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Literature summary for 1.7.5.1 extracted from

  • Lanciano, P.; Magalon, A.; Bertrand, P.; Guigliarelli, B.; Grimaldi, S.
    High-stability semiquinone intermediate in nitrate reductase A (NarGHI) from Escherichia coli is located in a quinol oxidation site close to heme bD (2007), Biochemistry, 46, 5323-5329.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
H187Y mutant lacking the distal heme bD, no EPR signal of the semiquinone is observed Escherichia coli
H187Y mutant lacks the distal heme bD, no EPR signal of the semiquinone is observed Escherichia coli
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
H56Y mutant lacks the distal heme bD, a EPR signal of the semiquinone is observed Escherichia coli
H66Y mutant lacking the distal heme bD, no EPR signal of the semiquinone is observed Escherichia coli
H66Y mutant lacks the distal heme bD, no EPR signal of the semiquinone is observed Escherichia coli
K86A mutation dramatically reduces the rate of oxidation of both menaquinol and ubiquinol analogues Escherichia coli
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

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Escherichia coli 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
nitrate + quinol Escherichia coli first enzyme involved in respiratory denitrification in prokaryotes nitrite + quinone + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nitrate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinol i.e. decylubiquinol Escherichia coli nitrite + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone + H2O
-
 ?
nitrate + 2-methyl-1,4-naphthoquinol i.e menadiol Escherichia coli nitrite + 2-methyl-1,4-naphthoquinone + H2O
-
 ?
nitrate + 2-methyl-1,4-naphthoquinol i.e. menadiol Escherichia coli nitrite + 2-methyl-1,4-naphthoquinone + H2O
-
 ?
nitrate + 5-hydroxy-1,4-naphthoquinol i.e. juglone Escherichia coli nitrite + 5-hydroxy-1,4-naphthoquinone + H2O
-
 ?
nitrate + 5-hydroxy-1,4-naphthoquinol i.e. reduced form of juglone Escherichia coli nitrite + 5-hydroxy-1,4-naphthoquinone + H2O
-
 ?
nitrate + 5-hydroxy-2-methyl-naphthalene-1,4-diol i.e plumbagin Escherichia coli nitrite + 5-hydroxy-2-methyl-naphthalene-1,4-dione + H2O
-
 ?
nitrate + 5-hydroxy-2-methyl-naphthalene-1,4-diol i.e. reduced form of plumbagin Escherichia coli nitrite + 5-hydroxy-2-methyl-naphthalene-1,4-dione + H2O
-
 ?
nitrate + quinol first enzyme involved in respiratory denitrification in prokaryotes Escherichia coli nitrite + quinone + H2O
-
 ?
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 Escherichia coli nitrite + quinone
-
 ?
nitrate + tetramethyl-p-benzoquinol i.e. duroquinol Escherichia coli nitrite + tetramethyl-p-benzoquinone + H2O
-
 ?

Synonyms

Synonyms Comment Organism
NarGHI
-
 Escherichia coli
nitrate reductase A
-
 Escherichia coli
quinol/nitrate oxidoreductase
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
cytochrome NarI is strongly associated with heme bD, Lys86 is required for its stabilization Escherichia coli
cytochrome bD NarI is strongly associated with heme bD, Lys86 is required for its stabilization Escherichia coli
additional information the semiquinone is located within the quinol oxidation site QD Escherichia coli