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Literature summary for 1.18.1.1 extracted from
- Electron transfer from flavin to iron in the Pseudomonas oleovorans rubredoxin reductase-rubredoxin electron transfer complex (1998), Biochemistry, 37, 15513-15522.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| overexpression in Escherichia coli | Pseudomonas oleovorans |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas oleovorans | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Pseudomonas oleovorans |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 86 | - |
rubredoxin-dependent reduction of cytochrome c | Pseudomonas oleovorans |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | both the nonphysiological 1Fe form of rubredoxin and the physiological 2 Fe form combine with rubredoxin reductase to form functional electron transfer complexes. The reductive half-reaction of the rubredoxin reductase occurs by a simple one-step mechanism in which oxidized enzyme is reduced to an enzyme-NAD+ charge-transfer species | Pseudomonas oleovorans | ? | - |
? |  |
| additional information | enzyme catalyzes rubredoxin-dependent reduction of cytochrome c in presence of NADH | Pseudomonas oleovorans | ? | - |
? | |
| NADH + oxidized rubredoxin | - |
Pseudomonas oleovorans | NAD+ + reduced rubredoxin | - |
? | |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADH | - |
Pseudomonas oleovorans | |
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