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Literature summary extracted from

  • Kitada, M.; Krulwich, T.A.
    Purification and characterization of the cytochrome oxidase from alkalophilic Bacillus firmus RAB (1984), J. Bacteriol., 158, 963-966.
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.1.1.9 Cu
-
 Cytobacillus firmus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
7.1.1.9 14000
-
 1 * 56000 + 1 * 40000 + 1 * 14000, SDS-PAGE Cytobacillus firmus
7.1.1.9 40000
-
 1 * 56000 + 1 * 40000 + 1 * 14000, SDS-PAGE Cytobacillus firmus
7.1.1.9 56000
-
 1 * 56000 + 1 * 40000 + 1 * 14000, SDS-PAGE Cytobacillus firmus

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.9 Cytobacillus firmus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.1.1.9 Triton X-100, DEAE-Sepharose, hydroxyapatite, Sephadex G-200 Cytobacillus firmus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
7.1.1.9 12
-
-
 Cytobacillus firmus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.9 ferrocytochrome c + O2 Saccharomyces cerevisiae cytochrome c Cytobacillus firmus ferricytochrome c + H2O
-
 ?
7.1.1.9 ferrocytochrome c + O2 horse ferrocytochrome c Cytobacillus firmus ferricytochrome c + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
7.1.1.9 trimer 1 * 56000 + 1 * 40000 + 1 * 14000, SDS-PAGE Cytobacillus firmus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
7.1.1.9 6
-
 purified enzyme Cytobacillus firmus

Cofactor

EC Number Cofactor Comment Organism Structure
7.1.1.9 heme a
-
 Cytobacillus firmus