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Literature summary extracted from

  • Ohnishi, T.; Ohnishi, S.T.; Shinzawa-Ito, K.; Yoshikawa, S.
    Functional role of coenzyme Q in the energy coupling of NADH-CoQ oxidoreductase (Complex I): stabilization of the semiquinone state with the application of inside-positive membrane potential to proteoliposomes (2008), Biofactors, 32, 13-22.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.1.1.2 Piericidin A degree of inhibition for the reaction with decylubiquinone is higher than for the reaction with ubiquinone-1 as electron acceptor Bos taurus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.1.1.2 mitochondrion
-
 Bos taurus 5739
-

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.2 Bos taurus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.1.1.2
-
 Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
7.1.1.2 heart
-
 Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.2 NADH + H+ + decylubiquinone decylubiquinone is slightly better than ubiquinone-1 as electron acceptor Bos taurus NAD+ + decylubiquinol
-
 ?
7.1.1.2 NADH + H+ + ubiquinone-1 formation of the semiquinone signals during steady state electron transfer from NADH to ubiquinone-1 Bos taurus NAD+ + ubiquinol-1
-
 ?

Synonyms

EC Number Synonyms Comment Organism
7.1.1.2 complex I
-
 Bos taurus
7.1.1.2 NADH-CoQ oxidoreductase
-
 Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
7.1.1.2 NADH
-
 Bos taurus