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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Darrouzet E,Issartel JP,Lunardi J,Dupuis A

doi

10.1016/s0014-5793(98)00719-4

subject

Has Abstract

pub_date

1998-07-10 00:00:00

pages

34-8

issue

1

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(98)00719-4

journal_volume

431

pub_type

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