Cytochrome c peroxidase from Phanerochaete chrysosporium

Cytochrome c peroxidase from the white-rot basidiomycete Phanerochate chrysosporium (PcCcP) was investigated. A phylogenic analysis of PcCcP amino acid sequence showed that PcCcP was closely related to cytochrome c peroxidase from Saccharomyces cerevisiae (yeastCcP) and pea cytosolic ascorbate peroxidase (APX). Recombinant PcCcP was obtained by expression in Eshcherichia coil and a heme incorporation into the apoenzymes. Spectral charactersitics indicated that the heme iron of PcCcP was mainly 5-coordinated high spin species. The absorption spectrum of PcCcP compound I 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 or inorganic compounds, were not oxidized by PcCcP, ferrocytochrome c was effectively oxidized. Both PcCcP and yeastCcP shared catalytic features. A homology modeling of PcCcP and cytochrome c from P. chrysosporium (PcCc) strongly suggested the interaction between PcCcP and PcCc.