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

BRENDA support

1.7.5.1: nitrate reductase (quinone)

This is an abbreviated version!
For detailed information about nitrate reductase (quinone), go to the full flat file.

Word Map on EC 1.7.5.1

Reaction

nitrate
+
a quinol
=
nitrite
 +
a quinone
 +
H2O

Synonyms

EC 1.7.99.4, gene narH, membrane-bound nitrate reductase, membrane-bound quinol:nitrate oxidoreductase, MSMEG_5140, NaR, NaR1, NarG, NarGHI, narH, NarI, NarZ, nitrate reducatse A, nitrate reductase A, nitrate reductase Z, NRA nitrate reductase A, NRZ, NRZ nitrate reductase, Pden_4236, quinol-nitrate oxidoreductase, quinol/nitrate oxidoreductase, quinol:nitrate oxidoreductase, SCO6532, SCO6533, SCO6534, SCO6535

ECTree

     1 Oxidoreductases
         1.7 Acting on other nitrogenous compounds as donors
             1.7.5 With a quinone or similar compound as acceptor
                1.7.5.1 nitrate reductase (quinone)

Engineering

Engineering on EC 1.7.5.1 - nitrate reductase (quinone)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C196A
mutation results in the full loss of the four Fe-S clusters and of the Mo-cofactor, leading to inactive enzyme
C227A
mutation results in the full loss of the four Fe-S clusters and of the Mo-cofactor, leading to inactive enzyme
C263A
mutant retains significant nitrate reductase activity. EPR analysis shows that the highest redox potential [4Fe-4S] cluster (center 1) is selectively removed by the C263A mutation
C26A
mutant retains significant nitrate reductase activity. Mutation likely eliminates the lowest potential [4Fe-4S] cluster (center 4)
G65A
site-directed mutageness of subunit NarI, mutant G65A is able to support growth and retains significant quinol:nitrate oxidoreductase activity
H187Y
H205Y
-
mutant without heme bH but with heme bL, a smaller and slower heme reduction compared to that of the wild-type enzyme is observed. A transient species, likely to be associated with a semiquinone radical anion, is generated not only on reduction of the wild-type enzyme but also on reduction of NarGHIH56R and NarGHIH205Y. Compared to the wild type, no significant heme reoxidation is observed for NarGHIH56R and NarGHIH205Y. This result indicates that a single mutation removing heme bH blocks the electron-transfer pathway from the subunit NarI to the catalytic dimer NarGH
H49C
the mutant lacks catalytic activity
H49S
the mutant lacks catalytic activity and the FS0 [4Fe-4S] cluster and molybdo-bis(pyranopterin guanine dinucleotide) cofactor but retains the GDP moieties
H56R
-
mutant without heme bH but with heme bL, a smaller and slower heme reduction compared to that of the wild-type enzyme is observed. A transient species, likely to be associated with a semiquinone radical anion, is generated not only on reduction of the wild-type enzyme but also on reduction of NarGHIH56R and NarGHIH205Y. Compared to the wild type, no significant heme reoxidation is observed for NarGHIH56R and NarGHIH205Y. This result indicates that a single mutation removing heme bH blocks the electron-transfer pathway from the subunit NarI to the catalytic dimer NarGH
R94S
the mutant shows a concomitant decrease in enzyme turnover to about 30% of the wild type
H49C
-
the mutant lacks catalytic activity
-
H49S
-
the mutant lacks catalytic activity and the FS0 [4Fe-4S] cluster and molybdo-bis(pyranopterin guanine dinucleotide) cofactor but retains the GDP moieties
-
R94S
-
the mutant shows a concomitant decrease in enzyme turnover to about 30% of the wild type
-
additional information
-
mutant enzyme lacking the highest-potential [4Fe-4S] cluster is devoid of menadione activity, but still retains duroquinone activity