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Literature summary for 7.1.1.9 extracted from

  • De Vrij, W.; Poolman, B.; Konings, W.N.; Azzi, A.
    Purification, enzymatic properties, and reconstitution of cytochrome-c oxidase from Bacillus subtilis (1986), Methods Enzymol., 126, 159-173.
    View publication on PubMed
Search for more literature for 7.1.1.9

Activating Compound

Activating Compound Comment Organism Structure
Tween 80
-
 Bacillus subtilis

General Stability

General Stability Organism
ultrafiltration causes inactivation Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
azide 0.08 mM, 50% inhibition Bacillus subtilis
CN- 0.001 mM, 50% inhibition Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information enzyme exhibits positive cooperativity at low ionic strength, increasing the KCl concentration to 25 mM causes loss of cooperativity Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
22000
-
 1 * 57000 + 1 * 37000 + 1 * 22000, SDS-PAGE Bacillus subtilis
37000
-
 1 * 57000 + 1 * 37000 + 1 * 22000, SDS-PAGE Bacillus subtilis
57000
-
 1 * 57000 + 1 * 37000 + 1 * 22000, SDS-PAGE Bacillus subtilis
290000 315000 enzyme associated with detergents Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
method 1: cytochrome c affinity chromatography, ion-exchange, method 2: ammonium sulfate, anion exchange, gel filtration Bacillus subtilis

Renatured (Commentary)

Renatured (Comment) Organism
reconstitution Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ferrocytochrome c + O2 horse ferrocytochrome c Bacillus subtilis ferricytochrome c + H2O
-
 ?
ferrocytochrome c + O2 artificial electron donor: ascorbate/hexaamine ruthenium Bacillus subtilis ferricytochrome c + H2O
-
 ?
ferrocytochrome c + O2 artificial electron donor: ascorbate/N,N,N',N'-tetramethyl-p-phenylenediamine Bacillus subtilis ferricytochrome c + H2O
-
 ?
ferrocytochrome c + O2 + H+
-
 Bacillus subtilis ferricytochrome c + H2O
-
 r

Subunits

Subunits Comment Organism
trimer 1 * 57000 + 1 * 37000 + 1 * 22000, SDS-PAGE Bacillus subtilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
8 12 ferrocytochrome c in the presence of 0.1% dodecyl-beta-D-maltoside Bacillus subtilis