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Literature summary extracted from

  • Birrell, J.A.; Hirst, J.
    Investigation of NADH binding, hydride transfer, and NAD+ dissociation during NADH oxidation by mitochondrial complex I using modified nicotinamide nucleotides (2013), Biochemistry, 52, 4048-4055.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.1.1.2 additional information inhibition of flavin-site reactions by NADH analogues and fragments, overview Bos taurus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.1.1.2 mitochondrial inner membrane
-
 Bos taurus 5743
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.1.1.2 NADH + ubiquinone + 6 H+[side 1] Bos taurus
-
 NAD+ + ubiquinol + 7 H+[side 2]
-
 ?

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
7.1.1.2 NADH + ubiquinone + 6 H+[side 1] = NAD+ + ubiquinol + 7 H+[side 2] reaction mechanism, overview Bos taurus
a

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 + ubiquinone + 6 H+[side 1]
-
 Bos taurus NAD+ + ubiquinol + 7 H+[side 2]
-
 ?

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
7.1.1.2 32
-
 assay at Bos taurus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
7.1.1.2 7.5
-
 assay at Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
7.1.1.2 NADH the adenosine moiety is crucial for binding, while the nicotinamide is detrimental to binding Bos taurus

General Information

EC Number General Information Comment Organism
7.1.1.2 additional information mechanism of NADH oxidation by complex I, the adenosine moiety of NADH is crucial for binding, overview Bos taurus
7.1.1.2 physiological function NADH:ubiquinone oxidoreductase (complex I) is a complicated respiratory enzyme that conserves the energy from NADH oxidation, coupled to ubiquinone reduction, as a proton motive force across the mitochondrial inner membrane. During catalysis, NADH oxidation by a flavin mononucleotide is followed by electron transfer to a chain of iron-sulfur clusters. Alternatively, the flavin may be reoxidized by hydrophilic electron acceptors, by artificial electron acceptors in kinetic studies, or by oxygen and redox-cycling molecules to produce reactive oxygen species Bos taurus