Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.5.5.1 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

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

Metals/Ions

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

Organism

EC Number Organism UniProt Comment Textmining
1.5.5.1 Sus scrofa
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.5.5.1 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

EC Number Cofactor Comment Organism Structure
1.5.5.1 FAD
-
 Sus scrofa