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Literature summary for 7.1.1.2 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

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

Localization

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Reaction

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

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NADH + ubiquinone + 6 H+[side 1]
-
Bos taurus NAD+ + ubiquinol + 7 H+[side 2]
-
?

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

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

General Information

General Information Comment Organism
additional information mechanism of NADH oxidation by complex I, the adenosine moiety of NADH is crucial for binding, overview Bos taurus
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