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Literature summary extracted from

  • Nedielkov, R.; Steffen, W.; Steuber, J.; Moller, H.M.
    NMR reveals double occupancy of quinone-type ligands in the catalytic quinone binding site of the Na+-translocating NADH:quinone oxidoreductase from Vibrio cholerae (2013), J. Biol. Chem., 288, 30597-30606.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.2.1.1 expression of N-terminally His6-tagged full-length enzyme and large subunit NqrA in Escherichia coli strain BL21(DE3) Vibrio cholerae serotype O1

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.2.1.1 2,5-dibromo-3-methyl-6-isopropyl-4-benzoquinone a known inhibitor of the bc1 and b6f complexes found in mitochondria and chloroplasts, also inhibits quinone reduction by the Na+-NQR in a mixed inhibition mode. It does not just act as a simple competitor or redox mediator at the quinol oxidase site, but also as an antagonist to ubiquinone, inducing a redox bypass of the respiratory chain. The compound both acts as an inhibitor and as an alternative substrate of the Na+-NQR of Vibrio cholerae by a specific interaction with the NqrA subunit of the complex Vibrio cholerae serotype O1
7.2.1.1 2-n-heptyl-4-hydroxyquinoline N-oxide
-
 Vibrio cholerae serotype O1
7.2.1.1 korormicin
-
 Vibrio cholerae serotype O1

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.2.1.1 additional information
-
 additional information Michaelis-Menten kinetics in the absence of 2,5-dibromo-3-methyl-6-isopropyl-4-benzoquinone Vibrio cholerae serotype O1
7.2.1.1 0.0245
-
 ubiquinone pH 7.5, 25°C, quinol formation Vibrio cholerae serotype O1
7.2.1.1 0.0296
-
 NADH pH 7.5, 25°C, NADH oxidation Vibrio cholerae serotype O1

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.2.1.1 membrane
-
 Vibrio cholerae serotype O1 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.2.1.1 Fe2+ 2 [2Fe-2S] clusters iin the NqrF subunit Vibrio cholerae serotype O1

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.2.1.1 NADH + H+ + ubiquinone + n Na+/in Vibrio cholerae serotype O1
-
 NAD+ + ubiquinol + n Na+/out
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
7.2.1.1 Vibrio cholerae serotype O1
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.2.1.1 recombinant N-terminally His6-tagged full-length enzyme and large subunit NqrA from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration Vibrio cholerae serotype O1

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.2.1.1 additional information 2,5-dibromo-3-methyl-6-isopropyl-4-benzoquinone both acts as an inhibitor and as an alternative substrate of the Na+-NQR of Vibrio cholerae by a specific interaction with the NqrA subunit of the complex Vibrio cholerae serotype O1 ?
-
 ?
7.2.1.1 NADH + H+ + ubiquinone + n Na+/in
-
 Vibrio cholerae serotype O1 NAD+ + ubiquinol + n Na+/out
-
 ?
7.2.1.1 NADH + H+ + ubiquinone-1 + n Na+/in subunit NqrA of the Na+-NQR harbours a Q binding site, and the catalytic site of quinone reduction is located on NqrA Vibrio cholerae serotype O1 NAD+ + ubiquinol-1 + n Na+/out
-
 ?

Subunits

EC Number Subunits Comment Organism
7.2.1.1 hexamer the enzyme consists of four membrane-bound subunits NqrBCDE and the peripheral NqrF and NqrA subunits. The catalytic site of quinone reduction is located on subunit NqrA Vibrio cholerae serotype O1

Synonyms

EC Number Synonyms Comment Organism
7.2.1.1 Na+-NQR
-
 Vibrio cholerae serotype O1
7.2.1.1 Na+-translocating NADH:quinone oxidoreductase
-
 Vibrio cholerae serotype O1
7.2.1.1 sodium ion-translocating NADH:quinone oxidoreductase
-
 Vibrio cholerae serotype O1

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
7.2.1.1 25
-
 assay at Vibrio cholerae serotype O1

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2.1.1 7.5
-
 assay at Vibrio cholerae serotype O1

Cofactor

EC Number Cofactor Comment Organism Structure
7.2.1.1 FAD non-covalently bound in the NqrF subunit Vibrio cholerae serotype O1
7.2.1.1 FMN two covalently bound in subunits NqrB und NqrC Vibrio cholerae serotype O1
7.2.1.1 NADH
-
 Vibrio cholerae serotype O1
7.2.1.1 riboflavin one non-covalently bound in the subunit NqrB Vibrio cholerae serotype O1

General Information

EC Number General Information Comment Organism
7.2.1.1 additional information Na+-NQR is composed of six subunits NqrA-F and harbours at least five redox active cofactors: A non-covalently bound FAD and a 2Fe-2S cluster in the NqrF subunit, two covalently bound FMNs. The catalytic site of quinone reduction is located on NqrA. The two ligands bind to an extended binding pocket in direct vicinity to each other Vibrio cholerae serotype O1
7.2.1.1 physiological function the enzyme exploits the free energy liberated during oxidation of NADH with ubiquinone to pump sodium ions across the cytoplasmic membrane Vibrio cholerae serotype O1