LOW-TEMPERATURE SPECTRAL PROPERTIES OF MAMMALIAN CYTOCHROME OXIDASE .I. ENZYME IN INTACT RAT-LIVER MITOCHONDRIA

被引：29

作者：

WILSON, DF

GILMOUR, MV

机构：

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1967年 / 143卷 / 01期

关键词：

D O I：

10.1016/0005-2728(67)90108-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The liquid-N2 temperature spectra of cytochrome oxidase (cytochrome c: O2 oxidoreductase, EC 1.9.3.1) in rat-liver mitochondria are presented. Sulfide is postulated to inhibit respiration by forming an oxidized cytochrome a3-sulfide compound. The azide-inhibited cytochrome oxidase is characterized by the presence of a form of reduced cyto-chrome a which has a spectrum different from the usual spectrum of reduced cytochrome a both in the alpha and Soret regions. No evidence was found for interaction of cytochromes a and a3 in such a manner that either the spectrum of the reduced cytochrome a or its reactivity toward azide were affected by the valence state of cytochrome a3.

引用

页码：52 / +

页数：1