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Literature summary extracted from
- Structure and function of cytochrome c oxidase (1990), Annu. Rev. Biochem., 59, 569-596.
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.1.1.9 | Cu | proposed third copper center, CuX, may result from impurities | eukaryota |  |
| 7.1.1.9 | Cu | location in subunits | Mammalia | |
| 7.1.1.9 | Cu | location in subunits | Bacteria | |
| 7.1.1.9 | Cu | location in subunits | eukaryota | |
| 7.1.1.9 | Cu | location in subunits | Saccharomyces cerevisiae | |
| 7.1.1.9 | Fe | - |
Mammalia | |
| 7.1.1.9 | Fe | - |
Bacteria | |
| 7.1.1.9 | Fe | - |
eukaryota | |
| 7.1.1.9 | Fe | - |
Saccharomyces cerevisiae | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.1.1.9 | ferrocytochrome c + O2 | Bacteria | - |
ferricytochrome c + H2O | - |
? | |
| 7.1.1.9 | ferrocytochrome c + O2 | eukaryota | - |
ferricytochrome c + H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 7.1.1.9 | Bacteria | - |
- |
- |
| 7.1.1.9 | Bacteria | - |
overview | - |
| 7.1.1.9 | eukaryota | - |
- |
- |
| 7.1.1.9 | Mammalia | - |
overview | - |
| 7.1.1.9 | Saccharomyces cerevisiae | - |
overview | - |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 7.1.1.9 | 4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O | reaction mechanism | Bacteria | |
| 7.1.1.9 | 4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O | reaction mechanism | eukaryota | |
| 7.1.1.9 | 4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O | mechanism of proton pumping | Mammalia | |
| 7.1.1.9 | 4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O | mechanism of proton pumping | Bacteria | |
| 7.1.1.9 | 4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O | mechanism of proton pumping | eukaryota | |
| 7.1.1.9 | 4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O | mechanism of proton pumping | Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.1.1.9 | ferrocytochrome c + O2 | - |
Bacteria | ferricytochrome c + H2O | - |
? | |
| 7.1.1.9 | ferrocytochrome c + O2 | - |
eukaryota | ferricytochrome c + H2O | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 7.1.1.9 | More | - |
Mammalia |
| 7.1.1.9 | More | - |
Saccharomyces cerevisiae |
| 7.1.1.9 | More | it is suggested that the mitochondrial encoded subunits I, II and III are the catalytic core of the enzyme | eukaryota |
| 7.1.1.9 | oligomer | - |
Mammalia |
| 7.1.1.9 | oligomer | - |
Bacteria |
| 7.1.1.9 | oligomer | - |
eukaryota |
| 7.1.1.9 | oligomer | - |
Saccharomyces cerevisiae |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.1.1.9 | heme a | - |
Mammalia | |
| 7.1.1.9 | heme a | - |
Bacteria | |
| 7.1.1.9 | heme a | - |
eukaryota | |
| 7.1.1.9 | heme a | - |
Saccharomyces cerevisiae | |
| 7.1.1.9 | Heme a3 | - |
Mammalia | |
| 7.1.1.9 | Heme a3 | - |
Bacteria | |
| 7.1.1.9 | Heme a3 | - |
eukaryota | |
| 7.1.1.9 | Heme a3 | - |
Saccharomyces cerevisiae | |
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