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Literature summary for 1.7.2.2 extracted from

  • van Wonderen, J.H.; Burlat, B.; Richardson, D.J.; Cheesman, M.R.; Butt, J.N.
    The nitric oxide reductase activity of cytochrome c nitrite reductase from Escherichia coli (2008), J. Biol. Chem., 283, 9587-9594.
    View publication on PubMed
Search for more literature for 1.7.2.2

Protein Variants

Protein Variants Comment Organism
additional information anaerobically grown Escherichia coli nrf mutants are more sensitive to NO radicals than the parent strain Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
CN- cyanide is a potent inhibitor of NrfA nitrite and hydroxylamine reductase activities Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.012
-
 nitrite pH 7.0, 20°C, reduction Escherichia coli
0.3
-
 NO radical pH 7.0, 20°C, reduction Escherichia coli
60.4
-
 hydroxylamine pH 7.0, 20°C, reduction Escherichia coli

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli NrfA from Escherichia coli has a well established role in the respiratory reduction of nitrite to ammonium, it might also participate in NO radical detoxification, detoxifying exogenously generated NO radical encountered during invasion of a human host, overview ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 quantitation of steady-state NrfA reduction of NO radical, nitrite, and hydroxylamine Escherichia coli
25
-
 nitrite reduction Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hydroxylamine + reduced methyl viologen low activity Escherichia coli ?
-
 ?
additional information NrfA from Escherichia coli has a well established role in the respiratory reduction of nitrite to ammonium, it might also participate in NO radical detoxification, detoxifying exogenously generated NO radical encountered during invasion of a human host, overview Escherichia coli ?
-
 ?
additional information the enzyme shows a common site for reduction of all three substrates as axial ligands to the lysine-coordinated NrfA heme rather than nonspecific NO radical reduction at one of the four His-His coordinated hemes also present in each NrfA subunit. NO radical reduction is initiated at similar potentials to NrfA-catalyzed reduction of nitrite and hydroxylamine Escherichia coli ?
-
 ?
nitrite + reduced methyl viologen
-
 Escherichia coli NH3 + H2O + oxidized methyl viologen
-
 ?
NO radical + reduced methyl viologen
-
 Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
cytochrome c nitrite reductase
-
 Escherichia coli
NrfA
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20
-
 assay at Escherichia coli

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
4 25 NrfA activity increases when the temperature is raised from 4°C to 25°C Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
700
-
 nitrite pH 7.0, 20°C, reduction Escherichia coli
840
-
 NO radical pH 7.0, 20°C, reduction Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
 pH dependence of NrfA at 4-25°C, overview Escherichia coli

Cofactor

Cofactor Comment Organism Structure
heme
-
 Escherichia coli
methyl viologen used as the electron donor, reduced with dithionite, artificial cofactor Escherichia coli