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The 49‐kDa subunit of NADH‐ubiquinone oxidoreductase (Complex I) is involved in the binding of piericidin and rotenone, two quinone‐related inhibitors
Author(s) -
Darrouzet Elisabeth,
Issartel Jean-Paul,
Lunardi Joël,
Dupuis Alain
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00719-4
Subject(s) - electron transport complex i , protein subunit , rhodobacter , oxidoreductase , biochemistry , rotenone , quinone , binding site , biology , mutant , stereochemistry , enzyme , chemistry , mitochondrion , gene
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.