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Literature summary for extracted from

  • Bertero, M.G.; Rothery, R.A.; Boroumand, N.; Palak, M.; Blasco, F.; Ginet, N.; Weiner, J.H.; Strynadka, N.C.
    Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A (2005), J. Biol. Chem., 280, 14836-14843.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
the crystal structure of Escherichia coli nitrate reductase A in complex with pentachlorophenol is determined to 2.0 A of resolution Escherichia coli

Protein Variants

Protein Variants Comment Organism
K86A mutant has a lower plumbagin:nitrate oxidoreductase activity than the wild-type enzyme, 10/s compared with 68/s, respectively Escherichia coli


Inhibitors Comment Organism Structure
2-n-heptyl-4-hydroxyquinoline N-oxide
Escherichia coli
Pentachlorophenol mixed inhibition Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5-hydroxy-2-methyl-naphthalene-1,4-diol pH 7.0 Escherichia coli


Organism UniProt Comment Textmining
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 i.e. plumbagin ?


Synonyms Comment Organism
Escherichia coli
quinol:nitrate oxidoreductase
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
nitrate mutant enzyme K86A Escherichia coli
nitrate wild-type enzyme Escherichia coli


Cofactor Comment Organism Structure
additional information molecular characterization of a quinol binding and oxidation site (Q-site) in NarGHI Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
Pentachlorophenol pH 7.0, competitive inhibition constant Escherichia coli
Pentachlorophenol pH 7.0, uncompetitive inhibition constant Escherichia coli

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
pH 7.0 Escherichia coli Pentachlorophenol
pH 7.0 Escherichia coli 2-n-heptyl-4-hydroxyquinoline N-oxide