Literature summary for 7.2.1.1 extracted from

Bogachev, A.V.; Kulik, L.V.; Bloch, D.A.; Bertsova, Y.V.; Fadeeva, M.S.; Verkhovsky, M.I.
Redox properties of the prosthetic groups of Na(+)-translocating nadh:quinone oxidoreductase. 1. Electron paramagnetic resonance study of the enzyme (2009), Biochemistry, 48, 6291-6298.

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe	defined by dipole-dipole magnetic interaction measurements, the interspin distance between the [2Fe-2S]+ cluster and the NqrB subunit-bound FMN anion radical is found to be 22.5 A, which means that for the functional electron transfer between these two centers another cofactor, most likely FMN bound to the NqrC subunit, should be located	Vibrio harveyi

Organism

Organism	UniProt	Comment	Textmining
Vibrio harveyi	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	Na+-translocating NADH:quinone oxidoreductases activity	Vibrio harveyi	?	-	?

Synonyms

Synonyms	Comment	Organism
Na+-NQR	-	Vibrio harveyi
Na+-translocating NADH:quinone oxidoreductase	-	Vibrio harveyi
NADH:quinone oxidoreductase	-	Vibrio harveyi

Cofactor

Cofactor	Comment	Organism	Structure
FAD	noncovalently bound FAD located in the NqrF subunit	Vibrio harveyi
flavin	covalently bound to the NqrB subunit	Vibrio harveyi
FMN	FMN covalently bound to the NqrC subunit. Defined by dipole-dipole magnetic interaction measurements, the interspin distance between the [2Fe-2S]+ cluster and the NqrB subunit-bound FMN anion radical is found to be 22.5 A, which means that for the functional electron transfer between these two centers another cofactor, most likely FMN bound to the NqrC subunit, should be located	Vibrio harveyi

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Release 2023.1 (January 2023)