Stability of Bovine Cytochrome <i>c</i> Oxidase as Studied After Exposure to High Hydrostatic Pressure

Staničová, Jana; Musatov, Andrej; Robinson, Neal C.

doi:10.14712/18059694.2018.119

Acta Medica > Archive > 2004, Vol. 47 > Issue 4 > Stability of Bovine Cytochrome c…

Acta Med. 2004, 47: 335-338

https://doi.org/10.14712/18059694.2018.119

Stability of Bovine Cytochrome c Oxidase as Studied After Exposure to High Hydrostatic Pressure

Jana Staničová^a, Andrej Musatov^b, Neal C. Robinson^b

^aUniversity of Veterinary Medicine, Institute of Chemistry, Biochemistry, and Biophysics, Košice, Slovak Republic
^bThe University of Texas Health Science Center, Department of Biochemistry, San Antonio, Texas 78229–3900, USA

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.