Cloned (Comment) | Organism |
---|---|
expression of full-length enzyme and N-terminally His6-tagged large subunit NqrA in Vibrio cholerae strain O395 N1 DELTAnqr | Vibrio cholerae serotype O1 |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2-n-heptyl-4-hydroxyquinoline N-oxide | - |
Vibrio cholerae serotype O1 |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | membrane-embedded | Vibrio cholerae serotype O1 | 16020 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | the enzyme contains one FeS cluster | Vibrio cholerae serotype O1 |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
50793 | - |
1 * 50793, subunit NqrA, mass spectrometry | Vibrio cholerae serotype O1 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
NADH + H+ + ubiquinone + n Na+/in | Vibrio cholerae serotype O1 | - |
NAD+ + ubiquinol + n Na+/out | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Vibrio cholerae serotype O1 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
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 | Vibrio cholerae serotype O1 |
Renatured (Comment) | Organism |
---|---|
reconstitution of recombinant Na+-NQR and recombinant His6-tagged NqrA with ubiquinone-8, overview | Vibrio cholerae serotype O1 |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | Vibrio cholerae serotype O1 | ? | - |
? | |
NADH + H+ + ubiquinone + n Na+/in | - |
Vibrio cholerae serotype O1 | NAD+ + ubiquinol + n Na+/out | - |
? | |
NADH + H+ + ubiquinone + n Na+/in | 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 | Vibrio cholerae serotype O1 | NAD+ + ubiquinol + n Na+/out | - |
? |
Subunits | Comment | Organism |
---|---|---|
hexamer | Na+-NQR is a multisubunit, membrane-embedded NADH dehydrogenase | Vibrio cholerae serotype O1 |
monomer | 1 * 50793, subunit NqrA, mass spectrometry | Vibrio cholerae serotype O1 |
More | putative arrangement of subunits and cofactors of the Na+-NQR | Vibrio cholerae serotype O1 |
Synonyms | Comment | Organism |
---|---|---|
Na+-NQR | - |
Vibrio cholerae serotype O1 |
Na+-pumping NADH:quinone oxidoreductase | - |
Vibrio cholerae serotype O1 |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Vibrio cholerae serotype O1 |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Vibrio cholerae serotype O1 |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
flavin | the enzyme contains four flavins | Vibrio cholerae serotype O1 | |
additional information | putative arrangement of subunits and cofactors of the Na+-NQR | Vibrio cholerae serotype O1 | |
NADH | - |
Vibrio cholerae serotype O1 |
General Information | Comment | Organism |
---|---|---|
physiological function | Vibrio cholerae relies on the Na+-pumping NADH:quinone oxidoreductase as the first complex in its respiratory chain | Vibrio cholerae serotype O1 |