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Literature summary for 7.2.1.1 extracted from

  • Belevich, N.; Bertsova, Y.; Verkhovskaya, M.; Baykov, A.; Bogachev, A.
    Identification of the coupling step in Na+-translocating NADH quinone oxidoreductase from real-time kinetics of electron transfer (2016), Biochim. Biophys. Acta, 1857, 141-149 .
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Na+ electron transfer from the [2Fe-2S] cluster to the Cys4[Fe] center and all subsequent steps are markedly accelerated when Na+ concentration is increased from 20 miroM to 25 mM Vibrio harveyi

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Vibrio harveyi
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information real-time kinetic analyses of the six consecutive reaction steps of Na+-NQR reduction by NADH. The Cys4[Fe] center is alternatively exposed to either side of the membrane, allowing the [2Fe-2S] cluster of subunit NqrF and the FMN residue of subunit NqrC to alternatively approach the Cys4[Fe] center from different sides of the membrane Vibrio harveyi ?
-
?

Cofactor

Cofactor Comment Organism Structure
FAD
-
Vibrio harveyi
[2Fe-2S]-center electron transfer from the [2F2-2S] cluster to the Cys4[Fe] center and all subsequent steps are markedly accelerated when Na+ concentration is increased from 20 miroM to 25 mM Vibrio harveyi