Literature summary 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 .

Activating Compound

EC Number	Activating Compound	Comment	Organism	Structure
7.2.1.1	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

EC Number	Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

EC Number	Organism	UniProt	Comment	Textmining
7.2.1.1	Vibrio harveyi	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
7.2.1.1	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

EC Number	Cofactor	Comment	Organism	Structure
7.2.1.1	FAD	-	Vibrio harveyi
7.2.1.1	[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

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Release 2023.1 (January 2023)