6533b857fe1ef96bd12b3a42
RESEARCH PRODUCT
Cherimolin-1, New Selective Inhibitor of the First Energy-Coupling Site of the NADH:Ubiquinone Oxidoreductase (Complex I)
Diego CortesErnesto EstornellJosé R. Tormosubject
StereochemistryBiophysicsEnergy couplingBiologyBiochemistryLactonesStructure-Activity Relationshipchemistry.chemical_compoundOxidoreductaseNAD(P)H Dehydrogenase (Quinone)AnimalsStructure–activity relationshipFuransMode of actionMolecular Biologychemistry.chemical_classificationBinding SitesPlant ExtractsCell BiologyElectron transport chainEnzymeMitochondrial respiratory chainchemistryFruitAcetogeninCattleEnergy Metabolismdescription
The mechanism linking electron transport to proton translocation in the NADH:ubiquinone oxidoreductase (complex I of the mitochondrial respiratory chain) is still unclear. Inhibitors acting at different sites of the enzyme are powerful tools to clarify this mechanism. Up to now, a unique inhibitor, the Annonaceous acetogenin rolliniastatin-2, selectively blocks the most internal proton-translocation site. This study introduces cherimolin-1, a new acetogenin that inhibits the complex I with this special mode of action, which is more easily available from the plant material. Moreover, the mode of action of this scarce type of complex I inhibitor is further characterized.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1997-11-21 | Biochemical and Biophysical Research Communications |