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Literature summary for 7.1.1.2 extracted from

  • Esterhazy, D.; King, M.S.; Yakovlev, G.; Hirst, J.
    Production of reactive oxygen species by complex I (NADH:ubiquinone oxidoreductase) from Escherichia coli and comparison to the enzyme from mitochondria (2008), Biochemistry, 47, 3964-3971.
    View publication on PubMed
Search for more literature for 7.1.1.2

Application

Application Comment Organism
degradation quantification of superoxide production from Escherichia coli complex I is very prone to artifacts Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of the NuoE subunit from complex I Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by ion-exchange chromatography and gel filtration Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
amplex red + NADH + O2 the rate of H2O2 formation by complex I strongly depends upon the NAD+/NADH ratio Escherichia coli resorufin + NAD+ + H2O2
-
 ?
dihydroethidium + O2 dihydroethidium reduction shows that, upon reducing O2, it produces approximately 20% superoxide and 80% H2O2 Escherichia coli ethidium + H2O2
-
 ?

Synonyms

Synonyms Comment Organism
complex I
-
 Escherichia coli
NADH:ubiquinone oxidoreductase
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FMN O2 reacts with the fully reduced flavin mononucleotide Escherichia coli
additional information [2Fe-2S] cluster N1a is not the reductant of O2 in complex I, but has a specific role in determining the outcome of O2 reduction Escherichia coli