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 language | English |
|---|---|
| Pages (from-to) | 151-164 |
| Number of pages | 14 |
| Journal | Journal of the Faculty of Agriculture, Kyushu University |
| Volume | 50 |
| Issue number | 1 |
| Publication status | Published - Feb 2005 |
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All Science Journal Classification (ASJC) codes
- Agricultural and Biological Sciences (miscellaneous)
Cite this
Cytochrome c peroxidase from Phanerochaete chrysosporium. / Nonaka, Daisuke; Wariishi, Hiroyuki.
In: Journal of the Faculty of Agriculture, Kyushu University, Vol. 50, No. 1, 02.2005, p. 151-164.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Cytochrome c peroxidase from Phanerochaete chrysosporium
AU - Nonaka, Daisuke
AU - Wariishi, Hiroyuki
PY - 2005/2
Y1 - 2005/2
N2 - 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.
AB - 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.
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M3 - Article
AN - SCOPUS:15044346070
VL - 50
SP - 151
EP - 164
JO - Journal of the Faculty of Agriculture, Kyushu University
JF - Journal of the Faculty of Agriculture, Kyushu University
SN - 0023-6152
IS - 1
ER -