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

FEBS Letters

Lunardi, Joël¹  Darrouzet, Elisabeth¹  Dupuis, Alain¹  Issartel, Jean-Paul¹ 

[1]Laboratoire de Bioénergétique Cellulaire et Pathologique (EA 2411-UJF), Département de Biologie Moléculaire et Structurale CEA Grenoble, 17 rue des Martyrs, 38054 Grenoble Cedex 9, France

关键词: Complex I;    Mitochondrion;    Piericidin;    Rotenone;    Ubiquinone;    Rhodobacter capsulatus mutant;    bp;    nucleotide base pair;    IC50;    50% inhibitory concentration;    MyxR;    myxothiazol resistant;    ND;    mitochondrially encoded subunit of the mitochondrial Complex I;    nuo/NUO;    gene/subunit of the bacterial Complex I;    PiR;    piericidin resistant;   

DOI  :  10.1016/S0014-5793(98)00719-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown