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Literature summary for 1.5.5.1 extracted from

  • Zhang, J.; Frerman, F.E.; Kim, J.J.
    Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone pool (2006), Proc. Natl. Acad. Sci. USA, 103, 16212-16217.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.5.5.1

Crystallization (Commentary)

Crystallization (Comment) Organism
with and without substrate ubiquinone. Molecule forms a single structural domain binding FAD, the 4Fe-4S cluster and ubiquinone in three functional regions that are closely packed and share structural elements Sus scrofa

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion inner mitochondrial membrane Sus scrofa 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Iron 4Fe-4S center Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Reaction

Reaction Comment Organism Reaction ID
reduced electron-transferring flavoprotein + ubiquinone = electron-transferring flavoprotein + ubiquinol when enzyme is reduced to a two-electron reduced state, with one electron at each redox center, it is primed to reduce ubiquinone via FAD Sus scrofa
a

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Sus scrofa