Aerobic and anaerobic functioning of superoxide-producing cytochrome b-559 reconstituted with phospholipids

被引：13

作者：

Koshkin, V

机构：

[1] The Julius Friedrich Cohnheim Center for Phagoccte Research, Tel-Aviv University, Tel-Aviv

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 1995年 / 1232卷 / 03期

基金：

以色列科学基金会;

关键词：

respiratory burst; NADPH oxidase; flavocytochrome b-559; oxygen activation;

D O I：

10.1016/0005-2728(95)00123-9

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：

Cytochrome b-559 reconstituted with phospholipids and FAD represents the simplest model of the respiratory burst NADPH oxidase and reproduces the main catalytic features of this system (Koshkin, V. and Pick, E. (1993) FEES Lett. 327, 57-62; (1994) FEES Lett. 338, 285-289). In the present report it is shown that activation by oxygen, characteristic of the NADPH oxidase complex, is an intrinsic property of flavocytochrome b-559, in principle independent of its complexation with the other components of NADPH oxidase. Facilitation of electron transfer from NADPH to FAD is found to be the reason for this phenomenon. Kinetic studies of anaerobic operation of flavocytochrome b-559 revealed the functional heterogeneity of two hemes, manifested as a dramatic difference in their reducibility under these conditions.

引用

页码：225 / 229

页数：5

共 37 条

[1] OXYGEN PULSED CYTOCHROME-C OXIDASE - FUNCTIONAL PROPERTIES AND CATALYTIC RELEVANCE [J].