Cytochrome b5 is a major reductant in vivo of human indoleamine 2,3-dioxygenase expressed in yeast

被引：33

作者：

Vottero, E ^{[1
]}

Mitchell, DA ^{[1
]}

Page, MJ ^{[1
]}

MacGillivray, RTA ^{[1
]}

Sadowski, IJ ^{[1
]}

Roberge, M ^{[1
]}

Mauk, AG ^{[1
]}

机构：

[1] Univ British Columbia, Life Sci Ctr, Dept Biochem & Mol Biol, Vancouver, BC V6T 1Z3, Canada

来源：

FEBS LETTERS | 2006年 / 580卷 / 09期

基金：

加拿大健康研究院;

关键词：

indoleamine 2,3-dioxygenase; cytochrome b5; autoxidation; electron transfer; yeast growth;

D O I：

10.1016/j.febslet.2006.03.034

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 evolutionary relationship of indoleamine 2,3-dioxygenase (IDO) to some gastropod myoglobins suggests that IDO may undergo autoxidation in vivo such that one or more currently unidentified electron donors are required to maintain IDO heme iron in the active, ferrous state. To evaluate this hypothesis we have used yeast knockout mutants in combination with a recently developed yeast growth assay for IDO activity in vivo to demonstrate a role for cytochrome b(5) and cytochrome b(5) reductase in maintaining IDO activity in vivo. (c) 2006 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：2265 / 2268

页数：4

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