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Literature summary extracted from

  • Silvestrini, M.C.; Falcinelli, S.; Ciabatti, I.; Cutruzzola, F.; Brunori, M.
    Pseudomonas aeruginosa nitrite reductase (or cytochrome oxidase): an overview (1994), Biochimie, 76, 641-654.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.7.2.1 Subtilisin species of 48000 Da which contains the d1 but not the c heme Pseudomonas aeruginosa

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.7.2.1 epression in Pseudomonas putida Pseudomonas aeruginosa

General Stability

EC Number General Stability Organism
1.7.2.1 urea, 4 M, 9% of initial activity, 6 M, no dissociation into subunits but irreversible inactivation Pseudomonas aeruginosa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7.2.1 0.028
-
 O2
-
 Pseudomonas aeruginosa
1.7.2.1 0.0305
-
 ferricytochrome c succinylated monomeric enzyme Pseudomonas aeruginosa
1.7.2.1 0.053
-
 NO2-
-
 Pseudomonas aeruginosa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.7.2.1 periplasm
-
 Paracoccus denitrificans
-
-
1.7.2.1 periplasm
-
 Pseudomonas aeruginosa
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.7.2.1 60204
-
 2 * 60204, deduced from amino acid sequence Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.7.2.1 ferrocytochrome c-551 + O2 Pseudomonas aeruginosa
-
 ferricytochrome c-551 + H2O
-
 ?
1.7.2.1 NO2- + ferrocytochrome c Pseudomonas aeruginosa probably most dominant activity in vivo NO + ferricytochrome c
-
 ?
1.7.2.1 reduced azurin + O2 Pseudomonas aeruginosa not known whether azurin donates electrons in vivo in parallel or sequentially to cytochrome c551 oxidized azurin + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.7.2.1 Alcaligenes faecalis
-
-
-
1.7.2.1 Halomonas halodenitrificans
-
-
-
1.7.2.1 Paracoccus denitrificans
-
-
-
1.7.2.1 Paracoccus pantotrophus
-
-
-
1.7.2.1 Pseudomonas aeruginosa
-
-
-
1.7.2.1 Pseudomonas stutzeri
-
-
-
1.7.2.1 Thiobacillus denitrificans
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.7.2.1
-
 Alcaligenes faecalis
1.7.2.1
-
 Pseudomonas stutzeri
1.7.2.1
-
 Paracoccus pantotrophus
1.7.2.1
-
 Halomonas halodenitrificans
1.7.2.1 monomeric enzyme prepared by controlled succinylation of the native dimer Pseudomonas aeruginosa
1.7.2.1 recombinant enzyme, contains only the c heme Pseudomonas aeruginosa

Reaction

EC Number Reaction Comment Organism Reaction ID
1.7.2.1 nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+ proposed reaction mechanism Pseudomonas aeruginosa
a

Renatured (Commentary)

EC Number Renatured (Comment) Organism
1.7.2.1
-
 Pseudomonas aeruginosa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.2.1 ferrocytochrome c-551 + NO2-
-
 Paracoccus denitrificans NO + ferricytochrome c-551
-
 ?
1.7.2.1 ferrocytochrome c-551 + NO2-
-
 Pseudomonas aeruginosa NO + ferricytochrome c-551
-
 ?
1.7.2.1 ferrocytochrome c-551 + O2
-
 Paracoccus denitrificans H2O + ferricytochrome c-551
-
 ?
1.7.2.1 ferrocytochrome c-551 + O2 inactive with eukaryotic cytochromes c Pseudomonas aeruginosa H2O + ferricytochrome c-551
-
 ?
1.7.2.1 ferrocytochrome c-551 + O2
-
 Pseudomonas aeruginosa ferricytochrome c-551 + H2O
-
 ?
1.7.2.1 nitric oxide + H2O + ferricytochrome c
-
 Pseudomonas aeruginosa nitrite + ferrocytochrome c + H+
-
 r
1.7.2.1 NO2- + ferrocytochrome c probably most dominant activity in vivo Pseudomonas aeruginosa NO + ferricytochrome c
-
 ?
1.7.2.1 reduced azurin + O2 not known whether azurin donates electrons in vivo in parallel or sequentially to cytochrome c551 Pseudomonas aeruginosa oxidized azurin + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.7.2.1 dimer
-
 Pseudomonas stutzeri
1.7.2.1 dimer
-
 Thiobacillus denitrificans
1.7.2.1 dimer 2 * 60204, deduced from amino acid sequence Pseudomonas aeruginosa

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.7.2.1 1.33
-
 ferricytochrome c succinylated monomeric enzyme Pseudomonas aeruginosa

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.2.1 heme c
-
 Pseudomonas stutzeri
1.7.2.1 heme c c heme is the electron accepting pole of the enzyme Pseudomonas aeruginosa