Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 7.1.1.9 extracted from

  • Geier, B.M.; Schagger, H.; Ortwein, C.; Link, T.A.; Hagen, W.R.; Brandt, U.; Von Jagow, G.
    Kinetic properties and ligand binding of the eleven-subunit cytochrome-c oxidase from Saccharomyces cerevisiae isolated with a novel large-scale purification method (1995), Eur. J. Biochem., 227, 296-302.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00132
-
ferrocytochrome c horse heart cytochrome c, high-affinity Km, 30 mM ionic strength Saccharomyces cerevisiae
0.0153
-
ferrocytochrome c horse heart cytochrome c, 100 mM ionic strength Saccharomyces cerevisiae
0.13
-
ferrocytochrome c horse heart cytochrome c, low-affinity Km, 30 mM ionic strength Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial membrane
-
Saccharomyces cerevisiae 31966
-

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
hydroxyapatite, Sepharose CL-6B Saccharomyces cerevisiae

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
More enzyme complex contains eleven rather than twelve subunits Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1500
-
ferrocytochrome c horse heart cytochrome c Saccharomyces cerevisiae