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Literature summary for 7.1.1.9 extracted from
- Kinetic resolution of a tryptophan-radical intermediate in the reaction cycle of Paracoccus denitrificans cytochrome c oxidase (2007), J. Biol. Chem., 282, 31580-31591.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Cu2+ | CuA and heme a are in electronic equilibrium acting as a redox pair. Trp-272 is the direct reductant either to the heme a3 oxoferryl species or to CuB2+ | Paracoccus denitrificans |  |
| Mn2+ | - |
Paracoccus denitrificans | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Paracoccus denitrificans | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| reduced cytochrome aa3 + O2 + H+ | formation of a tryptophan-radical intermediate (tryptophan neutral radical of the strictly conserved Trp-272). The formation of the Trp-272 constitutes the major rate-determining step of the catalytic cycle | Paracoccus denitrificans | oxidized cytochrome aa3 + H2O | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CCO | - |
Paracoccus denitrificans |
| cytochrome c oxidase | - |
Paracoccus denitrificans |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| heme a | CuA and heme a are in electronic equilibrium acting as a redox pair | Paracoccus denitrificans | |
| Heme a3 | Trp-272 is the direct reductant either to the heme a3 oxoferryl species or to CuB2+ | Paracoccus denitrificans | |
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Release 2023.1 (January 2023)
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