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Literature summary extracted from

  • Fadeeva, M.S.; Bertsova, Y.V.; Euro, L.; Bogachev, A.V.
    Cys377 residue in NqrF subunit confers Ag+ sensitivity of Na+-translocating NADH:quinone oxidoreductase from Vibrio harveyi (2011), Biochemistry (Moscow), 76, 186-195.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.2.1.1 replacement of the native chromosomal nqrF gene of Vibrio harveyi strain R3 with the six-histidine-tagged nqrF bearing the C377A mutation. Expression of the wild-type and mutant C377A enzymes in Escherichia coli and Vibrio harveyi VHtag60 cells Vibrio harveyi

Protein Variants

EC Number Protein Variants Comment Organism
7.2.1.1 C377A replacement of the conserved Cys377 residue with alanine in the NqrF subunit results in resistance of the enzyme to Ag+ and to other heavy metal ions. The rate of electron input into the mutant Na+-NQR decreases by about 14fold in comparison to the wild-type enzyme, whereas all other properties of NqrFC377A Na+-NQR including its stability remain unaffected. Cys377 replacement in NqrF subunit does not lead to destabilization of Na+NQR Vibrio harveyi
7.2.1.1 additional information construction of a truncated NqrF subunit, i.e. NqrF', the soluble variant of NqrF containing its Fe-S domain and FAD binding domain Vibrio harveyi

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.2.1.1 2-n-heptyl-4-hydroxyquinoline N-oxide
-
 Vibrio harveyi
7.2.1.1 Ag+ the enzyme is specifically inhibited by low concentrations of silver ions Vibrio harveyi
7.2.1.1 Cd2+ 98% inhibition at 0.1 M, addition of 0.1 M of Cd2+ to the reaction medium results in almost complete inhibition of dNADH:K3 oxidoreductase activity of membrane vesicles from the wild-type strain Vibrio harveyi
7.2.1.1 Cu2+ 89% inhibition at 0.1 M, addition of 0.1 mM of Cu2+ to the reaction medium results in almost complete inhibition of dNADH:K3 oxidoreductase activity of membrane vesicles from the wild-type strain Vibrio harveyi
7.2.1.1 korormicin the antibiotic specifically inhibits Na+-NQR at the level of its interaction with ubiquinone. Korormicin affects the enzyme without competition with quinone and binds the enzyme with high affinity Vibrio harveyi
7.2.1.1 additional information replacement of the conserved Cys377 residue with alanine in the NqrF subunit results in resistance of the enzyme to Ag+ and to other heavy metal ions; the enzyme is sensitive against SH reagents. Modification of Cys383 by heavy metal ions or by SH reagents can prevent hydride ion transport from NADH to FAD and hence interrupt the Na+-NQR activities Vibrio harveyi
7.2.1.1 Pb2+
-
 Vibrio harveyi
7.2.1.1 Zn2+ 93% inhibition at 0.1 M, addition of 0.1 mM of Zn2+ to the reaction medium results in almost complete inhibition of dNADH:K3 oxidoreductase activity of membrane vesicles from the wild-type strain Vibrio harveyi

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.2.1.1 0.0147
-
 NADH pH 8.0, 30°C, wild-type enzyme Vibrio harveyi
7.2.1.1 0.0465
-
 NADH pH 8.0, 30°c, mutant C377A Vibrio harveyi

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.2.1.1 membrane
-
 Vibrio harveyi 16020
-

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 harveyi the redox reaction is coupled with a vectorial transfer of two sodium ions across the membrane, i.e. the ratio Na+/– for Na+-NQR is 1 NAD+ + ubiquinol + n Na+/out
-
 ?

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.2.1.1 additional information in addition to the native quinone reductase reaction, the enzyme can also catalyze a socalled NADH dehydrogenase reaction that includes a singleelectron reduction of soluble quinones or some other electron acceptors (hexaammineruthenium(III), ferricyanide, etc.). This artificial activity does not depend on the concentration of sodium ions and is not coupled with energy conservation. Only the FAD binding domain of the NqrF subunit seems to be required for this activity Vibrio harveyi ?
-
 ?
7.2.1.1 NADH + H+ + ubiquinone + n Na+/in
-
 Vibrio harveyi NAD+ + ubiquinol + n Na+/out
-
 ?
7.2.1.1 NADH + H+ + ubiquinone + n Na+/in the redox reaction is coupled with a vectorial transfer of two sodium ions across the membrane, i.e. the ratio Na+/– for Na+-NQR is 1 Vibrio harveyi NAD+ + ubiquinol + n Na+/out
-
 ?

Subunits

EC Number Subunits Comment Organism
7.2.1.1 More structural analysis of the NqrF subunit, overview Vibrio harveyi

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
7.2.1.1 30
-
 assay at Vibrio harveyi

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2.1.1 8
-
 assay at Vibrio harveyi

Cofactor

EC Number Cofactor Comment Organism Structure
7.2.1.1 FAD non-covalently bound in the NqrF subunit. Conserved residue C383 is involved in the hydride ion transport from NADH to FAD Vibrio harveyi
7.2.1.1 FMN two covalently bound in subunits NqrB und NqrC, attached by phosphoester bonds to threonine residues Vibrio harveyi
7.2.1.1 NADH
-
 Vibrio harveyi
7.2.1.1 riboflavin one non-covalently bound Vibrio harveyi

General Information

EC Number General Information Comment Organism
7.2.1.1 additional information structural analysis of the NqrF subunit, overview Vibrio harveyi