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Enzyme Nomenclature
Information on EC 1.6.5.8 - NADH:ubiquinone reductase (Na+-transporting)
Word Map on EC 1.6.5.8
- 1.6.5.8
- vibrio
- cholerae
- flavin
- fmn
- harveyi
- medicine
- alginolyticus
- riboflavin
-
redox-driven
-
one-electron
- semiquinone
-
na+-dependent
- ubiquinol
-
two-electron
-
flavosemiquinone
- 2-n-heptyl-4-hydroxyquinoline
-
exergonic
-
oxidoreduction
- hqno
-
electrogenic
- ag+
- ubiquinone-1
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.6.5.8
-
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RECOMMENDED NAME
GeneOntology No.
NADH:ubiquinone reductase (Na+-transporting)
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NADH + H+ + ubiquinone + n Na+/in = NAD+ + ubiquinol + n Na+/out
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
NADH:ubiquinone oxidoreductase (Na+-translocating)
An iron-sulfur flavoprotein, containing two covalently bound molecules of FMN, one noncovalently bound FAD, one riboflavin, and one [2Fe-2S] cluster.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
392715, 658029, 658968, 671141, 674705, 698842, 698995, 699385, 710746, 711269, 711293, 711997, 712274, 713414, 725433, 725448, 725481, 725538, 725539, 732791
-
-
Na(+)-translocating NADH-quinone reductase subunit D
SwissProt
Na(+)-translocating NADH-quinone reductase subunit E
SwissProt
Q9KPS1: NqrA, Q9KPS2: NqrB, A5F5Y7: NqrC, Q9X4Q8: NqrF
Q9KPS1 and Q9KPS2 and A5F5Y7 and Q9X4Q8
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
glycine 140 and glycine 141 of the NqrB subunit in the functional binding of ubiquinone. Mutations at these residues alter the affinity of the enzyme for ubiquinol. Mutations in residue NqrBG140 almost completely abolished the electron transfer to ubiquinone
metabolism
physiological function
additional information
metabolism
-
Na+-NQR couples the free energy of electron transfer reactions to electrogenic pumping of sodium across the cell membrane. Na+ uptake by Na+-NQR is a nonelectrogenic process that occurs upon electron transfer from the 2Fe-2S-center to FMN of subunit NqrC, while the electrogenic transport of Na+ across the membrane, and likely release into solution, occurs upon electron transfer from FMN of subunit NqrB to riboflavin
metabolism
-
the enzyme is the main entrance for electrons into the respiratory chain of many marine and pathogenic bacteria. The enzyme accepts electrons from NADH and donates them to ubiquinone, and the free energy released by this redox reaction is used to create an electrochemical gradient of sodium across the cell membrane
physiological function
-
Na+-NQR is a component of respiratory chain and generates a redox-driven transmembrane electrochemical Na+ potential
physiological function
A6XUU9
the sodium ion-translocating NADH:quinone oxidoreductase from the human pathogen Vibrio cholerae is a respiratory membrane protein complex that couples the oxidation of NADHto the transport of Na+ across the bacterial membrane
physiological function
-
the Na+-translocating NADH:quinone oxidoreductase is the entry site for electrons into the respiratory chain and the main sodium pump in Vibrio cholerae
physiological function
-
Vibrio cholerae relies on the Na+-pumping NADH:quinone oxidoreductase as the first complex in its respiratory chain
physiological function
-
the enzyme exploits the free energy liberated during oxidation of NADH with ubiquinone to pump sodium ions across the cytoplasmic membrane
physiological function
-
the enzyme is the entry site of electrons into the aerobic respiratory chain, catalyzing the electron transfer from NADH to ubiquinone, which is coupled to the pumping of sodium ions across the membrane. The sodium gradient produced by Na+-NQR is used by the cell for ATP synthesis, transport of nutrients, rotation of the flagellum, among other processes
physiological function
-
the Vibrio cholerae Na+ translocating NADH:quinone oxidoreductase mutant shows multiple defects in metabolism. The mutant up-regulates 31 genes and down-regulates 55 genes in both early and mid-growth phases. The most up-regulated genes included the cadA and cadB genes, encoding a lysine decarboxylase and a lysine/cadaverine antiporter, respectively. The down-regulated genes include sialic acid catabolism genes. There is also an increase in the reductive pathway of TCA cycle and decreased purine metabolism in the mutant. Lack of Na+ translocating NADH:quinone oxidoreductase does not affect any of the Na+ pumping-related phenotypes of Vibrio cholerae
additional information
structural analysis of the NqrF subunit, overview
additional information
-
subunit NqrB residues G140 and G141 are critical for the binding and reaction of Na+-NQR with its electron acceptor, ubiquinone
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
additional information
-
aspartate 397 in subunit B of the Na+-pumping NADH: quinone oxidoreductase forms part of a sodium binding site, is involved in cation selectivity and affects cation binding site cooperativity. The enzyme is partially functional with only one sodium-binding site, which indicates that the sites are connected to independent and probably parallel sodium pumping pathways
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NADH + H+ + ubiquinone
NADH + ubiquinol
Vibrio cholerae and many other marine and pathogenic bacteria possess a unique respiratory complex, the Na+-pumping NADH:quinone oxidoreductase, which pumps Na+ across the cell membrane using the energy released by the redox reaction between NADH and ubiquinone
-
-
?
NADH + H+ + ubiquinone-8 + n Na+/in
NAD+ + ubiquinol-8 + n Na+/out
A6XUU9
-
-
-
?
reduced nicotinamide hypoxanthine dinucleotide + menadione
oxidited nicotinamide hypoxanthine dinucleotide + menadiol
-
-
-
?
reduced nicotinamide hypoxanthine dinucleotide + menadione
oxidized nicotinamide hypoxanthine dinucleotide + menadiol
-
-
-
?
2 ferricyanide + NADH + n Na+/in
2 ferrocyanide + NAD+ + H+ + n Na+/out
-
-
-
?
2 ferricyanide + NADH + n Na+/in
2 ferrocyanide + NAD+ + H+ + n Na+/out
-
-
-
?
deamino-NADH + H+ + ubiquinone + 2 Na+/in
deamino-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
deamino-NADH + H+ + ubiquinone + 2 Na+/in
deamino-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
deamino-NADH + H+ + ubiquinone + 2 Na+/in
deamino-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
deamino-NADH + H+ + ubiquinone + 2 Na+/in
deamino-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
deamino-NADH + H+ + ubiquinone + 2 Na+/in
deamino-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
deamino-NADH + H+ + ubiquinone + 2 Na+/in
deamino-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
deamino-NADH + H+ + ubiquinone + 2 Na+/in
deamino-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
deamino-NADH + H+ + ubiquinone + 2 Na+/in
deamino-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
deamino-NADH + H+ + ubiquinone + 2 Na+/in
deamino-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
deamino-NADH + H+ + ubiquinone + 2 Na+/in
deamino-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
deamino-NADH + H+ + ubiquinone + 2 Na+/in
deamino-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
deamino-NADH + H+ + ubiquinone + n Na+/in
deamino-NAD+ + ubiquinol + n Na+/out
-
-
-
-
?
deamino-NADH + H+ + ubiquinone + n Na+/in
deamino-NAD+ + ubiquinol + n Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
-
the lack of Na+-NQR activity causes the absence of a transmembrane Na+ gradient and an increase in alginate production
-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
-
the lack of Na+-NQR activity causes the absence of a transmembrane Na+ gradient and an increase in alginate production
-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
-
the Na+-pumping NADH:ubiquinone oxidoreductase is a molecular energy transducer present in the membrane of many marine and pathogenic bacteria. The enzyme accepts electrons from NADH and donates them to ubiquinone. This redox reaction releases a significant amount of energy, which is used to pump Na+ across the cell membrane, creating a Na+ gradient as well as an electrical potential. Electrons flow from NADH to quinone through the FAD in subunit F, the 2Fe-2S center, the FMN in subunit C, the FMN in subunit B, and finally riboflavin. The reduction of the FMN(C) to its anionic flavosemiquinone state is the first Na+-dependent process, suggesting that reduction of this site is linked to Na+ uptake. During the reduction reaction, two FMNs are transformed to their anionic flavosemiquinone in a single kinetic step. Subsequently, FMN(C) is converted to the flavohydroquinone, accounting for the single anionic flavosemiquinone radical in the fully reduced enzyme
-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
-
electrons flow from NADH to quinone through the FAD in subunit F, the 2Fe-2S center, the FMN in subunit C, the FMN in subunit B, and finally riboflavin. The reduction of the FMN(C) to its anionic flavosemiquinone state is the first Na+-dependent process, suggesting that reduction of this site is linked to Na+ uptake. During the reduction reaction, two FMNs are transformed to their anionic flavosemiquinone in a single kinetic step. Subsequently, FMN(C) is converted to the flavohydroquinone, accounting for the single anionic flavosemiquinone radical in the fully reduced enzyme
-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
-
the results on the reverse reaction, in which the oxidized enzyme takes electrons from quinol, confirm that riboflavin, the center that gives rise to the neutral flavosemiquinone, is located downstream of both FMNB and FMNC in the forward pathway. Riboflavin is likely to be the site from which electrons are donated to quinone during enzyme turnover
-
-
r
NADH + H+ + ubiquinone + 2 Na+/in
NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + 2 Na+/in
NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + 2 Na+/in
NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + 2 Na+/in
NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + 2 Na+/in
NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + 2 Na+/in
NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + 2 Na+/in
NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + 2 Na+/in
NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + 2 Na+/in
NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + 2 Na+/in
NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + 2 Na+/in
NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + 2 Na+/in
NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + n Na+/in
NAD+ + ubiquinol + n Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + n Na+/in
NAD+ + ubiquinol + n Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + n Na+/in
NAD+ + ubiquinol + n Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + n Na+/in
NAD+ + ubiquinol + n Na+/out
-
-
-
?
NADH + H+ + ubiquinone + n Na+/in
NAD+ + ubiquinol + n Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + n Na+/in
NAD+ + ubiquinol + n Na+/out
A6XUU9
-
-
-
?
NADH + H+ + ubiquinone + n Na+/in
NAD+ + ubiquinol + n Na+/out
NqrB-G140 and -G141 are critical for the binding and reaction of Na+-NQR with its electron acceptor, ubiquinone
-
-
?
NADH + H+ + ubiquinone + n Na+/in
NAD+ + ubiquinol + n Na+/out
-
the electrons move through the different redox centers in the enzyme in a linear pathway. During the first step of electron transfer, the non-covalently bound FAD accepts two electrons from NADH. Subsequently, the electrons are transferred stepwise by passing to the 2Fe-2S center, the two FMN molecules covalently attached to NqrC and NqrB (in this order), riboflavin, and finally to ubiquinone-8. The one-electron reduction of FMN in NqrC is the step involved in sodium uptake, and the reduction of riboflavin is involved in sodium translocation
-
-
?
NADH + H+ + ubiquinone + n Na+/in
NAD+ + ubiquinol + n Na+/out
-
the large, peripheral NqrA subunit of the Na+-NQR binds one molecule of ubiquinone-8 with high affinity, which is determined by the methoxy groups at the C-2 and C-3 positions of the quinone headgroup. Ubiquinone-8 bound to NqrA occupies a functional site. Analysis of dynamic interaction of NqrA with quinones by surface plasmon resonance and saturation transfer difference NMR. Electron transfer in Na+-NQR is initiated by NADH oxidation on subunit NqrF and leads to quinol formation on subunit NqrA
-
-
?
NADH + H+ + ubiquinone + n Na+/in
NAD+ + ubiquinol + n Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + n Na+/in
NAD+ + ubiquinol + n Na+/out
-
Na+-NQR reduction is not limited by the rate of NADH binding
-
-
?
NADH + H+ + ubiquinone + n Na+/in
NAD+ + ubiquinol + n Na+/out
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
-
-
?
NADH + H+ + ubiquinone-1
NAD+ + ubiquinol-1
-
-
the enzyme catalyzes NADH-driven Na+ transport
-
-
?
NADH + H+ + ubiquinone-1
NAD+ + ubiquinol-1
Q9KPS1 and Q9KPS2 and A5F5Y7 and Q9X4Q8
-
-
-
?
NADH + H+ + ubiquinone-1
NAD+ + ubiquinol-1
Q9KPS1 and Q9KPS2 and A5F5Y7 and Q9X4Q8
the enzyme catalyzes NADH-driven Na+ transport
-
-
?
NADH + H+ + ubiquinone-1
NAD+ + ubiquinol-1
-
the NqrF subunit catalyzes the initial oxidation of NADH
-
-
?
NADH + H+ + ubiquinone-1 + n Li+/in
NAD+ + ubiquinol-1 + n Li+/out
-
-
-
-
?
NADH + H+ + ubiquinone-1 + n Na+/in
NAD+ + ubiquinol-1 + n Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone-1 + n Na+/in
NAD+ + ubiquinol-1 + n Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone-1 + n Na+/in
NAD+ + ubiquinol-1 + n Na+/out
-
-
-
?
NADH + H+ + ubiquinone-1 + n Na+/in
NAD+ + ubiquinol-1 + n Na+/out
-
-
-
?
NADH + H+ + ubiquinone-1 + n Na+/in
NAD+ + ubiquinol-1 + n Na+/out
-
-
-
?
NADH + H+ + ubiquinone-1 + n Na+/in
NAD+ + ubiquinol-1 + n Na+/out
-
subunit NqrA of the Na+-NQR harbours a Q binding site, and the catalytic site of quinone reduction is located on NqrA
-
-
?
NADH + H+ + ubiquinone-1 + n Na+/in
NAD+ + ubiquinol-1 + n Na+/out
A6XUU9
ubiquinone-1 acts as substrate for the oxidation of NADH by the holo-Na+-NQR coupled to Na+ translocation. Ubiquinoone-1 also accepts electrons in a non-physiological reaction catalyzed by isolated NqrF or subcomplexes containing the NqrF subunit. Both the coupled and the non-physiological modes of NADH oxidation with Q1 require FAD as cofactor
-
-
?
NADH + H+ + ubiquinone-1 + n Na+/in
NAD+ + ubiquinol-1 + n Na+/out
-
-
-
?
NADH + H+ + ubiquinone-1 + n Na+/in
NAD+ + ubiquinol-1 + n Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone-1 + n Na+/in
NAD+ + ubiquinol-1 + n Na+/out
-
-
-
?
NADH + ubiquinone
?
-
the enzyme couples the exergonic oxidation of NADH with ubiquinone to the transport of Na+ ions from the inside of a bacterial cell to the periplasmic space
-
-
?
NADH + ubiquinone
?
-
the Na+ pump is coupled to the respiratory chain at the step of NADH:quinone oxidoreductase
-
-
-
NADH + ubiquinone-1
NAD+ + ubiquinol-1
-
electron transfer to ubiquinone-1 involves the semiquinone radical as an intermediate
-
-
?
thio-NADH + H+ + ubiquinone + 2 Na+/in
thio-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
thio-NADH + H+ + ubiquinone + 2 Na+/in
thio-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
thio-NADH + H+ + ubiquinone + 2 Na+/in
thio-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
thio-NADH + H+ + ubiquinone + 2 Na+/in
thio-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
thio-NADH + H+ + ubiquinone + 2 Na+/in
thio-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
thio-NADH + H+ + ubiquinone + 2 Na+/in
thio-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
thio-NADH + H+ + ubiquinone + 2 Na+/in
thio-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
thio-NADH + H+ + ubiquinone + 2 Na+/in
thio-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
thio-NADH + H+ + ubiquinone + 2 Na+/in
thio-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
thio-NADH + H+ + ubiquinone + 2 Na+/in
thio-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
thio-NADH + H+ + ubiquinone + 2 Na+/in
thio-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
additional information
?
-
-
Na+-translocating NADH:quinone oxidoreductases activity, the enzyme also shows NADH-oxidase activity
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction, the isolated enzyme can also catalyze the so-called NADH-dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexaammineruthenium (III), ferricyanide, etc.)
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction, the isolated enzyme can also catalyze the so-called NADH-dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexaammineruthenium (III), ferricyanide, etc.)
-
-
-
additional information
?
-
-
construction of a double NDH-2/NDH-1-deficient strain. Sub-bacterial particles isolated from these strains oxidize NADH entirely via the corresponding Na+-NQR, which makes them a useful tool to study the catalytic properties of these enzymes
-
-
-
additional information
?
-
-
the enzyme also shows NADH-oxidase activity
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction, the isolated enzyme can also catalyze the so-called NADH-dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexaammineruthenium (III), ferricyanide, etc.)
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction, the isolated enzyme can also catalyze the so-called NADH-dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexaammineruthenium (III), ferricyanide, etc.)
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction, the isolated enzyme can also catalyze the so-called NADH-dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexaammineruthenium (III), ferricyanide, etc.)
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinines. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction, the isolated enzyme can also catalyze the so-called NADH-dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexaammineruthenium (III), ferricyanide, etc.)
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction, the isolated enzyme can also catalyze the so-called NADH-dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexaammineruthenium (III), ferricyanide, etc.)
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction, the isolated enzyme can also catalyze the so-called NADH-dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexaammineruthenium (III), ferricyanide, etc.)
-
-
-
additional information
?
-
-
the enzyme is the entry point for electrons into the respiratory chain
-
-
-
additional information
?
-
-
the NADH oxidation is coupled to the pumping of Na+ across the membrane
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction, the isolated enzyme can also catalyze the so-called NADH-dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexaammineruthenium (III), ferricyanide, etc.)
-
-
-
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
-
-
-
additional information
?
-
-
binding activity of subunit NqrA with different quinones, i.e. quinone, ubiquinone-1, ubiquinone-2, ubiquinone-8, 3-azido-2-methoxy-5-methyl-6-geranyl-1,4-benzoquinone, 2-azido-3-methoxy-5-methyl-6-geranyl-1,4-benzoquinone, 3-azido-2-methoxy-5-methyl-6-geranyl-1,4-benzoquinone-biotin, biotinylated 3-azido-2-methoxy-5-methyl-6-geranyl-1,4-benzoquinone, overview
-
-
-
additional information
?
-
-
Na+-NQR enables pumping of Li+, as well as Na+ across the membrane, but the enzyme is not able to translocate other monovalent cations, such as potassium or rubidium
-
-
-
additional information
?
-
-
construction of a NADH-dehydrogenase NDH-2-deficient strain. Sub-bacterial particles isolated from these strains oxidize NADH entirely via the corresponding Na+-NQR, which makes them a useful tool to study the catalytic properties of these enzymes
-
-
-
additional information
?
-
-
Na+-translocating NADH:quinone oxidoreductases activity
-
-
-
additional information
?
-
-
the enzyme also shows NADH-oxidase activity
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction, the isolated enzyme can also catalyze the so-called NADH-dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexaammineruthenium (III), ferricyanide, etc.)
-
-
-
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
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction, the isolated enzyme can also catalyze the so-called NADH-dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexaammineruthenium (III), ferricyanide, etc.)
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NADH + H+ + ubiquinone
NADH + ubiquinol
Q9KPS2
Vibrio cholerae and many other marine and pathogenic bacteria possess a unique respiratory complex, the Na+-pumping NADH:quinone oxidoreductase, which pumps Na+ across the cell membrane using the energy released by the redox reaction between NADH and ubiquinone
-
-
?
deamino-NADH + H+ + ubiquinone + 2 Na+/in
deamino-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
deamino-NADH + H+ + ubiquinone + 2 Na+/in
deamino-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
deamino-NADH + H+ + ubiquinone + 2 Na+/in
deamino-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
deamino-NADH + H+ + ubiquinone + 2 Na+/in
deamino-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
deamino-NADH + H+ + ubiquinone + 2 Na+/in
deamino-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
deamino-NADH + H+ + ubiquinone + 2 Na+/in
deamino-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
deamino-NADH + H+ + ubiquinone + 2 Na+/in
deamino-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
deamino-NADH + H+ + ubiquinone + 2 Na+/in
deamino-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
deamino-NADH + H+ + ubiquinone + 2 Na+/in
deamino-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
deamino-NADH + H+ + ubiquinone + 2 Na+/in
deamino-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
deamino-NADH + H+ + ubiquinone + 2 Na+/in
deamino-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
deamino-NADH + H+ + ubiquinone + n Na+/in
deamino-NAD+ + ubiquinol + n Na+/out
-
-
-
-
?
deamino-NADH + H+ + ubiquinone + n Na+/in
deamino-NAD+ + ubiquinol + n Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
-
the lack of Na+-NQR activity causes the absence of a transmembrane Na+ gradient and an increase in alginate production
-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
-
the lack of Na+-NQR activity causes the absence of a transmembrane Na+ gradient and an increase in alginate production
-
-
?
NADH + H+ + ubiquinone
NAD+ + ubiquinol
-
the Na+-pumping NADH:ubiquinone oxidoreductase is a molecular energy transducer present in the membrane of many marine and pathogenic bacteria. The enzyme accepts electrons from NADH and donates them to ubiquinone. This redox reaction releases a significant amount of energy, which is used to pump Na+ across the cell membrane, creating a Na+ gradient as well as an electrical potential. Electrons flow from NADH to quinone through the FAD in subunit F, the 2Fe-2S center, the FMN in subunit C, the FMN in subunit B, and finally riboflavin. The reduction of the FMN(C) to its anionic flavosemiquinone state is the first Na+-dependent process, suggesting that reduction of this site is linked to Na+ uptake. During the reduction reaction, two FMNs are transformed to their anionic flavosemiquinone in a single kinetic step. Subsequently, FMN(C) is converted to the flavohydroquinone, accounting for the single anionic flavosemiquinone radical in the fully reduced enzyme
-
-
?
NADH + H+ + ubiquinone + 2 Na+/in
NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + 2 Na+/in
NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + 2 Na+/in
NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + 2 Na+/in
NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + 2 Na+/in
NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + 2 Na+/in
NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + 2 Na+/in
NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + 2 Na+/in
NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + 2 Na+/in
NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + 2 Na+/in
NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + 2 Na+/in
NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + 2 Na+/in
NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + n Na+/in
NAD+ + ubiquinol + n Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + n Na+/in
NAD+ + ubiquinol + n Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + n Na+/in
NAD+ + ubiquinol + n Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + n Na+/in
NAD+ + ubiquinol + n Na+/out
A5F5X0
-
-
-
?
NADH + H+ + ubiquinone + n Na+/in
NAD+ + ubiquinol + n Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + n Na+/in
NAD+ + ubiquinol + n Na+/out
A6XUU9
-
-
-
?
NADH + H+ + ubiquinone + n Na+/in
NAD+ + ubiquinol + n Na+/out
-
-
-
-
?
NADH + H+ + ubiquinone + n Na+/in
NAD+ + ubiquinol + n Na+/out
-
Na+-NQR reduction is not limited by the rate of NADH binding
-
-
?
NADH + H+ + ubiquinone + n Na+/in
NAD+ + ubiquinol + n Na+/out
Q9RFV6
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
-
-
?
NADH + H+ + ubiquinone-1
NAD+ + ubiquinol-1
-
-
the enzyme catalyzes NADH-driven Na+ transport
-
-
?
NADH + H+ + ubiquinone-1
NAD+ + ubiquinol-1
Q9KPS1 and Q9KPS2 and A5F5Y7 and Q9X4Q8
the enzyme catalyzes NADH-driven Na+ transport
-
-
?
NADH + H+ + ubiquinone-1 + n Na+/in
NAD+ + ubiquinol-1 + n Na+/out
Q9X4Q8
-
-
-
?
NADH + H+ + ubiquinone-1 + n Na+/in
NAD+ + ubiquinol-1 + n Na+/out
Q9X4Q8
-
-
-
?
NADH + ubiquinone
?
-
the enzyme couples the exergonic oxidation of NADH with ubiquinone to the transport of Na+ ions from the inside of a bacterial cell to the periplasmic space
-
-
?
NADH + ubiquinone
?
-
the Na+ pump is coupled to the respiratory chain at the step of NADH:quinone oxidoreductase
-
-
-
thio-NADH + H+ + ubiquinone + 2 Na+/in
thio-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
thio-NADH + H+ + ubiquinone + 2 Na+/in
thio-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
thio-NADH + H+ + ubiquinone + 2 Na+/in
thio-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
thio-NADH + H+ + ubiquinone + 2 Na+/in
thio-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
thio-NADH + H+ + ubiquinone + 2 Na+/in
thio-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
thio-NADH + H+ + ubiquinone + 2 Na+/in
thio-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
thio-NADH + H+ + ubiquinone + 2 Na+/in
thio-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
thio-NADH + H+ + ubiquinone + 2 Na+/in
thio-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
thio-NADH + H+ + ubiquinone + 2 Na+/in
thio-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
thio-NADH + H+ + ubiquinone + 2 Na+/in
thio-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
thio-NADH + H+ + ubiquinone + 2 Na+/in
thio-NAD+ + ubiquinol + 2 Na+/out
-
-
-
-
?
additional information
?
-
-
in addition to the quinone reductase reaction, the isolated enzyme can also catalyze the so-called NADH-dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexaammineruthenium (III), ferricyanide, etc.)
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction, the isolated enzyme can also catalyze the so-called NADH-dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexaammineruthenium (III), ferricyanide, etc.)
-
-
-
additional information
?
-
-
construction of a double NDH-2/NDH-1-deficient strain. Sub-bacterial particles isolated from these strains oxidize NADH entirely via the corresponding Na+-NQR, which makes them a useful tool to study the catalytic properties of these enzymes
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction, the isolated enzyme can also catalyze the so-called NADH-dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexaammineruthenium (III), ferricyanide, etc.)
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction, the isolated enzyme can also catalyze the so-called NADH-dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexaammineruthenium (III), ferricyanide, etc.)
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction, the isolated enzyme can also catalyze the so-called NADH-dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexaammineruthenium (III), ferricyanide, etc.)
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinines. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction, the isolated enzyme can also catalyze the so-called NADH-dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexaammineruthenium (III), ferricyanide, etc.)
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction, the isolated enzyme can also catalyze the so-called NADH-dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexaammineruthenium (III), ferricyanide, etc.)
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction, the isolated enzyme can also catalyze the so-called NADH-dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexaammineruthenium (III), ferricyanide, etc.)
-
-
-
additional information
?
-
-
the enzyme is the entry point for electrons into the respiratory chain
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction, the isolated enzyme can also catalyze the so-called NADH-dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexaammineruthenium (III), ferricyanide, etc.)
-
-
-
additional information
?
-
-
construction of a NADH-dehydrogenase NDH-2-deficient strain. Sub-bacterial particles isolated from these strains oxidize NADH entirely via the corresponding Na+-NQR, which makes them a useful tool to study the catalytic properties of these enzymes
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction, the isolated enzyme can also catalyze the so-called NADH-dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexaammineruthenium (III), ferricyanide, etc.)
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction the isolated enzyme can also catalyze so-called NADH dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexammineruthenium(III), ferricyanide, etc.). Similarly to the transdehydrogenase activity, the NADH dehydrogenase activity does not depend on concentration of sodium ions, is inhibited by heavy metal ions, and is insensitive to 2-heptyl-4-hydroxyquinoline N-oxide and korormicin
-
-
-
additional information
?
-
-
in addition to the quinone reductase reaction, the isolated enzyme can also catalyze the so-called NADH-dehydrogenase reaction during interaction with soluble quinones. This activity includes a single-electron reduction of soluble quinones (menadione, Q0, Q1, etc.) or some other electron acceptors (hexaammineruthenium (III), ferricyanide, etc.)
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
putative arrangement of subunits and cofactors of the Na+-NQR
-
FAD
-
contains one molecule of covalently bound FAD, believed to be bound to subunit F; enzyme contains one molecule of noncovalently bound FAD
FAD
contains one noncovalently bound FAD; contains one noncovalently bound FAD
FAD
the electron transfer NADH -> FAD ->[2Fe-2S] in NqrF requires positioning of the FAD and the Fe-S cluster in close proximity in accordance with a structural model of the subunit
FAD
-
the enzyme contains four flavin cofactors. The two-electron reduction of the FAD located in the NqrF subunit is coupled with the uptake of only one H+. The one-electron reduction of neutral semiquinone of riboflavin and the formation of anion flavosemiquinone from the oxidized FMN bound to the NqrB subunit are not coupled to any proton uptake. The two sequential one-electron reductions of the FMN residue bound to the NqrC subunit show pH-independent formation of anion radical in the first step and the formation of fully reduced flavin coupled to the uptake of one H+ in the second step. All four flavins stays in the anionic form in the fully reduced enzyme
FAD
-
electrons flow from NADH to quinone through the FAD in subunit F, the 2Fe-2S center, the FMN in subunit C, the FMN in subunit B, and finally riboflavin. The reduction of the FMN(C) to its anionic flavosemiquinone state is the first Na+-dependent process, suggesting that reduction of this site is linked to Na+ uptake. During the reduction reaction, two FMNs are transformed to their anionic flavosemiquinone in a single kinetic step. Subsequently, FMN(C) is converted to the flavohydroquinone, accounting for the single anionic flavosemiquinone radical in the fully reduced enzyme
FAD
-
the NqrF subunit contains one FAD and a [2Fe–2S] cluster and catalyzes the initial oxidation of NADH
FAD
non-covalently bound in the NqrF subunit. Conserved residue C383 is involved in the hydride ion transport from NADH to FAD
flavin
-
contains a single extremely stable flavin semiquinone, which becomes deprotonated upon reduction of the enzyme
flavin
-
puriied NQR complex contains 11-12.5 nmol total flavins/mg protein
FMN
-
enzyme contains 2 molecules of covalently bound FMN; the enzyme contains two molecules of covalently bound FMN, covalently bound to subunits NqrB and NqrC
FMN
contains two covalently bound FMNs; contains two covalently bound FMNs
FMN
-
enzyme contains two covalently bound FMN‘s. A neutral FMN flavosemiquinone preexists in the oxidized enzyme, it is reduced to the fully reduced flavin by NADH. The other FMN moiety is initially oxidized, and is reduced to the anionic flavosemiquinone
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
FMN
-
the enzyme contains four flavin cofactors. The two-electron reduction of the FAD located in the NqrF subunit is coupled with the uptake of only one H+. The one-electron reduction of neutral semiquinone of riboflavin and the formation of anion flavosemiquinone from the oxidized FMN bound to the NqrB subunit are not coupled to any proton uptake. The two sequential one-electron reductions of the FMN residue bound to the NqrC subunit show pH-independent formation of anion radical in the first step and the formation of fully reduced flavin coupled to the uptake of one H+ in the second step. All four flavins stayed in the anionic form in the fully reduced enzyme
FMN
-
electrons flow from NADH to quinone through the FAD in subunit F, the 2Fe-2S center, the FMN in subunit C, the FMN in subunit B, and finally riboflavin. The reduction of the FMN(C) to its anionic flavosemiquinone state is the first Na+-dependent process, suggesting that reduction of this site is linked to Na+ uptake. During the reduction reaction, two FMNs are transformed to their anionic flavosemiquinone in a single kinetic step. Subsequently, FMN(C) is converted to the flavohydroquinone, accounting for the single anionic flavosemiquinone radical in the fully reduced enzyme
FMN
-
the flavin is linked to Thr-235 in the NqrB and Thr-223 in the NqrC subunits
FMN
-
subunits NqrB and NqrC contain covalently bound FMN, the wild type subunit NqrC contains approximately 1 mol of FMN per mol of protein
FMN
two covalently bound in subunits NqrB und NqrC, attached by phosphoester bonds to threonine residues
FMN
M7R347
the isoalloxazine moiety of the FMN residue is buried in a hydrophobic cavity and its pyrimidine ring is squeezed between hydrophobic amino acid residues while its benzene ring is extended from the protein surroundings. This structure of the flavin-binding pocket appears to provide flexibility of the benzene ring, which can help the FMN residue to take the bended conformation and to stabilize the one-electron reduced form of the prosthetic group, and may also lead to relatively weak noncovalent binding of the flavin
NADH
Q9KPS1 and Q9KPS2 and A5F5Y7 and Q9X4Q8
NQR-2 exhibits approximately 15% of the specific NADH dehydrogenase activity of NQR-1
NADH
-
-
NADH
-
-
392715, 659342, 671141, 674443, 674705, 696362, 698995, 699385, 710746, 711269, 711997, 712274, 713414, 725402, 725433, 725448, 725481, 725538, 725539
riboflavin
-
the enzyme contains four flavin cofactors. The two-electron reduction of the FAD located in the NqrF subunit is coupled with the uptake of only one H+. The one-electron reduction of neutral semiquinone of riboflavin and the formation of anion flavosemiquinone from the oxidized FMN bound to the NqrB subunit are not coupled to any proton uptake. The two sequential one-electron reductions of the FMN residue bound to the NqrC subunit show pH-independent formation of anion radical in the first step and the formation of fully reduced flavin coupled to the uptake of one H+ in the second step. All four flavins stays in the anionic form in the fully reduced enzyme
riboflavin
Q9KPS1 and Q9KPS2 and A5F5Y7 and Q9X4Q8
riboflavin detected in NQR-2 is bound to the NqrB or NqrC subunit
riboflavin
-
riboflavin is an active redox cofactor of Na+-NQR, giving rise to the neutral flavosemiquinone, it is likely to be the final electron carrier in the enzyme before the quinone
riboflavin
-
electrons flow from NADH to quinone through the FAD in subunit F, the 2Fe-2S center, the FMN in subunit C, the FMN in subunit B, and finally riboflavin. The reduction of the FMN(C) to its anionic flavosemiquinone state is the first Na+-dependent process, suggesting that reduction of this site is linked to Na+ uptake. During the reduction reaction, two FMNs are transformed to their anionic flavosemiquinone in a single kinetic step. Subsequently, FMN(C) is converted to the flavohydroquinone, accounting for the single anionic flavosemiquinone radical in the fully reduced enzyme
riboflavin
A6XUU9
noncovalently bound riboflavin in purified Na+-NQR is not liberated from FMN but represents an intrinsic component of the Na+-NQR complex
[2Fe-2S]-center
-
the NqrF subunit of the Na+-NQR complex harbors a [2Fe-2S] cluster which accepts electrons from the FAD cofactor
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
Fe2+
Iron
K+
-
acts as a nonessential activator, increasing the activity and affinity for sodium. Na+-NQR contains a regulatory site for K+
Li+
Na+
[2Fe-2S]
Fe
-
the enzyme contains 650-780 ng Fe per mg protein, which corresponds to 2.5-3.0 atoms of Fe per enzyme complex. The enzyme bears only the 2Fe-2S cluster as the sole metal-containing prosthetic group; the enzyme contains 650-780 ng Fe per mg protein, which corresponds to 2.5-3.0 atoms of Fe per enzyme complex. The enzyme bears only the 2Fe-2S cluster as the sole metal-containing prosthetic group
Fe
-
enzyme contains a 2Fe-2S center. Electrons flow from NADH to quinone through the FAD in subunit F, the 2Fe-2S center, the FMN in subunit C, the FMN in subunit B, and finally riboflavin. The reduction of the FMN(C) to its anionic flavosemiquinone state is the first Na+-dependent process, suggesting that reduction of this site is linked to Na+ uptake. During the reduction reaction, two FMNs are transformed to their anionic flavosemiquinone in a single kinetic step. Subsequently, FMN(C) is converted to the flavohydroquinone, accounting for the single anionic flavosemiquinone radical in the fully reduced enzyme; the enzyme contains one 2Fe-2S center, electrons flow from NADH to quinone through the FAD in subunit F, the 2Fe-2S center, the FMN in subunit C, the FMN in subunit B, and finally riboflavin. The reduction of the FMN(C) to its anionic flavosemiquinone state is the first Na+-dependent process, suggesting that reduction of this site is linked to Na+ uptake. During the reduction reaction, two FMNs are transformed to their anionic flavosemiquinone in a single kinetic step. Subsequently, FMN(C) is converted to the flavohydroquinone, accounting for the single anionic flavosemiquinone radical in the fully reduced enzyme
Fe
-
the NqrF subunit contains one FAD and a [2Fe–2S] cluster and catalyzes the initial oxidation of NADH. The Na+-NQR is proposed to increase the stability of NqrF' by stimulating the maturation of FeS centers
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
Iron
-
an Fe-S-cluster of the [2Fe-2S] type is involved in electron translocation
Iron
contains one 2Fe-2S center. Fout conserved cysteines, C70, C76, C79, and C111 in the subunit NqrF match the canonical 2Fe-2S motif
Li+
-
the wild-type enzyme is stimulated 3fold by lithium, while the mutants NqrBD397A and NqrB-D397K, that are completely insensitive to sodium, are also not stimulated by lithium. The activities of the mutants NqrBD397C, NqrB-D397E, NqrB-D397N and NqrB-D397S are stimulated by lithium, and interestingly the fraction of stimulationis greater for lithium compared to sodium
Na+
-
specific requirement for sodium ions, even in the absence of sodium ions Na+-NQR is unable to translocate protons
Na+
-
sodium ions are indispensable components of the Na+-NQR-catalyzed reaction, therefore its rate depends on concentration of Na+ and the reaction virtually does not occur in media depleted in this ion
Na+
-
specific requirement for sodium ions, even in the absence of sodium ions Na+-NQR is unable to translocate protons
Na+
-
the NADH oxidase activity of NQR is greatly stimulated by NaC1, but not by KCI. The concentration of Na+ required for half-maximum activation is 5.5 mM. When menadione is used as the electron acceptor, the activity is stimulated about 2fold by the addition of either 200 mM KCl or NaCl, but no specific requirement for Na+ is observed in this reaction
Na+
-
sodium ions are indispensable components of the Na+-NQR-catalyzed reaction, therefore its rate depends on concentration of Na+ and the reaction virtually does not occur in media depleted in this ion
Na+
-
specific requirement for sodium ions, even in the absence of sodium ions Na+-NQR is unable to translocate protons
Na+
-
sodium ions are indispensable components of the Na+-NQR-catalyzed reaction, therefore its rate depends on concentration of Na+ and the reaction virtually does not occur in media depleted in this ion
Na+
-
specific requirement for sodium ions, even in the absence of sodium ions Na+-NQR is unable to translocate protons
Na+
-
sodium ions are indispensable components of the Na+-NQR-catalyzed reaction, therefore its rate depends on concentration of Na+ and the reaction virtually does not occur in media depleted in this ion
Na+
-
specific requirement for sodium ions, even in the absence of sodium ions Na+-NQR is unable to translocate protons
Na+
-
sodium ions are indispensable components of the Na+-NQR-catalyzed reaction, therefore its rate depends on concentration of Na+ and the reaction virtually does not occur in media depleted in this ion
Na+
-
specific requirement for sodium ions, even in the absence of sodium ions Na+-NQR is unable to translocate protons
Na+
-
sodium ions are indispensable components of the Na+-NQR-catalyzed reaction, therefore its rate depends on concentration of Na+ and the reaction virtually does not occur in media depleted in this ion
Na+
-
specific requirement for sodium ions, even in the absence of sodium ions Na+-NQR is unable to translocate protons
Na+
-
sodium ions are indispensable components of the Na+-NQR-catalyzed reaction, therefore its rate depends on concentration of Na+ and the reaction virtually does not occur in media depleted in this ion
Na+
-
sodium ions are indispensable components of the Na+-NQR-catalyzed reaction, therefore its rate depends on concentration of Na+ and the reaction virtually does not occur in media depleted in this ion
Na+
-
specific requirement for sodium ions, even in the absence of sodium ions Na+-NQR is unable to translocate protons
Na+
-
the reaction catalyzed by subunits NqrA to NqrE to produce ubiquinol specifically requires Na+ for activity. The reaction catalyzed by subunit NqrF which reduces ubiquinone by a one-electron transfer pathway to produce ubisemiquinone radical does not require Na+ for activity
Na+
-
sodium ions are indispensable components of the Na+-NQR-catalyzed reaction, therefore its rate depends on concentration of Na+ and the reaction virtually does not occur in media depleted in this ion
Na+
-
specific requirement for sodium ions, even in the absence of sodium ions Na+-NQR is unable to translocate protons
Na+
-
environmental Na+ can stimulate ubisemiquinone formation by the Na+-NQR and hereby enhances the production of reactive oxygen species formed during the autoxidation of reduced quinines, increasing the Na+ concentration from below 0.1 mM to 25 mM results in a 3fold stimulation of activity of the purified enzyme
Na+
-
the wild-type enzyme's physiologic activity is stimulated 8fold in the presence of saturating amounts of sodium
Na+
-
the Na+-dependent step of the Na+-translocating NADH:ubiquinone oxidoreductase is located between the noncovalently bound FAD and the covalently bound FMN
Na+
-
sodium ions are indispensable components of the Na+-NQR-catalyzed reaction, therefore its rate depends on concentration of Na+ and the reaction virtually does not occur in media depleted in this ion
Na+
-
specific requirement for sodium ions, even in the absence of sodium ions Na+-NQR is unable to translocate protons
Na+
-
sodium ions are indispensable components of the Na+-NQR-catalyzed reaction, therefore its rate depends on concentration of Na+ and the reaction virtually does not occur in media depleted in this ion
Na+
-
specific requirement for sodium ions, even in the absence of sodium ions Na+-NQR is unable to translocate protons
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
NADH
-
incubation of the aerobic enzyme with NADH in the absence of an electron acceptor, the enzyme is destroyed with a half-inactivation time of about 2 min
2-n-heptyl-4-hydroxyquinoline N-oxide
-
inhibited by micromolar concentrations. In contrast to the corresponding enzymes from Vibrio harveyi and Klebsiella pneumoniae, the enzyme from Azotobacter vinelandii is resistant to low 2-n-heptyl-4-hydroxyquinoline N-oxide concentrations
Ag+
-
in the presence of Ag+, rates of NADH oxidation by membranes from the parent Vibrio cholera strain decrease to 14% (0.001 mM Ag+) of the activity observed in the absence of the inhibitor
Ag+
; the enzyme is specifically inhibited by low concentrations of silver ions
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
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
diphenyliodonium
-
0.05 mM, rapid inhibition, modifies the noncovalently bound FAD of the enzyme
korormicin
-
specifically inhibits Na+-NQR at the level of its interaction with ubiquinone
korormicin
-
specifically inhibits Na+-NQR at the level of its interaction with ubiquinone
korormicin
-
specifically inhibits Na+-NQR at the level of its interaction with ubiquinone
korormicin
-
specifically inhibits Na+-NQR at the level of its interaction with ubiquinone
korormicin
-
specifically inhibits Na+-NQR at the level of its interaction with ubiquinone
korormicin
-
specifically inhibits Na+-NQR at the level of its interaction with ubiquinone
korormicin
-
specifically inhibits Na+-NQR at the level of its interaction with ubiquinone
korormicin
-
specifically inhibits Na+-NQR at the level of its interaction with ubiquinone
korormicin
-
specifically inhibits Na+-NQR at the level of its interaction with ubiquinone
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
korormicin
-
specifically inhibits Na+-NQR at the level of its interaction with ubiquinone
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
additional information
-
the enzyme is fully resistant to either Ag+ or N-ethylmaleimide
-
additional information
-
Na+-NQR from Azotobacter vinelandii is not sensitive to low 2-n-heptyl-4-hydroxyquinoline-N-oxide concentrations
-
additional information
-
korormicin has no effect on the enzyme from Haemophilus influenza
-
additional information
-
the enzyme is fully resistant to either Ag+ or N-ethylmaleimide
-
additional information
-
Na+-NQR from Klebsiella pneumoniae is fully resistant to either Ag+ or N-ethylmaleimide
-
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
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
enzyme contains a 2Fe-2S center. Electrons flow from NADH to quinone through the FAD in subunit F, the 2Fe-2S center, the FMN in subunit C, the FMN in subunit B, and finally riboflavin. The reduction of the FMN(C) to its anionic flavosemiquinone state is the first Na+-dependent process, suggesting that reduction of this site is linked to Na+ uptake. During the reduction reaction, two FMNs are transformed to their anionic flavosemiquinone in a single kinetic step. Subsequently, FMN(C) is converted to the flavohydroquinone, accounting for the single anionic flavosemiquinone radical in the fully reduced enzyme
FMN
-
enzyme contains a 2Fe-2S center. Electrons flow from NADH to quinone through the FAD in subunit F, the 2Fe-2S center, the FMN in subunit C, the FMN in subunit B, and finally riboflavin. The reduction of the FMN(C) to its anionic flavosemiquinone state is the first Na+-dependent process, suggesting that reduction of this site is linked to Na+ uptake. During the reduction reaction, two FMNs are transformed to their anionic flavosemiquinone in a single kinetic step. Subsequently, FMN(C) is converted to the flavohydroquinone, accounting for the single anionic flavosemiquinone radical in the fully reduced enzyme
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.4
n Li+/in
-
mutant D397N, pH 8.0, temperature not specified in the publication
2.5
n Li+/in
-
mutant D397E, pH 8.0, temperature not specified in the publication
2.7
n Li+/in
-
mutant D397C, presence of 2-mercaptoethanol, pH 8.0, temperature not specified in the publication
2.9
n Li+/in
-
mutant D397S, pH 8.0, temperature not specified in the publication
3.5
n Li+/in
-
wild-type, pH 8.0, temperature not specified in the publication
0.25
n Na+/in
-
mutant D397C, presence of 2-mercaptoethanol, pH 8.0, temperature not specified in the publication
0.7
n Na+/in
-
mutant D397C, pH 8.0, temperature not specified in the publication
1.8
n Na+/in
-
mutant D397E, pH 8.0, temperature not specified in the publication
2.5
n Na+/in
-
wild-type, pH 8.0, temperature not specified in the publication
2.8
n Na+/in
-
mutant D397S, pH 8.0, temperature not specified in the publication
3.1
n Na+/in
-
mutant D397N, pH 8.0, temperature not specified in the publication
0.0025
ubiquinone
-
wild-type enzyme, pH 8.0, temperature not specified in the publication
0.0088
ubiquinone
-
mutant G141L, pH 8.0, temperature not specified in the publication
0.015
ubiquinone
-
mutant G141A, pH 8.0, temperature not specified in the publication
0.0234
ubiquinone
-
mutant G141V, pH 8.0, temperature not specified in the publication
0.1
ubiquinone
-
above, mutant G140A, pH 8.0, temperature not specified in the publication
0.0025
ubiquinone-1
-
wild-type, pH 8.0, temperature not specified in the publication
0.0088
ubiquinone-1
-
mutant G141L, pH 8.0, temperature not specified in the publication
0.015
ubiquinone-1
-
mutant G141A, pH 8.0, temperature not specified in the publication
0.0234
ubiquinone-1
-
mutant G141V, pH 8.0, temperature not specified in the publication
0.1
ubiquinone-1
-
mutant G140A, pH 8.0, temperature not specified in the publication; mutant G140L, pH 8.0, temperature not specified in the publication
additional information
additional information
Kmapp(Na+) is: 1.1 mM for wild-type enzyme, 13.1 mM for subunit E mutant E95A; Kmapp(Na+) is: 1.1 mM for wild-type enzyme, 1.4 mM for subunit D mutant D88L, 9.3 mM for subunit D mutant D133A; Kmapp(Na+) is: 1.1 mM for wild-type enzyme, 2.1 mM for subunit B mutant E28A, 4.2 mM for subunit B mutant E144L, 0.9 mM for subunit B mutant D346A, above 100 mM for subunit B mutant D397A
-
additional information
additional information
-
Km(Na+) is 0.0001 mM
-
additional information
additional information
-
steady-state and transient kinetics, together with equilibrium binding measurements to define the number of cation-binding sites and characterize their roles in the enzyme, overview
-
additional information
additional information
-
Michaelis-Menten kinetics in the absence of 2,5-dibromo-3-methyl-6-isopropyl-4-benzoquinone
-
additional information
additional information
-
in wild-type Na+-NQR, the sodium dependence of the steady state turnover follows a Michaelis-Menten behavior, while the kinetics of the NqrB-D397A mutant show an unsaturable behavior for sodium. Kinetic mechanism, modeling, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
100
n Li+/in
Vibrio cholerae
-
mutant D397N, pH 8.0, temperature not specified in the publication
110
n Li+/in
Vibrio cholerae
-
mutant D397E, pH 8.0, temperature not specified in the publication
115
n Li+/in
Vibrio cholerae
-
mutant D397C, presence of 2-mercaptoethanol, pH 8.0, temperature not specified in the publication
124
n Li+/in
Vibrio cholerae
-
mutant D397S, pH 8.0, temperature not specified in the publication
180
n Li+/in
Vibrio cholerae
-
wild-type, pH 8.0, temperature not specified in the publication
115
n Na+/in
Vibrio cholerae
-
mutant D397S, pH 8.0, temperature not specified in the publication
127
n Na+/in
Vibrio cholerae
-
mutant D397E, pH 8.0, temperature not specified in the publication; mutant D397N, pH 8.0, temperature not specified in the publication
170
n Na+/in
Vibrio cholerae
-
mutant D397C, pH 8.0, temperature not specified in the publication; mutant D397C, presence of 2-mercaptoethanol, pH 8.0, temperature not specified in the publication
500
n Na+/in
Vibrio cholerae
-
wild-type, pH 8.0, temperature not specified in the publication
487.7
NADH
Vibrio cholerae
-
mutant D397K, pH 8.0, temperature not specified in the publication, presence of 100 mM Na+
495.4
NADH
Vibrio cholerae
-
mutant D397C, presence of 2-mercaptoethanol, pH 8.0, temperature not specified in the publication
501.4
NADH
Vibrio cholerae
-
mutant D397C, pH 8.0, temperature not specified in the publication
511.7
NADH
Vibrio cholerae
-
mutant D397S, pH 8.0, temperature not specified in the publication
521.9
NADH
Vibrio cholerae
-
mutant D397K, pH 8.0, temperature not specified in the publication, presence of 100 mM Li+
544.7
NADH
Vibrio cholerae
-
mutant D397E, pH 8.0, temperature not specified in the publication
560.8
NADH
Vibrio cholerae
-
mutant D397N, pH 8.0, temperature not specified in the publication
580.2
NADH
Vibrio cholerae
-
mutant D397A, pH 8.0, temperature not specified in the publication, presence of 100 mM Na+
587.2
NADH
Vibrio cholerae
-
wild-type, pH 8.0, temperature not specified in the publication, presence of 100 mM Li+
600.1
NADH
Vibrio cholerae
-
wild-type, pH 8.0, temperature not specified in the publication, presence of 100 mM Na+
603.2
NADH
Vibrio cholerae
-
mutant D397S, pH 8.0, temperature not specified in the publication, presence of 100 mM Li+
622.2
NADH
Vibrio cholerae
-
mutant D397A, pH 8.0, temperature not specified in the publication
629.8
NADH
Vibrio cholerae
-
mutant D397A, pH 8.0, temperature not specified in the publication, presence of 100 mM Li+
656.6
NADH
Vibrio cholerae
-
mutant D397C, pH 8.0, temperature not specified in the publication, presence of 100 mM Na+
660.4
NADH
Vibrio cholerae
-
mutant D397N, pH 8.0, temperature not specified in the publication, presence of 100 mM Li+
662.9
NADH
Vibrio cholerae
-
mutant D397S, pH 8.0, temperature not specified in the publication, presence of 100 mM Na+
673.7
NADH
Vibrio cholerae
-
mutant D397E, pH 8.0, temperature not specified in the publication, presence of 100 mM Na+
681.6
NADH
Vibrio cholerae
-
mutant D397N, pH 8.0, temperature not specified in the publication, presence of 100 mM Na+
690.9
NADH
Vibrio cholerae
-
mutant D397C, pH 8.0, temperature not specified in the publication, presence of 100 mM Li+
694.6
NADH
Vibrio cholerae
-
mutant D397C, presence of 2-mercaptoethanol, pH 8.0, temperature not specified in the publication, presence of 100 mM Na+
695.4
NADH
Vibrio cholerae
-
mutant D397E, pH 8.0, temperature not specified in the publication, presence of 100 mM Li+
696.7
NADH
Vibrio cholerae
-
mutant D397C, presence of 2-mercaptoethanol, pH 8.0, temperature not specified in the publication, presence of 100 mM Li+
5199
NADH
Vibrio cholerae
-
mutant D397K, pH 8.0, temperature not specified in the publication
200
ubiquinone
Vibrio cholerae
-
mutant G140A, pH 8.0, temperature not specified in the publication
388
ubiquinone
Vibrio cholerae
-
mutant G141V, pH 8.0, temperature not specified in the publication
425
ubiquinone
Vibrio cholerae
-
mutant G141A, pH 8.0, temperature not specified in the publication
463
ubiquinone
Vibrio cholerae
-
mutant G141L, pH 8.0, temperature not specified in the publication
525
ubiquinone
Vibrio cholerae
-
wild-type enzyme, pH 8.0, temperature not specified in the publication
57.7
ubiquinone-1
Vibrio cholerae
-
mutant D397S, pH 8.0, temperature not specified in the publication
58.8
ubiquinone-1
Vibrio cholerae
-
mutant D397K, pH 8.0, temperature not specified in the publication, presence of 100 mM Na+
59.7
ubiquinone-1
Vibrio cholerae
-
mutant D397N, pH 8.0, temperature not specified in the publication
59.8
ubiquinone-1
Vibrio cholerae
-
mutant D397K, pH 8.0, temperature not specified in the publication, presence of 100 mM Li+
61.3
ubiquinone-1
Vibrio cholerae
-
mutant D397K, pH 8.0, temperature not specified in the publication
61.9
ubiquinone-1
Vibrio cholerae
-
mutant D397C, presence of 2-mercaptoethanol, pH 8.0, temperature not specified in the publication
65.7
ubiquinone-1
Vibrio cholerae
-
mutant D397C, pH 8.0, temperature not specified in the publication
66
ubiquinone-1
Vibrio cholerae
-
mutant D397E, pH 8.0, temperature not specified in the publication
66.3
ubiquinone-1
Vibrio cholerae
-
wild-type, pH 8.0, temperature not specified in the publication
70.6
ubiquinone-1
Vibrio cholerae
-
mutant D397A, pH 8.0, temperature not specified in the publication, presence of 100 mM Na+
72.3
ubiquinone-1
Vibrio cholerae
-
mutant D397A, pH 8.0, temperature not specified in the publication; mutant D397A, pH 8.0, temperature not specified in the publication, presence of 100 mM Li+
80.7
ubiquinone-1
Vibrio cholerae
-
mutant D397S, pH 8.0, temperature not specified in the publication, presence of 100 mM Li+
95.5
ubiquinone-1
Vibrio cholerae
-
mutant D397N, pH 8.0, temperature not specified in the publication, presence of 100 mM Li+
96.4
ubiquinone-1
Vibrio cholerae
-
mutant D397E, pH 8.0, temperature not specified in the publication, presence of 100 mM Li+
101.3
ubiquinone-1
Vibrio cholerae
-
mutant D397S, pH 8.0, temperature not specified in the publication, presence of 100 mM Na+
102.9
ubiquinone-1
Vibrio cholerae
-
mutant D397C, pH 8.0, temperature not specified in the publication, presence of 100 mM Li+
110.6
ubiquinone-1
Vibrio cholerae
-
mutant D397C, presence of 2-mercaptoethanol, pH 8.0, temperature not specified in the publication, presence of 100 mM Li+
122.9
ubiquinone-1
Vibrio cholerae
-
mutant D397N, pH 8.0, temperature not specified in the publication, presence of 100 mM Na+
129.6
ubiquinone-1
Vibrio cholerae
-
mutant D397E, pH 8.0, temperature not specified in the publication, presence of 100 mM Na+
152.9
ubiquinone-1
Vibrio cholerae
-
mutant D397C, pH 8.0, temperature not specified in the publication, presence of 100 mM Na+
162.2
ubiquinone-1
Vibrio cholerae
-
mutant D397C, presence of 2-mercaptoethanol, pH 8.0, temperature not specified in the publication, presence of 100 mM Na+
200
ubiquinone-1
Vibrio cholerae
-
mutant G140A, pH 8.0, temperature not specified in the publication; mutant G140L, pH 8.0, temperature not specified in the publication
205.5
ubiquinone-1
Vibrio cholerae
-
wild-type, pH 8.0, temperature not specified in the publication, presence of 100 mM Li+
388
ubiquinone-1
Vibrio cholerae
-
mutant G141V, pH 8.0, temperature not specified in the publication
425
ubiquinone-1
Vibrio cholerae
-
mutant G141A, pH 8.0, temperature not specified in the publication
463
ubiquinone-1
Vibrio cholerae
-
mutant G141L, pH 8.0, temperature not specified in the publication
525
ubiquinone-1
Vibrio cholerae
-
wild-type, pH 8.0, temperature not specified in the publication
528.5
ubiquinone-1
Vibrio cholerae
-
wild-type, pH 8.0, temperature not specified in the publication, presence of 100 mM Na+
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
525
ubiquinone-1
Vibrio cholerae
-
mutant G140A, pH 8.0, temperature not specified in the publication; mutant G140L, pH 8.0, temperature not specified in the publication; mutant G141A, pH 8.0, temperature not specified in the publication; mutant G141L, pH 8.0, temperature not specified in the publication; mutant G141V, pH 8.0, temperature not specified in the publication; wild-type, pH 8.0, temperature not specified in the publication
1150
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0005
2-n-heptyl-4-hydroxyquinoline N-oxide
-
wild-type enzyme, pH 8.0, temperature not specified in the publication; wild-type, pH 8.0, temperature not specified in the publication
0.0012
2-n-heptyl-4-hydroxyquinoline N-oxide
-
mutant G141V, pH 8.0, temperature not specified in the publication; mutant G141V, pH 8.0, temperature not specified in the publication
0.0075
2-n-heptyl-4-hydroxyquinoline N-oxide
-
above, mutant G140A, pH 8.0, temperature not specified in the publication; mutant G140A, pH 8.0, temperature not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.6
subunit Nqr6, isoelectric focusing
4.8
subunit Nqr3, isoelectric focusing
5.4
subunit Nqr1, isoelectric focusing
7
subunit Nqr5, isoelectric focusing
8.2
subunit Nqr2, isoelectric focusing
9.2
subunit Nqr4, isoelectric focusing
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
19000
1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE
20000
1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE
21500
21540
1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence
22470
1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence
22602
-
1 * 48622 + 1 * 46809 + 1 * 27672 + 1 * 22602, subunits NqrA, NqrB, NqrC and NqrD, calculated from amino acid sequence
22700
27500
27571
1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence
27619
Q9KPS1 and Q9KPS2 and A5F5Y7 and Q9X4Q8
1 * 48624 (NqrA) + 1 * 45357 (NqrB) + 1 * 27619 (NqrC) + 1 * 45067 (Nqrf), NQR-2 is the smaller subcomplex of the Na+-NQR consists of NqrA-His, NqrF, NqrB and NqrCNQR-2 but lacks the highly hydrophobic NqrD and NqrE subunit, calculated from sequence
27672
-
1 * 48622 + 1 * 46809 + 1 * 27672 + 1 * 22602, subunits NqrA, NqrB, NqrC and NqrD, calculated from amino acid sequence
32000
45067
Q9KPS1 and Q9KPS2 and A5F5Y7 and Q9X4Q8
1 * 48624 (NqrA) + 1 * 45357 (NqrB) + 1 * 27619 (NqrC) + 1 * 45067 (Nqrf), NQR-2 is the smaller subcomplex of the Na+-NQR consists of NqrA-His, NqrF, NqrB and NqrCNQR-2 but lacks the highly hydrophobic NqrD and NqrE subunit, calculated from sequence
45200
45210
1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence
45274
1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence
45357
Q9KPS1 and Q9KPS2 and A5F5Y7 and Q9X4Q8
1 * 48624 (NqrA) + 1 * 45357 (NqrB) + 1 * 27619 (NqrC) + 1 * 45067 (Nqrf), NQR-2 is the smaller subcomplex of the Na+-NQR consists of NqrA-His, NqrF, NqrB and NqrCNQR-2 but lacks the highly hydrophobic NqrD and NqrE subunit, calculated from sequence
45400
46000
1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE
46809
-
1 * 48622 + 1 * 46809 + 1 * 27672 + 1 * 22602, subunits NqrA, NqrB, NqrC and NqrD, calculated from amino acid sequence
48400
48622
48624
Q9KPS1 and Q9KPS2 and A5F5Y7 and Q9X4Q8
1 * 48624 (NqrA) + 1 * 45357 (NqrB) + 1 * 27619 (NqrC) + 1 * 45067 (Nqrf), NQR-2 is the smaller subcomplex of the Na+-NQR consists of NqrA-His, NqrF, NqrB and NqrCNQR-2 but lacks the highly hydrophobic NqrD and NqrE subunit, calculated from sequence
50000
1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE
110000
Q9KPS1 and Q9KPS2 and A5F5Y7 and Q9X4Q8
NQR-2 is the smaller subcomplex of the Na+-NQR consists of NqrA-His, NqrF, NqrB and NqrCNQR-2 but lacks the highly hydrophobic NqrD and NqrE subunit, gel filtration
360000
-
gel filtration; it is likely that the protein is a monomer, calculated molecular mass of 215000 Da with bound detergent, gel filtration
21500
-
1 * 48400 + 1 * 45400 + 1 * 27500 + 1 * 22700 + 1 * 21500 + 1 * 45200, calculated from amino acid sequence
22700
-
1 * 48400 + 1 * 45400 + 1 * 27500 + 1 * 22700 + 1 * 21500 + 1 * 45200, calculated from amino acid sequence
27500
-
1 * 48400 + 1 * 45400 + 1 * 27500 + 1 * 22700 + 1 * 21500 + 1 * 45200, calculated from amino acid sequence
32000
1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE
45200
-
1 * 48400 + 1 * 45400 + 1 * 27500 + 1 * 22700 + 1 * 21500 + 1 * 45200, calculated from amino acid sequence
45400
-
1 * 48400 + 1 * 45400 + 1 * 27500 + 1 * 22700 + 1 * 21500 + 1 * 45200, calculated from amino acid sequence
48400
-
1 * 48400 + 1 * 45400 + 1 * 27500 + 1 * 22700 + 1 * 21500 + 1 * 45200, calculated from amino acid sequence
48622
-
1 * 48622 + 1 * 46809 + 1 * 27672 + 1 * 22602, subunits NqrA, NqrB, NqrC and NqrD, calculated from amino acid sequence
48622
1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterohexamer
heterotetramer
hexamer
monomer
tetramer
Q9KPS1 and Q9KPS2 and A5F5Y7 and Q9X4Q8
1 * 48624 (NqrA) + 1 * 45357 (NqrB) + 1 * 27619 (NqrC) + 1 * 45067 (Nqrf), NQR-2 is the smaller subcomplex of the Na+-NQR consists of NqrA-His, NqrF, NqrB and NqrCNQR-2 but lacks the highly hydrophobic NqrD and NqrE subunit, calculated from sequence
additional information
heterohexamer
1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 48622 + 1 * 45210 + 1 * 27571 + 1 * 22470 + 1 * 21540 + 1 * 45274, calculated from amino acid sequence; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE; 1 * 50000 + 1 * 30000-35000 + 1 * 32000 + 1 * 20000 + 1 * 19000 + 1 * 46000, SDS-PAGE
heterohexamer
-
Na+-NQR is a heterohexameric complex consisting of six different protein subunits (NqrA-NqrF)
heterohexamer
-
1 * 48400 + 1 * 45400 + 1 * 27500 + 1 * 22700 + 1 * 21500 + 1 * 45200
heterohexamer
-
1 * 48400 + 1 * 45400 + 1 * 27500 + 1 * 22700 + 1 * 21500 + 1 * 45200, calculated from amino acid sequence
heterotetramer
-
1 * 48622 + 1 * 46809 + 1 * 27672 + 1 * 22602, subunits NqrA, NqrB, NqrC and NqrD, calculated from amino acid sequence
heterotetramer
-
1 * 48622 + 1 * 46809 + 1 * 27672 + 1 * 22602, subunits NqrA, NqrB, NqrC and NqrD, calculated from amino acid sequence
-
hexamer
-
-
1 * 48624 (NqrA) + 1 * 45357 (NqrB) + 1 * 27619 (NqrC) + 1 * 22837 (NqrD) + 1 * 21470 (NqrE) + 1 * 45067 (Nqrf), one copy of each Nqr subunit is present in the Na+-NQR complex and a theoretical molecular of 212000 Da is calculated for the complex. Taking into account the additional 50-76 kDa of a n-dodecyl beta-D-maltoside micelle which shields the hydrophobic part of the complex from the polar solvent, it is conluded that NQR-1 complex mainly consists of monomeric Na+-NQR, calculated from sequence
hexamer
the NqrF subunit harbors the active site of NADH oxidation and acts as a converter between the hydride donor NADH and subsequent one-electron reaction steps in the Na+-translocating NADH:quinone oxidoreductase complex
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
additional information
-
contains 14 central subunits and 32 accessory subunits
additional information
-
contains 14 central subunits and 32 accessory subunits
additional information
-
contains 14 central subunits and 32 accessory subunits
additional information
-
contains 14 central subunits and 32 accessory subunits
additional information
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contains 14 central subunits and 32 accessory subunits
additional information
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contains 14 central subunits and 32 accessory subunits
additional information
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contains 14 central subunits and 32 accessory subunits
additional information
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contains 14 central subunits and 32 accessory subunits
additional information
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contains 14 central subunits and 32 accessory subunits
additional information
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contains 14 central subunits and 32 accessory subunits
additional information
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the enzyme consists of three different hydrophilic and probably three different hydrophobic subunits
additional information
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putative arrangement of subunits and cofactors of the Na+-NQR
additional information
structural analysis of the NqrF subunit, overview
additional information
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contains 14 central subunits and 32 accessory subunits
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 40 mM KSCN, 21.0% PEG 2000 MME, 100 mM Tris acetate pH 8.5 and 8% (v/v) 1-propanol, cofactors such as FAD, riboflavin or NADH are not added during crystallization
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holo-enzyme, to 1.56 A resolution. The isoalloxazine moiety of the FMN residue is buried in a hydrophobic cavity and its pyrimidine ring is squeezed between hydrophobic amino acid residues while its benzene ring is extended from the protein surroundings. This structure of the flavin-binding pocket appears to provide flexibility of the benzene ring, which can help the FMN residue to take the bended conformation and to stabilize the one-electron reduced form of the prosthetic group, and may also lead to relatively weak noncovalent binding of the flavin
M7R347
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE Sephacel column chromatography, TSK-gel DEAE-5PW column chromatography, and Superdex 200 gel filtration; DEAE Sephacel column chromatography, TSK-gel DEAE-5PW column chromatography, and Superdex 200 gel filtration; DEAE Sephacel column chromatography, TSK-gel DEAE-5PW column chromatography, and Superdex 200 gel filtration; DEAE Sephacel column chromatography, TSK-gel DEAE-5PW column chromatography, and Superdex 200 gel filtration; DEAE Sephacel column chromatography, TSK-gel DEAE-5PW column chromatography, and Superdex 200 gel filtration; DEAE Sephacel column chromatography, TSK-gel DEAE-5PW column chromatography, and Superdex 200 gel filtration
Fractogel DEAE-650(S) column chromatography and Source 15Q Superformance column chromatography
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His6-tagged wild-type and mutant forms of the Na+-NQR from Vibrio cholerae mutant strain DELTAnqr by nickel affinity chromatography and gel filtration
A6XUU9
Ni-NTA column chromatography
partially purified by DEAE Sepharose column chromatography and preparative gel electrophoresis
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recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by affinity chromatography
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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
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recombinant N-terminally His6-tagged monomeric large subunit NqrA from Vibrio cholerae strain O395 N1 DELTAnqr membranes by ultracentrifugation, nickel affinity chromatography, and gel filtration in the presence of 0.05% w/v n-dodecyl-beta-D-maltoside
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned under the regulation of the PBAD promoter and expressed in Vibrio cholera; cloned under the regulation of the P(BAD) promoter, successfully expressed in Vibrio cholerae
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expression of full-length enzyme and N-terminally His6-tagged large subunit NqrA in Vibrio cholerae strain O395 N1 DELTAnqr
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expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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expression of N-terminally His6-tagged full-length enzyme and large subunit NqrA in Escherichia coli strain BL21(DE3)
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hexahistidine-tagged Na+-NQR is expressed in Vibrio cholerae strain DELTAnqr lacking expression of the NQR complex
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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
subunit NqrC is expressed in Vibrio cholerae and in Escherichia coli TOP10 cells. Subunit NqrB expression is toxic for Vibrio cholerae
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wild-type and mutant forms of the Na+-NQR from Vibrio cholerae as recombinant proteins containing a His6-tag at the N-terminus of subunit NqrA in an enzyme-deficient mutant strain DELTAnqr of Vibrio cholerae
A6XUU9
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C111A
2Fe-2S center mutant with severely reduced activity using ubiquinone-1 and NADH as substrates. NADH:ferricyanide oxidoreduction activity remains unchanged compared to the wild type enzyme; 3% of the NADH:ubiquinone-1 oxidoreductase activity compared to wild-type enzyme
C112I
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the substitutions of the conserved cysteine residue in NqrD blocks the Na+-dependent and HQNO-sensitive quinone reductase activity of the enzyme, being without effect on the interaction of the enzyme with reduced nicotinamide hypoxanthine dinucleotide and menadione. The substitution of the conserved cysteine residues results in inability of covalently bound flavins to stabilize flavosemiquinone states, i.e. lead to incorrect folding of the NQR complex
C120G
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the substitutions of the conserved cysteine residue in NqrE subunit of the enzyme blocks the Na+-dependent and HQNO-sensitive quinone reductase activity of the enzyme, being without effect on the interaction of the enzyme with reduced nicotinamide hypoxanthine dinucleotide and menadione. The substitution of the conserved cysteine residues results in inability of covalently bound flavins to stabilize flavosemiquinone states, i.e. lead to incorrect folding of the NQR complex
C26G
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the substitutions of the conserved cysteine residue in NqrE subunits of the enzyme blocks the Na+-dependent and HQNO-sensitive quinone reductase activity of the enzyme, being without effect on the interaction of the enzyme with reduced nicotinamide hypoxanthine dinucleotide and menadione. The substitution of the conserved cysteine residues results in inability of covalently bound flavins to stabilize flavosemiquinone states, i.e. lead to incorrect folding of the NQR complex
C29A
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the substitutions of the conserved cysteine residue in NqrD subunit of the enzyme blocks the Na+-dependent and HQNO-sensitive quinone reductase activity of the enzyme, being without effect on the interaction of the enzyme with reduced nicotinamide hypoxanthine dinucleotide and menadione. The substitution of the conserved cysteine residues results in inability of covalently bound flavins to stabilize flavosemiquinone states, i.e. lead to incorrect folding of the NQR complex
C70A
2Fe-2S center mutant with severely reduced activity using ubiquinone-1 and NADH as substrates, the amount of FAD in the C70A mutant is essentially the same as in the wild type. NADH:ferricyanide oxidoreduction activity remains unchanged compared to the wild type enzyme; 3% of the NADH:ubiquinone-1 oxidoreductase activity compared to wild-type enzyme
C76A
C79A
2Fe-2S center mutant with severely reduced activity using ubiquinone-1 and NADH as substrates. NADH:ferricyanide oxidoreduction activity remains unchanged compared to the wild type enzyme; 3% of the NADH:ubiquinone-1 oxidoreductase activity compared to wild-type enzyme
D133A
the mutant enzyme in which sodium stimulation of sodium-dependent quinone reductase activity activity is lowered significantly but not eliminated, produces diminished levels of sodium pumping activity
D346A
D397A
D397C
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mutant is stimulated by Li+. Mutation results in negative cooperativity; site-directed mutagenesis of subunit NqrB residue, part of the sodium binding site,; site-directed mutagenesis of subunit NqrB residue, part of the sodium binding site, the mutation that eliminates half of the negative charge, is stimulated only 2.6fold by sodium
D397E
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mutant is stimulated by Li+. Km value is not affected. Mutant contains approximately the same conformational flexibility as the wild type enzyme and is able to undergo a series of conformational changes induced by the redox reaction and by the addition of different cations; site-directed mutagenesis of subunit NqrB residue, part of the sodium binding site,
D397K
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mutant is completely insensitive to sodium and also not stimulated by lithium; site-directed mutagenesis of subunit NqrB residue, part of the sodium binding site, the introduction of a positive charge abates completely the stimulatory effect of sodium, the mutant is not stimulated by lithium
D397N
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mutant is stimulated by Li+. Km value is not affected. Sodium-binding site II is inactive; site-directed mutagenesis of subunit NqrB residue, part of the sodium binding site, the mutation that eliminates the negative charge, but that introduces a polar residue with a partial negative charge, is stimulated only 2fold by sodium
D397S
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mutant is stimulated by Li+. Km value is not affected; site-directed mutagenesis of subunit NqrB residue, part of the sodium binding site, the mutation that eliminates the negative charge, but that introduces a polar residue with a partial negative charge, is stimulated only 2fold by sodium
D88L
mutant enzyme shows little or no change in the KmappNa+ for sodium. The mutant enzyme in which sodium stimulation of sodium-dependent quinone reductase activity activity is lowered significantly but not eliminated, produces diminished levels of sodium pumping activity
E144L
the mutant in which sodium stimulation of sodium-dependent quinone reductase activity is lowered significantly but not eliminated, produces diminished levels of sodium pumping activity
E28A
the mutant in which sodium stimulation of sodium-dependent quinone reductase activity is lowered significantly but not eliminated, produces diminished levels of sodium pumping activity. Little or no change in the KmappNa+ for sodium
E95A
the effect of sodium on sodium-dependent quinone reductase activity is almost eliminated. Sodium-dependent quinone reductase activity of mutant enzyme is very similar to that of wild-type Na+-NQR in the absence of sodium. The mutant enzyme in which the sodium-dependent quinone reductase activity activity is insensitive to sodium is unable to form a sodium gradient
G140A
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site-directed mutagenesis, the mutant shows highly reduced activity and reduced inhibition by 2-n-heptyl-4-hydroxyquinoline N-oxide compared to the wild-type enzyme; sodium-pumping activity of the mutant is not affected under partial turnover conditions. Mutation affects exclusively the binding of ubiquinone
G140L
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mutant shows nonsaturating behavior with up to 50 microM ubiquinone; site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme and no inhibition by 2-n-heptyl-4-hydroxyquinoline N-oxide in contrast to the wild-type enzyme
G141A
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overall structure of the enzyme is not disturbed by the mutation. Mutation specifically affects the ubiquinone binding site. 6fold increase in Km value; site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme and no inhibition by 2-n-heptyl-4-hydroxyquinoline N-oxide in contrast to the wild-type enzyme
G141L
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3fold increase in Km value; site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme and no inhibition by 2-n-heptyl-4-hydroxyquinoline N-oxide in contrast to the wild-type enzyme
G141V
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9fold increase in Km value; site-directed mutagenesis, the mutant shows reduced activity and reduced inhibition by 2-n-heptyl-4-hydroxyquinoline N-oxide compared to the wild-type enzyme
H216L
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the subunit NqrC mutant contains 0.2-0.3 mol of FMN per mol of protein, the mutation reduces the FMN content (30%) of the isolated subunit NqrC
R210L
FAD mutant of subunit NqrF with severely reduced activity using ubiquinone-1or ferricyanide and NADH as substrates
S246A
T225L
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no covalent flavin is detected when threonine-225 is replaced by leucine, the mutation eliminates flavin binding by subunit NqrC
T225Y
T236Y
T236Y/T225Y
Y212L
extremely low NADH:ubiquinone-1 oxidoreductase activity compared to wild-type enzyme; FAD mutant of subunit NqrF with severely reduced activity using ubiquinone-1 or ferricyanide and NADH as substrates
D397A
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mutant is completely insensitive to sodium and also not stimulated by lithium
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D397E
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mutant is stimulated by Li+. Km value is not affected. Mutant contains approximately the same conformational flexibility as the wild type enzyme and is able to undergo a series of conformational changes induced by the redox reaction and by the addition of different cations
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D397K
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mutant is completely insensitive to sodium and also not stimulated by lithium
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D397N
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mutant is stimulated by Li+. Km value is not affected. Sodium-binding site II is inactive
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G140A
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sodium-pumping activity of the mutant is not affected under partial turnover conditions. Mutation affects exclusively the binding of ubiquinone
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G140L
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mutant shows nonsaturating behavior with up to 50 microM ubiquinone
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G141A
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overall structure of the enzyme is not disturbed by the mutation. Mutation specifically affects the ubiquinone binding site. 6fold increase in Km value
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H216L
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the subunit NqrC mutant contains 0.2-0.3 mol of FMN per mol of protein, the mutation reduces the FMN content (30%) of the isolated subunit NqrC
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T225L
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no covalent flavin is detected when threonine-225 is replaced by leucine, the mutation eliminates flavin binding by subunit NqrC
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C111A
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2Fe-2S center mutant with severely reduced activity using ubiquinone-1 and NADH as substrates. NADH:ferricyanide oxidoreduction activity remains unchanged compared to the wild type enzyme
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C70A
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2Fe-2S center mutant with severely reduced activity using ubiquinone-1 and NADH as substrates, the amount of FAD in the C70A mutant is essentially the same as in the wild type. NADH:ferricyanide oxidoreduction activity remains unchanged compared to the wild type enzyme
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C76A
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2Fe-2S center mutant with severely reduced activity using ubiquinone-1 and NADH as substrates. NADH:ferricyanide oxidoreduction activity remains unchanged compared to the wild type enzyme
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C79A
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2Fe-2S center mutant with severely reduced activity using ubiquinone-1 and NADH as substrates. NADH:ferricyanide oxidoreduction activity remains unchanged compared to the wild type enzyme
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S246A
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FAD mutant of subunit NqrF with severely reduced activity possessing only a small residual amount of FAD using ubiquinone-1 or ferricyanide and NADH as substrates
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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
additional information
C76A
2Fe-2S center mutant with severely reduced activity using ubiquinone-1 and NADH as substrates. NADH:ferricyanide oxidoreduction activity remains unchanged compared to the wild type enzyme; 3% of the NADH:ubiquinone-1 oxidoreductase activity compared to wild-type enzyme
C76A
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in the NqrF-C76A mutant, turnover with ferricyanide is almost the same as in the wild type enzyme; in this mutant one of the cysteine ligands of the 2Fe-2S center is changed to alanine, resulting in the complete loss of this cofactor. In all three flavin mutants (NqrB-T236Y, NqrCT225Y, and the double mutant) as well as the 2Fe-2S center mutant (NqrF-C76A), the reduction by NADH of the neutral flavosemiquinone is dramatically slowed, or abolished, compared with the wild type enzyme; mutant lacks the 2Fe-2S center in NqrF (NqrF-C76A). The reaction of the mutant enzyme with NADH consists of a single phase, whether or not Na+ is present. Turnover with ferricyanide is almost the same as in the wild type enzyme. Two electron reduction of a flavin is the only significant phase remaining from the wild type reaction, allows the redox carrier upstream of the 2Fe-2S center to be assigned to the first kinetic phase of the wild type reaction and hence to the FAD in NqrF. Reduction by NADH of the neutral flavosemiquinone is strongly slowed or abolished, compared with the wild type enzyme
C76A
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mutant of subunit NqrF which lacks the 2Fe-2S-center cofactor and shows a 90% decrease in menadione reductase activity
D346A
sodium-dependent quinone reductase activity of mutant enzyme is very similar to that of wild-type Na+-NQR in the absence of sodium. The mutant enzyme in which the sodium-dependent quinone reductase activity activity is insensitive to sodium is unable to form a sodium gradient; the effect of sodium on sodium-dependent quinone reductase activity is almost eliminated. Little or no change in the KmappNa+ for sodium
D346A
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the redox reaction in this mutant is significantly inhibited and the Na+ sensitivity of CoQ reduction is completely abolished, while the apparent affinity for Na+ is essentially unchanged. In D346A, electron transfer between FMN from subunit NqrB and riboflavin is inhibited
D397A
sodium-dependent quinone reductase activity of mutant enzyme is very similar to that of wild-type Na+-NQR in the absence of sodium. The mutant enzyme in which the sodium-dependent quinone reductase activity is insensitive to sodium is unable to form a sodium gradient; the effect of sodium on sodium-dependent quinone reductase activity is almost eliminated
D397A
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the reduction of subunit NqrB mutant D397A by NADH is very similar to the reduction of wild type enzyme but does not show sensitivity to Na+, and the rate of the stable neutral riboflavin radical to riboflavin-H2 is decreased 3fold. In NqrB-D397A, the reaction takes place in two steps: rapid oxidation of riboflavin and the two FMNs, followed by oxidation of FAD, at a 16fold lower rate
D397A
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mutant is completely insensitive to sodium and also not stimulated by lithium; site-directed mutagenesis of subunit NqrB residue, part of the sodium binding site, the kinetics of the NqrB-D397A mutant show an unsaturable behavior for sodium in contrast to the Michaelis-Menten kinetics of the wild-type enzyme. The mutant is not stimulated by lithium
S246A
extremely low NADH:ubiquinone-1 oxidoreductase activity compared to wild-type enzyme; FAD mutant of subunit NqrF with severely reduced activity possessing only a small residual amount of FAD using ubiquinone-1 or ferricyanide and NADH as substrates
S246A
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the wild type enzyme is capable of transferring electrons from NADH to ferricyanide. This reaction is almost completely abolished in the NqrFS246A mutant, which lacks the FAD; this reaction is almost completely abolished in the NqrFS246A mutant, which lacks the FAD
T225Y
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lacks FMN in subunit NqrC, is not able to carry out electron transfer from NADH to ubiquinone, but instead from NADH to ferricyanide
T225Y
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in all three flavin mutants (NqrB-T236Y, NqrCT225Y, and the double mutant) as well as the 2Fe-2S center mutant (NqrF-C76A), the reduction by NADH of the neutral flavosemiquinone is dramatically slowed, or abolished, compared with the wild type enzyme; mutant lacks FMN in subunit C (NqrC-T225Y). Reduction by NADH of the neutral flavosemiquinone is strongly slowed or abolished, compared with the wild type enzyme
T225Y
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the mutant lacks FMN from subunit NqrC and is unable to produce an electrochemical potential under either partial or multiple turnover conditions
T236Y
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lacks FMN in subunit NqrB, is not able to carry out electron transfer from NADH to ubiquinone, but instead from NADH to ferricyanide
T236Y
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in all three flavin mutants (NqrB-T236Y, NqrCT225Y, and the double mutant) as well as the 2Fe-2S center mutant (NqrF-C76A), the reduction by NADH of the neutral flavosemiquinone is dramatically slowed, or abolished, compared with the wild type enzyme; mutant lacks FMN in subunit B (NqrB-T236Y). Reduction by NADH of the neutral flavosemiquinone is strongly slowed or abolished, compared with the wild type enzyme
T236Y
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the mutant lacks FMN from subunit NqrB and is unable to produce an electrochemical potential under either partial or multiple turnover conditions
T236Y/T225Y
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NqrB-T236Y/NqrC-T225Y, double mutant that lacks both covalently bound FMN cofactors. The double mutant contains riboflavin and FAD in a 0.6:1 ratio, as the only flavins in the enzyme, noncovalently bound flavins are detected. In the oxidized form, the double mutant exhibits an EPR signal consistent with a neutral flavosemiquinone radical, which is abolished on reduction of the enzyme
T236Y/T225Y
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in all three flavin mutants (NqrB-T236Y, NqrCT225Y, and the double mutant) as well as the 2Fe-2S center mutant (NqrF-C76A), the reduction by NADH of the neutral flavosemiquinone is dramatically slowed, or abolished, compared with the wild type enzyme; mutant lacks FMN in subunit B and FMN in subunit C (NqrB-T236Y/NqrC-T225Y). This mutant contains only the noncovalently bound FAD in NqrF and the noncovalently bound riboflavin. The reaction of the mutant enzyme with NADH consists of a single phase, whether or not Na+ is present. The rate constants are almost identical, are as the spectra. The spectra appear to show two-electron reduction of a flavin. The spectra and rates are consistent with those of the first phase of the reaction of the wild type enzyme in the absence of Na+. Reduction by NADH of the neutral flavosemiquinone is strongly slowed or abolished, compared with the wild type enzyme
additional information
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a soluble variant of NqrF lacking its hydrophobic, N-terminal helix (NqrF') is produced in Vibrio cholerae wild type and nqr deletion strain. Under identical conditions of growth and induction, the yield of NqrF' increased by 30% in the presence of the Na+-NQR. FAD-containing NqrF' species with or without the FeS cluster are observed, indicating that assembly of the FeS center, but not insertion of the flavin cofactor, is limited during overproduction in Vibrio cholerae. NqrF' lacking the [2Fe–2S] cluster is less stable, partially unfolded, and therefore prone to proteolytic degradation in Vibrio cholerae
additional information
A6XUU9
preparation of membranes containing subcomplexes of Na+-NQR, NqrBCDEF, NqrACDEF, NqrABDEF, NqrABCEF, and NqrABCF, by expressing mutant forms of the Na+-NQR in Vibrio cholerae enzyme-deficient mutant strain DELTAnqr
additional information
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construction of a Vibrio cholerae deletion strain lacking the genomic nqr operon, DELTAnqr; residue D397 forms part of one of the at least two sodium-binding sites. Both size and charge at this position are critical for the function of the enzyme. The residue is involved in cation selectivity, has a critical role in the communication between sodium-binding sites, by promoting cooperativity, and controls the electron transfer step involved in sodium uptake
additional information
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residue D397 forms part of one of the at least two sodium-binding sites. Both size and charge at this position are critical for the function of the enzyme. The residue is involved in cation selectivity, has a critical role in the communication between sodium-binding sites, by promoting cooperativity, and controls the electron transfer step involved in sodium uptake
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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
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reconstitution of Na+-NQR in proteoliposomes and generation of membrane potential. Purified Na+-NQR is mixed with Escherichia coli phospholipids and n-octyl glucoside (detergent/phospholipid ratio = 1.3) in buffer containing 100 mM KCl, 50 mM HEPES, 1 mM EDTA, pH 7.0. The detergent is removed slowly
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reconstitution of purified recombinant enzyme with riboflavin, enzyme is mixed with 0.1 mM riboflavin from a1 mM riboflavin stock solution in N,N-dimethylformamide, 10 min, 25°C
A6XUU9
reconstitution of recombinant Na+-NQR and recombinant His6-tagged NqrA with ubiquinone-8, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
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about 50% of all mitochondrial disorders affecting the energy metabolism can be traced to mutations in complex 1
medicine
-
about 50% of all mitochondrial disorders affecting the energy metabolism can be traced to mutations in complex 1
medicine
-
about 50% of all mitochondrial disorders affecting the energy metabolism can be traced to mutations in complex 1
medicine
-
about 50% of all mitochondrial disorders affecting the energy metabolism can be traced to mutations in complex 1
medicine
-
about 50% of all mitochondrial disorders affecting the energy metabolism can be traced to mutations in complex 1
medicine
-
about 50% of all mitochondrial disorders affecting the energy metabolism can be traced to mutations in complex 1
medicine
-
about 50% of all mitochondrial disorders affecting the energy metabolism can be traced to mutations in complex 1
medicine
-
about 50% of all mitochondrial disorders affecting the energy metabolism can be traced to mutations in complex 1
medicine
-
about 50% of all mitochondrial disorders affecting the energy metabolism can be traced to mutations in complex 1
medicine
-
about 50% of all mitochondrial disorders affecting the energy metabolism can be traced to mutations in complex 1
medicine
-
about 50% of all mitochondrial disorders affecting the energy metabolism can be traced to mutations in complex 1
medicine
-
about 50% of all mitochondrial disorders affecting the energy metabolism can be traced to mutations in complex 1
medicine
-
about 50% of all mitochondrial disorders affecting the energy metabolism can be traced to mutations in complex 1
medicine
-
about 50% of all mitochondrial disorders affecting the energy metabolism can be traced to mutations in complex 1
medicine
-
about 50% of all mitochondrial disorders affecting the energy metabolism can be traced to mutations in complex 1
medicine
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Vibrio cholerae Na+-NQR is significant for the induction of virulence factors. Thus, this enzyme can be used as a target in the treatment or prevention of many infectious diseases
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