BRENDA - Enzyme Database

High-stability semiquinone intermediate in nitrate reductase A (NarGHI) from Escherichia coli is located in a quinol oxidation site close to heme bD

Lanciano, P.; Magalon, A.; Bertrand, P.; Guigliarelli, B.; Grimaldi, S.; Biochemistry 46, 5323-5329 (2007)

Data extracted from this reference:

Engineering
EC Number
Protein Variants
Commentary
Organism
1.7.5.1
H187Y
mutant lacking the distal heme bD, no EPR signal of the semiquinone is observed
Escherichia coli
1.7.5.1
H187Y
mutant lacks the distal heme bD, no EPR signal of the semiquinone is observed
Escherichia coli
1.7.5.1
H56Y
a semiquinone is detected in the mutant lacking the proximal heme bP. Its thermodynamic properties and spectroscopic characteristics, as revealed by Q-band EPR and ENDOR spectroscopies, are identical to those observed in the native enzyme
Escherichia coli
1.7.5.1
H56Y
mutant lacks the distal heme bD, a EPR signal of the semiquinone is observed
Escherichia coli
1.7.5.1
H66Y
mutant lacking the distal heme bD, no EPR signal of the semiquinone is observed
Escherichia coli
1.7.5.1
H66Y
mutant lacks the distal heme bD, no EPR signal of the semiquinone is observed
Escherichia coli
1.7.5.1
K86A
mutation dramatically reduces the rate of oxidation of both menaquinol and ubiquinol analogues
Escherichia coli
1.7.5.1
K86A
the mutation close to heme bD leads to the loss of the EPR signal of the semiquinone, although both hemes are present, the substitution dramatically reduces the rate of oxidation of both mena and ubiquinol analogues
Escherichia coli
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
1.7.5.1
membrane
-
Escherichia coli
16020
-
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
1.7.5.1
nitrate + quinol
Escherichia coli
first enzyme involved in respiratory denitrification in prokaryotes
nitrite + quinone + H2O
-
-
?
Organism
EC Number
Organism
UniProt
Commentary
Textmining
1.7.5.1
Escherichia coli
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
1.7.5.1
nitrate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinol
i.e. decylubiquinol
696212
Escherichia coli
nitrite + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone + H2O
-
-
-
?
1.7.5.1
nitrate + 2-methyl-1,4-naphthoquinol
i.e menadiol
696212
Escherichia coli
nitrite + 2-methyl-1,4-naphthoquinone + H2O
-
-
-
?
1.7.5.1
nitrate + 2-methyl-1,4-naphthoquinol
i.e. menadiol
696212
Escherichia coli
nitrite + 2-methyl-1,4-naphthoquinone + H2O
-
-
-
?
1.7.5.1
nitrate + 5-hydroxy-1,4-naphthoquinol
i.e. juglone
696212
Escherichia coli
nitrite + 5-hydroxy-1,4-naphthoquinone + H2O
-
-
-
?
1.7.5.1
nitrate + 5-hydroxy-1,4-naphthoquinol
i.e. reduced form of juglone
696212
Escherichia coli
nitrite + 5-hydroxy-1,4-naphthoquinone + H2O
-
-
-
?
1.7.5.1
nitrate + 5-hydroxy-2-methyl-naphthalene-1,4-diol
i.e plumbagin
696212
Escherichia coli
nitrite + 5-hydroxy-2-methyl-naphthalene-1,4-dione + H2O
-
-
-
?
1.7.5.1
nitrate + 5-hydroxy-2-methyl-naphthalene-1,4-diol
i.e. reduced form of plumbagin
696212
Escherichia coli
nitrite + 5-hydroxy-2-methyl-naphthalene-1,4-dione + H2O
-
-
-
?
1.7.5.1
nitrate + quinol
first enzyme involved in respiratory denitrification in prokaryotes
696212
Escherichia coli
nitrite + quinone + H2O
-
-
-
?
1.7.5.1
nitrate + quinol
NarGHI strongly stabilizes a semiquinone radical located within the dihemic anchor subunit NarI. The semiquinone is located within the quinol oxidation site QD
696212
Escherichia coli
nitrite + quinone
-
-
-
?
1.7.5.1
nitrate + tetramethyl-p-benzoquinol
i.e. duroquinol
696212
Escherichia coli
nitrite + tetramethyl-p-benzoquinone + H2O
-
-
-
?
Synonyms
EC Number
Synonyms
Commentary
Organism
1.7.5.1
NarGHI
-
Escherichia coli
1.7.5.1
nitrate reductase A
-
Escherichia coli
1.7.5.1
quinol/nitrate oxidoreductase
-
Escherichia coli
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.7.5.1
cytochrome
NarI is strongly associated with heme bD, Lys86 is required for its stabilization
Escherichia coli
1.7.5.1
cytochrome bD
NarI is strongly associated with heme bD, Lys86 is required for its stabilization
Escherichia coli
1.7.5.1
additional information
the semiquinone is located within the quinol oxidation site QD
Escherichia coli
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.7.5.1
cytochrome
NarI is strongly associated with heme bD, Lys86 is required for its stabilization
Escherichia coli
1.7.5.1
cytochrome bD
NarI is strongly associated with heme bD, Lys86 is required for its stabilization
Escherichia coli
1.7.5.1
additional information
the semiquinone is located within the quinol oxidation site QD
Escherichia coli
Engineering (protein specific)
EC Number
Protein Variants
Commentary
Organism
1.7.5.1
H187Y
mutant lacking the distal heme bD, no EPR signal of the semiquinone is observed
Escherichia coli
1.7.5.1
H187Y
mutant lacks the distal heme bD, no EPR signal of the semiquinone is observed
Escherichia coli
1.7.5.1
H56Y
a semiquinone is detected in the mutant lacking the proximal heme bP. Its thermodynamic properties and spectroscopic characteristics, as revealed by Q-band EPR and ENDOR spectroscopies, are identical to those observed in the native enzyme
Escherichia coli
1.7.5.1
H56Y
mutant lacks the distal heme bD, a EPR signal of the semiquinone is observed
Escherichia coli
1.7.5.1
H66Y
mutant lacking the distal heme bD, no EPR signal of the semiquinone is observed
Escherichia coli
1.7.5.1
H66Y
mutant lacks the distal heme bD, no EPR signal of the semiquinone is observed
Escherichia coli
1.7.5.1
K86A
mutation dramatically reduces the rate of oxidation of both menaquinol and ubiquinol analogues
Escherichia coli
1.7.5.1
K86A
the mutation close to heme bD leads to the loss of the EPR signal of the semiquinone, although both hemes are present, the substitution dramatically reduces the rate of oxidation of both mena and ubiquinol analogues
Escherichia coli
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
1.7.5.1
membrane
-
Escherichia coli
16020
-
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
1.7.5.1
nitrate + quinol
Escherichia coli
first enzyme involved in respiratory denitrification in prokaryotes
nitrite + quinone + H2O
-
-
?
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
1.7.5.1
nitrate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinol
i.e. decylubiquinol
696212
Escherichia coli
nitrite + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone + H2O
-
-
-
?
1.7.5.1
nitrate + 2-methyl-1,4-naphthoquinol
i.e menadiol
696212
Escherichia coli
nitrite + 2-methyl-1,4-naphthoquinone + H2O
-
-
-
?
1.7.5.1
nitrate + 2-methyl-1,4-naphthoquinol
i.e. menadiol
696212
Escherichia coli
nitrite + 2-methyl-1,4-naphthoquinone + H2O
-
-
-
?
1.7.5.1
nitrate + 5-hydroxy-1,4-naphthoquinol
i.e. juglone
696212
Escherichia coli
nitrite + 5-hydroxy-1,4-naphthoquinone + H2O
-
-
-
?
1.7.5.1
nitrate + 5-hydroxy-1,4-naphthoquinol
i.e. reduced form of juglone
696212
Escherichia coli
nitrite + 5-hydroxy-1,4-naphthoquinone + H2O
-
-
-
?
1.7.5.1
nitrate + 5-hydroxy-2-methyl-naphthalene-1,4-diol
i.e plumbagin
696212
Escherichia coli
nitrite + 5-hydroxy-2-methyl-naphthalene-1,4-dione + H2O
-
-
-
?
1.7.5.1
nitrate + 5-hydroxy-2-methyl-naphthalene-1,4-diol
i.e. reduced form of plumbagin
696212
Escherichia coli
nitrite + 5-hydroxy-2-methyl-naphthalene-1,4-dione + H2O
-
-
-
?
1.7.5.1
nitrate + quinol
first enzyme involved in respiratory denitrification in prokaryotes
696212
Escherichia coli
nitrite + quinone + H2O
-
-
-
?
1.7.5.1
nitrate + quinol
NarGHI strongly stabilizes a semiquinone radical located within the dihemic anchor subunit NarI. The semiquinone is located within the quinol oxidation site QD
696212
Escherichia coli
nitrite + quinone
-
-
-
?
1.7.5.1
nitrate + tetramethyl-p-benzoquinol
i.e. duroquinol
696212
Escherichia coli
nitrite + tetramethyl-p-benzoquinone + H2O
-
-
-
?