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1.7.7.2: ferredoxin-nitrate reductase

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

Word Map on EC 1.7.7.2

Reaction

nitrite
+
H2O
+
oxidized ferredoxin
=
nitrate
+
reduced ferredoxin
+ 2 H+

Synonyms

assimilatory ferredoxin-nitrate reductase, Assimilatory nitrate reductase, C452_13229, dissimilatory nitrate reductase, EC 1.7.99.4, Fd-dependent nitrate reductase, Fd-NAS, NaR, narB, NarGH, NAS, NasB, nitrate (ferredoxin) reductase, nitrate reductase, reductase, nitrate (ferredoxin), respiratory nitrate reductase

ECTree

     1 Oxidoreductases
         1.7 Acting on other nitrogenous compounds as donors
             1.7.7 With an iron-sulfur protein as acceptor
                1.7.7.2 ferredoxin-nitrate reductase

Engineering

Engineering on EC 1.7.7.2 - ferredoxin-nitrate reductase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E219Q
-
the mutant shows 96.1% activity when reduced ferredoxin serves as the electron donor compared to the wild type enzyme
K201Q
-
the mutant shows 14.8% activity and decreased binding affinity when reduced ferredoxin serves as the electron donor compared to the wild type enzyme
K614Q
-
the mutant shows 11.5% activity and decreased binding affinity when reduced ferredoxin serves as the electron donor compared to the wild type enzyme
K614R
-
the mutant shows 63.3% activity when reduced ferredoxin serves as the electron donor compared to the wild type enzyme
R197Q
-
the mutant shows 91.8% activity when reduced ferredoxin serves as the electron donor compared to the wild type enzyme
R43K
-
the mutant shows 91% activity when reduced ferredoxin serves as the electron donor compared to the wild type enzyme
R43Q
-
the mutant shows 16.4% activity and decreased binding affinity when reduced ferredoxin serves as the electron donor compared to the wild type enzyme
R46K
-
the mutant shows 97.7% activity when reduced ferredoxin serves as the electron donor compared to the wild type enzyme
R46Q
-
the mutant 24.3% activity and decreased binding affinity when reduced ferredoxin serves as the electron donor compared to the wild type enzyme
C12A
no actiivty, no iron-sulfur cluster
C16S
1.9% of wild type activity with ferredoxin, no iron-sulfur cluster
C56A
no activity, no iron-sulfur cluster
C56S
70% of wild type activity with ferredoxin, contains an iron-sulfur cluster
C9A
no activity, no iron-sulfur cluster
C9H
no narB expression
D60E
-
the mutant shows 71.3% activity compared to the wild type enzyme
D60N
-
the mutant shows 41.5% activity compared to the wild type enzyme
D65N
-
the mutant shows 97% activity compared to the wild type enzyme
D66N
-
the mutant shows 92% activity compared to the wild type enzyme
E29D
-
the mutant shows 84.8% activity compared to the wild type enzyme
E29N
-
the mutant shows 59% activity compared to the wild type enzyme
E30N
-
the mutant shows 92.7% activity compared to the wild type enzyme
E92D
-
the mutant shows 40.5% activity compared to the wild type enzyme
E92Q
-
the mutant shows less than 0.1% activity compared to the wild type enzyme
E93D
-
the mutant shows 113% activity compared to the wild type enzyme
E93N
-
the mutant shows 46% activity compared to the wild type enzyme
additional information
construction of A narB knockout mutant using a homologous recombination strategy. The DnarB strain produces 7times more H2 than the wild-type after 2 days of fermentation, while in the absence of nitrate, both DELTAnarB and wild-type produce the same amount of H2, as expected. The DELTAnarB strain cannot grow photoautotrophically on nitrate, but does grow on urea or ammonia. The DELTAnarB strain significantly redirects biomass accumulation into glycogen reserves at the expense of protein accumulation throughout growth. Phenotype, overview