Cytochrome c peroxidase from Phanerochaete chrysosporium

Daisuke Nonaka, Hiroyuki Wariishi

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish
Pages (from-to)151-164
Number of pages14
JournalJournal of the Faculty of Agriculture, Kyushu University
Volume50
Issue number1
Publication statusPublished - Feb 2005

All Science Journal Classification (ASJC) codes

  • Agricultural and Biological Sciences (miscellaneous)

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