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Literature summary for 7.1.1.9 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

Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

Metals/Ions Comment Organism Structure
Cu
-
Cytobacillus firmus

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Cytobacillus firmus
-
-
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
heme a
-
Cytobacillus firmus