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Title: The CoQH2/CoQ Ratio Serves as a Sensor of Respiratory Chain Efficiency.
Authors: Guarás, Adela
Perales-Clemente, Ester
Calvo, Enrique
Acín-Pérez, Rebeca
Loureiro-Lopez, Marta
Pujol, Claire
Martínez-Carrascoso, Isabel
Nuñez, Estefanía
García-Marqués, Fernando
Rodríguez-Hernández, María Angeles
Cortés, Ana
Diaz, Francisca
Pérez-Martos, Acisclo
Moraes, Carlos T
Fernández-Silva, Patricio
Trifunovic, Aleksandra
Navas, Plácido
Vazquez, Jesús
Enríquez, Jose A
metadata.dc.subject.mesh: Animals
Cell Line
Electron Transport
Electron Transport Chain Complex Proteins
Flavin-Adenine Dinucleotide
Mice, Inbred C57BL
Reactive Oxygen Species
Issue Date: 24-Mar-2016
Abstract: Electrons feed into the mitochondrial electron transport chain (mETC) from NAD- or FAD-dependent enzymes. A shift from glucose to fatty acids increases electron flux through FAD, which can saturate the oxidation capacity of the dedicated coenzyme Q (CoQ) pool and result in the generation of reactive oxygen species. To prevent this, the mETC superstructure can be reconfigured through the degradation of respiratory complex I, liberating associated complex III to increase electron flux via FAD at the expense of NAD. Here, we demonstrate that this adaptation is driven by the ratio of reduced to oxidized CoQ. Saturation of CoQ oxidation capacity induces reverse electron transport from reduced CoQ to complex I, and the resulting local generation of superoxide oxidizes specific complex I proteins, triggering their degradation and the disintegration of the complex. Thus, CoQ redox status acts as a metabolic sensor that fine-tunes mETC configuration in order to match the prevailing substrate profile.
metadata.dc.identifier.doi: 10.1016/j.celrep.2016.03.009
Appears in Collections:Producción 2020

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