High affinity cation-binding sites in Complex I from Escherichia coli

被引：9

作者：

Euro, Liliya ^{[1
]}

Belevich, Galina ^{[1
]}

Wikstrom, Marten ^{[1
]}

Verkhovskaya, Marina ^{[1
]}

机构：

[1] Univ Helsinki, Inst Biotechnol, Helsinki Bioenerget Grp, FIN-00014 Helsinki, Finland

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 2009年 / 1787卷 / 08期

基金：

芬兰科学院;

关键词：

Complex I; K(+)-binding site; La(3+)-binding site; NADH-UBIQUINONE OXIDOREDUCTASE; SUBMITOCHONDRIAL PARTICLES; POTASSIUM-ION; MITOCHONDRIAL; TRANSITION; INHIBITION; MEMBRANE; KINETICS; DOMAIN;

D O I：

10.1016/j.bbabio.2009.02.014

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

Studies on the activity of Complex I from Escherichia coli in the presence of different metal cations revealed at least two high affinity metal-binding sites. Membrane-bound or isolated Complex I was activated by K(+) (apparent binding constant similar to 125 mu M) and inhibited by La(3+) (IC(50) = 1 mu M). K(+) and La(3+) do not occupy the same site. Possible localization of these metal-binding sites and their implication in catalysis are discussed. (C) 2009 Elsevier B.V. All rights reserved.

引用

收藏

页码：1024 / 1028

页数：5

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