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NADH-泛醌氧化还原酶(复合体I)的49-kDa亚基参与了杀粉蝶菌素和鱼藤酮这两种醌类相关抑制剂的结合。

The 49-kDa subunit of NADH-ubiquinone oxidoreductase (Complex I) is involved in the binding of piericidin and rotenone, two quinone-related inhibitors.

作者信息

Darrouzet E, Issartel J P, Lunardi J, Dupuis A

机构信息

Laboratoire de Bioénergétique Cellulaire et Pathologique, (EA 2411-UJF), Départment de Biologie Moléculaire et Structurale CEA Grenoble, France.

出版信息

FEBS Lett. 1998 Jul 10;431(1):34-8. doi: 10.1016/s0014-5793(98)00719-4.

DOI:10.1016/s0014-5793(98)00719-4
PMID:9684860
Abstract

Piericidin is a potent inhibitor of the mitochondrial and bacterial type I NADH-ubiquinone oxidoreductases (Complex I) and is considered to bind at or close to the ubiquinone binding site(s) of the enzyme. Piericidin-resistant mutants of the bacterium Rhodobacter capsulatus have been isolated and the present work demonstrates that a single missense mutation at the level of the gene encoding the peripheral 49-kDa/NUOD subunit of Complex I is definitely associated with this resistance. Based on this original observation, we propose a model locating the binding site for piericidin (and quinone) at the interface between the hydrophilic and hydrophobic domains of Complex I.

摘要

杀粉蝶菌素是线粒体和细菌I型NADH-泛醌氧化还原酶(复合体I)的强效抑制剂,被认为结合于该酶的泛醌结合位点或其附近。已分离出荚膜红细菌的杀粉蝶菌素抗性突变体,目前的研究表明,复合体I外周49-kDa/NUOD亚基编码基因水平的单个错义突变肯定与这种抗性有关。基于这一最初观察结果,我们提出了一个模型,将杀粉蝶菌素(和醌)的结合位点定位在复合体I亲水和疏水结构域之间的界面处。

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