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

作者信息

Koshkin V

机构信息

Julius Friedrich Cohnheim Center for Phagocyte Research, Tel-Aviv University, Israel.

出版信息

Biochim Biophys Acta. 1995 Dec 12;1232(3):225-9. doi: 10.1016/0005-2728(95)00123-9.

DOI:10.1016/0005-2728(95)00123-9
PMID:8534675
Abstract

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) FEBS Lett. 327, 57-62; (1994) FEBS 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.

摘要

相似文献

1
Aerobic and anaerobic functioning of superoxide-producing cytochrome b-559 reconstituted with phospholipids.
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2
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Binding of FAD to cytochrome b558 is facilitated during activation of the phagocyte NADPH oxidase, leading to superoxide production.在吞噬细胞NADPH氧化酶激活过程中，FAD与细胞色素b558的结合得到促进，从而导致超氧化物的产生。
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引用本文的文献

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The NADPH oxidase of professional phagocytes--prototype of the NOX electron transport chain systems.专职吞噬细胞的NADPH氧化酶——NOX电子传递链系统的原型。
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2
The mechanism of activation of NADPH oxidase in the cell-free system: the activation process is primarily catalytic and not through the formation of a stoichiometric complex.无细胞体系中NADPH氧化酶的激活机制：激活过程主要是催化性的，而非通过形成化学计量复合物。
Biochem J. 1999 Jul 15;341 ( Pt 2)(Pt 2):251-5.