title: Stability of bovine cytochrome C oxidase as studied after exposure to high hydrostatic pressure.
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.
authors.affiliation: University of Veterinary Medicine, Institute of Chemistry, Biochemistry, and Biophysics, Kosice, Slovak Republic. stanicova@uvm.sk
authors.forename: Jana
authors.initials: J
authors.lastname: Staniová
authors.forename: Andrej
authors.initials: A
authors.lastname: Musatov
authors.forename: Neal C
authors.initials: NC
authors.lastname: Robinson
mesh_terms: D000818:Animals; D002417:Cattle; D004579:Electron Transport; D003576:Electron Transport Complex IV / Q000737:chemistry*; D004795:Enzyme Stability; D006874:Hydrostatic Pressure; D008929:Mitochondria, Heart / Q000201:enzymology*
chemical_list: D003576:Electron Transport Complex IV