Abstract

Cytochrome c oxidases of prion protein (PrP) gene-deficient (Prnp-/-) and Prnp+/+ mice were examined in vivo and in vitro. Non-invasive near-infrared spectra revealed that oxidation of copper and heme a+a3 in cytochrome c oxidase of Prnp-/- mice was similar to that in Prnp+/+ mice. Biochemical analysis of mitochondrial fractions also supported the results. PrP might not be involved in regulation of cytochrome c oxidase.

Keywords: Prion protein, cytochrome c oxidase, mitochondria, copper