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Literature summary extracted from

  • Chan, S.I.; Li, P.M.
    Cytochrome c oxidase: understanding natures design of a proton pump (1990), Biochemistry, 29, 1-12.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.1.1.9
-
 Paracoccus denitrificans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.1.1.9 Cu
-
 Mammalia
7.1.1.9 Cu CuB located in subunit I, electron flow from ferrocytochrome c to binuclear center Paracoccus denitrificans
7.1.1.9 Cu CuB located in subunit I, electron flow from ferrocytochrome c to binuclear center Bacteria
7.1.1.9 Cu CuB located in subunit I, electron flow from ferrocytochrome c to binuclear center eukaryota
7.1.1.9 Cu CuA located in subunit II, binding of O2 and reduction Paracoccus denitrificans
7.1.1.9 Cu CuA located in subunit II, binding of O2 and reduction Bacteria
7.1.1.9 Cu CuA located in subunit II, binding of O2 and reduction eukaryota
7.1.1.9 Fe
-
 Mammalia
7.1.1.9 Fe
-
 Bacteria
7.1.1.9 Fe
-
 eukaryota
7.1.1.9 Mg
-
 Mammalia
7.1.1.9 additional information all redox-active metal centers are contained in subunits I and II eukaryota

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.9 Bacteria
-
-
-
7.1.1.9 eukaryota
-
-
-
7.1.1.9 Mammalia
-
-
-
7.1.1.9 Paracoccus denitrificans
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
7.1.1.9 4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O mechanism of O2 reduction Bacteria
a
7.1.1.9 4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O mechanism of O2 reduction eukaryota
a
7.1.1.9 4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O proposal for complete turnover cycle, i.e. intramolecular electron transfer, O2 reduction and proton pumping Bacteria
a
7.1.1.9 4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O proposal for complete turnover cycle, i.e. intramolecular electron transfer, O2 reduction and proton pumping eukaryota
a
7.1.1.9 4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O mechanism of proton pumping Mammalia
a
7.1.1.9 4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O mechanism of proton pumping Bacteria
a
7.1.1.9 4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O mechanism of proton pumping eukaryota
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.9 ferrocytochrome c + O2
-
 Paracoccus denitrificans ferricytochrome c + H2O
-
 ?
7.1.1.9 ferrocytochrome c + O2 proton translocation across eukaryotic mitochondrial and prokyryotic cytoplasmic membrane, overview proposed mechanims Bacteria ferricytochrome c + H2O
-
 ?
7.1.1.9 ferrocytochrome c + O2 proton translocation across eukaryotic mitochondrial and prokyryotic cytoplasmic membrane, overview proposed mechanims eukaryota ferricytochrome c + H2O
-
 ?
7.1.1.9 ferrocytochrome c + O2 + H+
-
 Bacteria ferricytochrome c + H2O
-
 r
7.1.1.9 ferrocytochrome c + O2 + H+
-
 eukaryota ferricytochrome c + H2O
-
 r

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
7.1.1.9 30 600 ferrocytochrome c
-
 Bacteria
7.1.1.9 30 600 ferrocytochrome c
-
 eukaryota

pH Range

EC Number pH Minimum pH Maximum Comment Organism
7.1.1.9 additional information
-
 redox potential of cytochrome a is pH dependent eukaryota

Cofactor

EC Number Cofactor Comment Organism Structure
7.1.1.9 heme a
-
 Paracoccus denitrificans
7.1.1.9 heme a
-
 Mammalia
7.1.1.9 heme a located in subunit I Bacteria
7.1.1.9 heme a located in subunit I eukaryota
7.1.1.9 Heme a3
-
 Mammalia
7.1.1.9 Heme a3 located in subunit I Paracoccus denitrificans
7.1.1.9 Heme a3 located in subunit I Bacteria
7.1.1.9 Heme a3 located in subunit I eukaryota