Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 7.2.1.1 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
Search for more literature for 7.2.1.1

Cloned(Commentary)

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

Protein Variants

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

Metals/Ions Comment Organism Structure
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)

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

Organism

Organism UniProt Comment Textmining
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.
-
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)

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

Substrates and Products (Substrate)

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

Synonyms

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

Cofactor

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