Stability of bovine cytochrome C oxidase as studied after exposure to high hydrostatic pressure.

Jana Staniová, Andrej Musatov, Neal C. Robinson

Research output: Contribution to journalArticle

1 Scopus citations

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 languageEnglish (US)
Pages (from-to)335-338
Number of pages4
JournalActa medica (Hradec Králové) / Universitas Carolina, Facultas Medica Hradec Králové
Volume47
Issue number4
DOIs
StatePublished - 2004

ASJC Scopus subject areas

  • Medicine(all)

Fingerprint Dive into the research topics of 'Stability of bovine cytochrome C oxidase as studied after exposure to high hydrostatic pressure.'. Together they form a unique fingerprint.

Cite this