Abstract
Structural and functional stability of bovine cytochrome c oxidase as a function of exposure to high hydrostatic pressure is reported. The pressure affects the stability of monomeric and dimeric enzyme quite differently. Exposure of the monomeric cytochrome c oxidase to pressures higher than 2.5 kbar causes dissociation of subunits III, VIa, VIb, VIIa with a 35-50% decrease in electron transport activity. Dimeric enzyme is more resistant to high hydrostatic pressure since subunits III and VIIa do not dissociate and the electron transport activity loss is minimal.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 335-338 |
| Number of pages | 4 |
| Journal | Acta medica (Hradec Králové) / Universitas Carolina, Facultas Medica Hradec Králové |
| Volume | 47 |
| Issue number | 4 |
| DOIs | |
| State | Published - 2004 |
| Externally published | Yes |
ASJC Scopus subject areas
- Medicine(all)