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Literature summary for 1.97.1.9 extracted from
- Quinol-cytochrome c oxidoreductase and cytochrome c4 mediate electron transfer during selenate respiration in Thauera selenatis (2010), J. Biol. Chem., 285, 18433-18442.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Molybdenum | - |
Thauera selenatis |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thauera selenatis | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| selenate + reduced cytc-Ts4 | a c-type cytochrom is purified and shown to donate electrons to SerABC in vitro. Redox potentiometry, combined with UV-visible spectroscopy, show that cytc-Ts4 is a diheme cytochrome with a redox potential of +/-282 mV, and both hemes are predicted to have His-Met ligation | Thauera selenatis | selenite + H2O + oxidized cytc-Ts4 | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| selenate reductase | - |
Thauera selenatis |
| SerABC | - |
Thauera selenatis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Thauera selenatis |
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