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Literature summary extracted from

  • Barquera, B.; Nilges, M.J.; Morgan, J.E.; Ramirez-Silva, L.; Zhou, W.; Gennis, R.B.
    Mutagenesis study of the 2Fe-2S center and the FAD binding site of the Na(+)-translocating NADH:ubiquinone oxidoreductase from Vibrio cholerae (2004), Biochemistry, 43, 12322-12330.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.2.1.1 expressed in Vibrio cholerae strain O395N1-toxT:lac::DELTAnqrA-F Vibrio cholerae serotype O1

Protein Variants

EC Number Protein Variants Comment Organism
7.2.1.1 C111A subunit NqrF, 3% of the NADH:ubiquinone-1 oxidoreductase activity compared to wild-type enzyme Vibrio cholerae serotype O1
7.2.1.1 C111A subunit NqrF, 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 Vibrio cholerae serotype O1
7.2.1.1 C70A subunit NqrF, 3% of the NADH:ubiquinone-1 oxidoreductase activity compared to wild-type enzyme Vibrio cholerae serotype O1
7.2.1.1 C70A subunit NqrF, 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 Vibrio cholerae serotype O1
7.2.1.1 C76A subunit NqrF, 3% of the NADH:ubiquinone-1 oxidoreductase activity compared to wild-type enzyme Vibrio cholerae serotype O1
7.2.1.1 C76A subunit NqrF, 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 Vibrio cholerae serotype O1
7.2.1.1 C79A subunit NqrF, 3% of the NADH:ubiquinone-1 oxidoreductase activity compared to wild-type enzyme Vibrio cholerae serotype O1
7.2.1.1 C79A subunit NqrF, 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 Vibrio cholerae serotype O1
7.2.1.1 R210L FAD mutant of subunit NqrF with severely reduced activity using ubiquinone-1or ferricyanide and NADH as substrates Vibrio cholerae serotype O1
7.2.1.1 S246A subunit NqrF, extremely low NADH:ubiquinone-1 oxidoreductase activity compared to wild-type enzyme Vibrio cholerae serotype O1
7.2.1.1 S246A 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 Vibrio cholerae serotype O1
7.2.1.1 Y212L subunit NqrF, extremely low NADH:ubiquinone-1 oxidoreductase activity compared to wild-type enzyme Vibrio cholerae serotype O1
7.2.1.1 Y212L FAD mutant of subunit NqrF with severely reduced activity using ubiquinone-1 or ferricyanide and NADH as substrates Vibrio cholerae serotype O1

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.2.1.1 Iron contains one 2Fe-2S center. Four conserved cysteines, C70, C76, C79, and C111 in the subunit NqrF match the canonical 2Fe-2S motif Vibrio cholerae serotype O1

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.2.1.1 NADH + H+ + ubiquinone-1 + n Na+/in Vibrio cholerae serotype O1
-
 NAD+ + ubiquinol-1 + n Na+/out
-
 ?
7.2.1.1 NADH + H+ + ubiquinone-1 + n Na+/in Vibrio cholerae serotype O1 ATCC 39315
-
 NAD+ + ubiquinol-1 + n Na+/out
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
7.2.1.1 Vibrio cholerae serotype O1 Q9KPS1 and Q9KPS2 and P0C6E0 and Q9X4Q6 and Q9X4Q7 and Q9X4Q8 Q9KPS1: subunit NqrA, Q9KPS2: subunit NqrB, P0C6E0: subunit NqrC, Q9X4Q6: subunit NqrD, Q9X4Q7: subunit NqrE, Q9X4Q8: subunit NqrF. The enzyme consists of six subunits encoded by the NQR operon.
-
7.2.1.1 Vibrio cholerae serotype O1 ATCC 39315 Q9KPS1 and Q9KPS2 and P0C6E0 and Q9X4Q6 and Q9X4Q7 and Q9X4Q8 Q9KPS1: subunit NqrA, Q9KPS2: subunit NqrB, P0C6E0: subunit NqrC, Q9X4Q6: subunit NqrD, Q9X4Q7: subunit NqrE, Q9X4Q8: subunit NqrF. The enzyme consists of six subunits encoded by the NQR operon.
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.2.1.1 Ni-NTA column chromatography Vibrio cholerae serotype O1

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.2.1.1 2 ferricyanide + NADH + n Na+/in
-
 Vibrio cholerae serotype O1 2 ferrocyanide + NAD+ + H+ + n Na+/out
-
 ?
7.2.1.1 2 ferricyanide + NADH + n Na+/in
-
 Vibrio cholerae serotype O1 ATCC 39315 2 ferrocyanide + NAD+ + H+ + n Na+/out
-
 ?
7.2.1.1 NADH + H+ + ubiquinone-1 + n Na+/in
-
 Vibrio cholerae serotype O1 NAD+ + ubiquinol-1 + n Na+/out
-
 ?
7.2.1.1 NADH + H+ + ubiquinone-1 + n Na+/in
-
 Vibrio cholerae serotype O1 ATCC 39315 NAD+ + ubiquinol-1 + n Na+/out
-
 ?
7.2.1.1 NADH + ubiquinone-1
-
 Vibrio cholerae serotype O1 NAD+ + ubiquinol-1
-
 ?
7.2.1.1 NADH + ubiquinone-1
-
 Vibrio cholerae serotype O1 ATCC 39315 NAD+ + ubiquinol-1
-
 ?

Synonyms

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

Cofactor

EC Number Cofactor Comment Organism Structure
7.2.1.1 FAD contains one noncovalently bound FAD Vibrio cholerae serotype O1
7.2.1.1 FMN contains two covalently bound FMNs Vibrio cholerae serotype O1
7.2.1.1 NADH
-
 Vibrio cholerae serotype O1
7.2.1.1 riboflavin contains one riboflavin Vibrio cholerae serotype O1
7.2.1.1 [2Fe-2S]-center contains one 2Fe-2S-center Vibrio cholerae serotype O1