Oct 1, 1975

Studies on the microsomal electron-transport system of anaerobically grown yeast. III. Spectral characterization of cytochrome P-450

Journal of Biochemistry
Y Yoshida, H Kumaoka

Abstract

A carbon monoxide-binding pigment which shows an absorption peak at about 450 nm in the reduced carbon monoxide difference spectrum was purified from the microsomal fraction of yeast grown anaerobically. The spectral characteristics of the pigment were practically identical with those of cytochrome P-450 of hepatic microsomes, especially from polycyclic hydrocarbon-induced animals. The pigment was denatured to P-420, and bound with ethyl isocyanide in the reduced state. Although Type I spectral change was not evident, the pigment showed Type II and modified Type II spectral changes upon binding with some organic compounds, as in the case of hepatic cytochrome P-450. These observations clearly indicate that the carbon monoxide-binding pigment of yeast microsomes may be designated as cytochrome P-450 of yeast.

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Mentioned in this Paper

Dioxygen
Organic Chemicals
Microsomes
Ethyl isocyanide
Cytochrome P450
Isocyanides
Hepatic
Aniline Compounds
Cytochrome P-450 Oxygenase
Plasma Protein Binding Capacity

About this Paper

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