Differential stability of dimeric and monomeric cytochrome c oxidase exposed to elevated hydrostatic pressure.

ABSTRACT: Detergent-solubilized dimeric and monomeric cytochrome c oxidase (CcO) have significantly different quaternary stability when exposed to 2-3 kbar of hydrostatic pressure. Dimeric, dodecyl maltoside-solubilized cytochrome c oxidase is very resistant to elevated hydrostatic pressure with almost no perturbation of its quaternary structure or functional activity after release of pressure. In contrast to the stability of dimeric CcO, 3 kbar of hydrostatic pressure triggers multiple structural and functional alterations within monomeric cytochrome c oxidase. The perturbations are either irreversible or slowly reversible since they persist after the release of high pressure. Therefore, standard biochemical analytical procedures could be used to quantify the pressure-induced changes after the rele

SUBMITTER: Stanicova J 

PROVIDER: S-EPMC2561924 | biostudies-literature | 2007 Jun

REPOSITORIES: biostudies-literature