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Literature summary for 7.1.1.9 extracted from

  • Merle, P.; Kadenbach, B.
    Kinetic and structural differences between cytochrome c oxidases from beef liver and heart (1982), Eur. J. Biochem., 125, 239-244.
    View publication on PubMed
Search for more literature for 7.1.1.9

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00012
-
 ferrocytochrome c heart enzyme, high affinity Km, in the presence of 0.04% deoxycholate and 0.04% lipid Bos taurus
0.00016
-
 ferrocytochrome c liver enzyme, high affinity Km, in the presence of 0.04% deoxycholate and 0.04% lipid Bos taurus
0.00071
-
 ferrocytochrome c heart enzyme, low affinity Km, in the presence of 0.04% deoxycholate and 0.04% lipid Bos taurus
0.00148
-
 ferrocytochrome c liver enzyme, low affinity Km, in the presence of 0.04% deoxycholate and 0.04% lipid Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phospholipoprotein
-
 Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Bos taurus
-

Substrates and Products (Substrate)

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