000 |