2026-06-14T03:47:11Zhttps://repisalud.isciii.es/rest/oai/requestoai:repisalud.isciii.es:20.500.12105/52402024-09-27T07:57:07Zcom_20.500.12105_19604com_20.500.12105_2051col_20.500.12105_19605col_20.500.12105_19607
Repisalud
author
Guaras, Adela
author
Perales-Clemente, Ester
author
Calvo, Enrique
author
Acin-Perez, Rebeca
author
Loureiro, Marta
author
Pujol, Claire
author
Martinez-Carrascoso, Isabel
author
Nunez, Estefania
author
Garcia-Marques, Fernando
author
Angeles Rodriguez-Hernandez, Maria
author
Cortes, Ana
author
Diaz, Francisca
author
Perez-Martos, Acisclo
author
Moraes, Carlos T.
author
Fernandez-Silva, Patricio
author
Trifunovic, Aleksandra
author
Navas, Placido
author
Vazquez, Jesus
author
Enriquez, Jose Antonio
funder
Ministerio de Economía y Competitividad (España)
funder
Comunidad de Madrid (España)
funder
Unión Europea. Comisión Europea
funder
Instituto de Salud Carlos III
funder
National Institutes of Health (Estados Unidos)
funder
Fundación ProCNIC
2017-10-30T13:32:25Z
2017-10-30T13:32:25Z
2016
Cell Rep. 2016; 15(1):197-209
10.1016/j.celrep.2016.03.009
2211-1247
Cell Reports
27052170
http://hdl.handle.net/20.500.12105/5240
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.
eng
ELECTRON-TRANSPORT CHAIN
MITOCHONDRIAL COMPLEX I
CYTOCHROME-C-OXIDASE
MAMMALIAN MITOCHONDRIA
SUPRAMOLECULAR ORGANIZATION
MOUSE FIBROBLASTS
B GENE
ASSEMBLY/STABILITY
SUPERCOMPLEXES
PHOSPHORYLATION
The CoQH2/CoQ Ratio Serves as a Sensor of Respiratory Chain Efficiency
journal article
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TheCoQH2-CoQRatioServes_2016
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TheCoQH2-CoQRatioServes_2016.txt