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Literature summary for 1.8.2.6 extracted from
- Structural insight into SoxC and SoxD interaction and their role in electron transport process in the novel global sulfur cycle in Paracoccus pantotrophus (2005), Biochem. Biophys. Res. Commun., 331, 1107-1113 .
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| homology modeling of structure. SoxD belongs to the di-heme cytochrome c family of electron transport proteins whereas soxC gene product (SoxC) is a sulfur dehydrogenase | Paracoccus pantotrophus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Molybdenum | subunit SoxC has a Mo-cofactor containing domain | Paracoccus pantotrophus |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Paracoccus pantotrophus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | subunit SoxC first comes in contact with water and thereby breaks down the oxygen-hydrogen bond in water. The oxygen, which is liberated as oxide anion (O2-), then forms covalent bond with the protein bound sulfur atom and liberates two electrons, which are then taken up by the di-heme cytochrome c protein SoxD | Paracoccus pantotrophus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | dimerization of subunit SoxD helps to bring the two distant heme groups in close proximity, which helps in the transport of electrons efficiently from one part of the protein to the other part, structure modeling data. subunits SoxC and SoxD interact strongly with each other | Paracoccus pantotrophus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| SoxCD | - |
Paracoccus pantotrophus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| cytochrome c | the cytochrome c motifs of subunit SoxD are buried in the protein core | Paracoccus pantotrophus | |
| heme | the side chains of His297, Arg316 and the main chain nitrogen atoms of Ser327 and Lys360 are involved in H-bonding with the oxygen atoms of the heme propionate group | Paracoccus pantotrophus | |
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