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Literature summary for 7.1.1.9 extracted from
- Role of tryptophan 121 in the soluble CuA domain of cytochrome c oxidase: structure and electron transfer studies (2003), Protein Eng., 16, 435-441.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| wild-type of soluble CuA domain and its mutants W121Y, DELTAW121 and W121L are expressed in Escherichia coli BL21 | Paracoccus versutus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| DELTAW121 | mutant of the soluble CuA domain, both the coordination structure of the CuA center and the secondary structure of the protein are changed significantly, the electron transfer activity with cytochrome c is inhibited severely | Paracoccus versutus |
| W121L | mutant of the soluble CuA domain, both the coordination structure of the CuA center and the secondary structure of the protein are changed significantly, the electron transfer activity with cytochrome c is inhibited severely | Paracoccus versutus |
| W121Y | mutant of the soluble CuA domain, stability decreases compared with the wild-type enzyme. The mutant keeps the same secondary structure as the wild-type protein, but can only transfer electrons with cytochrome c at a rate of one-seventh-fold | Paracoccus versutus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Paracoccus versutus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| wild-type of soluble CuA domain and its mutants W121Y, DELTAW121 and W121L, expressed in Escherichia coli | Paracoccus versutus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ferrocytochrome c + O2 | - |
Paracoccus versutus | ferricytochrome c + H2O | - |
? |  |
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Release 2023.1 (January 2023)
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