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Literature summary extracted from
- Probing the unusual oxidation/reduction behavior of Paracoccus pantotrophus cytochrome cd1 nitrite reductase by replacing a switchable methionine heme iron ligand with histidine (2006), Biochemistry, 45, 11208-11216.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.7.2.1 | M106H | inactive protein, the unusual highly cooperative and strongly hysteretic redox titration of the wild-type is lost in the mutant protein | Paracoccus pantotrophus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.7.2.1 | Paracoccus pantotrophus | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.7.2.1 | nitrite + ferrocytochrome c550 | - |
Paracoccus pantotrophus | NO + oxidized ferricytochrome c550 | - |
? |  |
| 1.7.2.1 | nitrite + reduced pseudoazurin | - |
Paracoccus pantotrophus | NO + oxidized pseudoazurin | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.7.2.1 | CuNIR | - |
Paracoccus pantotrophus |
| 1.7.2.1 | cytochrome cd1 nitrite reductase | - |
Paracoccus pantotrophus |
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Release 2023.1 (January 2023)
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