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

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 kba...

Full description

Saved in:
Bibliographic Details
Published inActa medica Lékarskí fakulty Univerzity Karlovy v Hradci Králove Vol. 47; no. 4; pp. 335 - 338
Main Authors Staniová, Jana, Musatov, Andrej, Robinson, Neal C
Format Journal Article
LanguageEnglish
Published Czech Republic Karolinum Press 2004
Subjects
Animals
Cattle
Cytochrome c oxidase
Dimer
Electron Transport
Electron transport activity
Electron Transport Complex IV - chemistry
Enzyme Stability
High hydrostatic pressure
Hydrostatic Pressure
Mitochondria, Heart - enzymology
Monomer
Subunit dissociation
Online AccessGet full text

Cover

More Information
Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1211-4286
1805-9694
DOI:10.14712/18059694.2018.119