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Evidence for a quinone binding site close to the interface between NUOD and NUOB subunits of Complex I
I Prieur1, J Lunardi, A Dupuis
1Laboratoire de Bioénergétique Cellulaire et Pathologique (EA 2943-UJF), Département de Biologie Moléculaire et Structurale CEA Grenoble, 17 rue des Martyrs, 38054 Cedex 9, Grenoble, France. iprieur@cea.fr
Biochimica Et Biophysica Acta
|March 14, 2001
Abstract:
Piericidin, rotenone and pyridaben are specific inhibitors of the NADH-ubiquinone oxidoreductase (Complex I) that bind to its ubiquinone binding site(s). Using site directed mutagenesis, we demonstrate that residues G409, D412, R413 and V407 of the C-terminus of Complex I NUOD subunit are directly involved in the binding of these inhibitors. We propose that the corresponding inhibitor/quinone binding site would be located close to NUOD-NUOB interface.