BRENDA - Enzyme Database show

Catalytic and biophysical properties of a nitrogenase Apo-MoFe protein produced by a nifB-deletion mutant of Azotobacter vinelandii

Christiansen, J.; Goodwin, P.J.; Lanzilotta, W.N.; Seefeldt, L.C.; Dean, D.R.; Biochemistry 37, 12611-12623 (1998)

Data extracted from this reference:

Engineering
EC Number
Amino acid exchange
Commentary
Organism
1.18.6.1
additional information
natural nifB deletion mutant, MoFe protein without FeMo-cofactor and with small changes in the electronic properties of the [4Fe-4S] cluster
Azotobacter vinelandii
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
1.18.6.1
Iron
contains [4Fe4S] cluster
Azotobacter vinelandii
1.18.6.1
Molybdenum
-
Azotobacter vinelandii
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.18.6.1
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
Azotobacter vinelandii
-
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.18.6.1
Azotobacter vinelandii
-
nitrogen fixation complex is encoded on nif gene cluster
-
Purification (Commentary)
EC Number
Commentary
Organism
1.18.6.1
FeMo-cofactorless MoFe protein from nifB deletion mutant
Azotobacter vinelandii
Reaction
EC Number
Reaction
Commentary
Organism
1.18.6.1
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O = 8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
enzyme is composed of 2 metalloproteins: component I MoFe protein and component II Fe protein; schematic electron flow from Fe protein to substrate via MoFe protein and MoFe protein-cofactor
Azotobacter vinelandii
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.18.6.1
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
-
440179
Azotobacter vinelandii
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
1.18.6.1
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
-
440179
Azotobacter vinelandii
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
440179
Azotobacter vinelandii
?
Subunits
EC Number
Subunits
Commentary
Organism
1.18.6.1
More
apo-MoFe protein has a alpha2beta2 subunit composition and interacts with Fe protein, can be rebuilt by addition of FeMo-cofactor
Azotobacter vinelandii
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
1.18.6.1
additional information
natural nifB deletion mutant, MoFe protein without FeMo-cofactor and with small changes in the electronic properties of the [4Fe-4S] cluster
Azotobacter vinelandii
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
1.18.6.1
Iron
contains [4Fe4S] cluster
Azotobacter vinelandii
1.18.6.1
Molybdenum
-
Azotobacter vinelandii
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.18.6.1
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
Azotobacter vinelandii
-
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
?
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.18.6.1
FeMo-cofactorless MoFe protein from nifB deletion mutant
Azotobacter vinelandii
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.18.6.1
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
-
440179
Azotobacter vinelandii
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
-
-
?
1.18.6.1
8 reduced ferredoxin + 8 H+ + N2 + 16 ATP + 16 H2O
-
440179
Azotobacter vinelandii
8 oxidized ferredoxin + H2 + 2 NH3 + 16 ADP + 16 phosphate
-
440179
Azotobacter vinelandii
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.18.6.1
More
apo-MoFe protein has a alpha2beta2 subunit composition and interacts with Fe protein, can be rebuilt by addition of FeMo-cofactor
Azotobacter vinelandii