REACTIVITY OF AN FAD-DEPENDENT OXYGENASE WITH FREE FLAVINS - NEW MODE OF UNCOUPLING IN FLAVOPROTEIN OXYGENASES

被引：15

作者：

KISHORE, GM ^{[1
]}

SNELL, EE ^{[1
]}

机构：

[1] UNIV TEXAS,DEPT CHEM,AUSTIN,TX 78712

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1979年 / 87卷 / 02期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/0006-291X(79)91826-6

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：

Conversion of 2-methyl-3-hydroxypyridine-5-carboxylic acid (Cpd I) to α-(N-acetylaminomethylene)succinic acid (Cpd A) is catalyzed by an FAD protein, Cpd I oxygenase (Sparrow, et al., J. Biol. Chem. [1969] 244, 2590-2600) according to the equation: Cpd I + O2 + NADH + H+ → Cpd A + NAD+. When free FAD, FMN or riboflavin is added to reaction mixtures, oxidation of NADH remains dependent on presence of oxygenase and Cpd I, but is partially uncoupled from the oxygenation of Cpd I. Under these conditions, free reduced flavins appear in solution, as shown by their ability to reduce cytochrome c. These effects are not due to an increased rate of NADH oxidation. Such uncoupling may lead to appearance of artifactual species of activated oxygen or flavin that play no intermediate role in the oxygenase reaction. © 1979.

引用

页码：518 / 523

页数：6