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Literature summary for 1.18.1.1 extracted from
- Redox and spectroscopic properties of the Escherichia coli nitric oxide-detoxifying system involving flavorubredoxin and its NADH-oxidizing redox partner (2005), J. Biol. Chem., 280, 34599-34608.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | study of truncated versions of enzyme, one consisting only of the rubredoxin molecule, the other of its flavodiiron structural core. analysis of interaction with the physiological partner NADH:flavorubredoxin oxidoreductase | Escherichia coli |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Iron | redox and spectroscopic properties of non-heme diiron site | Escherichia coli |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | enzyme interacts with its physiological partner NADH:flavorubredoxin oxidoreductase. Redox properties and mechanism of electron transfer are fine-tuned upon the interaction | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FMN | redox and spectroscopic properties of FMN site | Escherichia coli | |
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Release 2023.1 (January 2023)
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