Cytochrome c Peroxidase from Phanerochaete chrysosporium

Cytochrome c peroxidase from the while-rot basidiomycete phanerochaete chrysosporium (PcCcP) was investigated. A phylogenic analysis of PcCcP amino acid sequence showed that PcCcP was closely related to cytochrome c peroxidase from Saccharomyces cereviside (yeastCcP) and per cytosolic ascorbate peroxidase (APX). Recombinant PcCcP was obtained by expression in Eshchericia coil and a heme incorporation into the apoenzymes. Spectral characteristics indicated that the heme iron of PcCcP was mainly 5-coordinated high spin species. The absorption spectrum of PcCcP compound and rapid-scan spectra of compound Ⅰ formation strongly suggested that PcCcP compound Ⅰ was ferryoxy heme iron and protein cation radical, as observed in yeastCcP. Although several typical peroxidase substrates, small organic inorganic compounds, were not oxidized by PcCcP, ferrocytochrome c was effectively oxidazed. Both PcCcP and yeastCcP shared catalytic features. A homology modeling of PcCcP and cytochrome c from P. chrysosporium (PcCc) stringly suggested the interaction between PcCcP and PcCc.