Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
[SoxY protein]-L-cysteine + thiosulfate + 2 ferricytochrome c | Paracoccus pantotrophus | the enzyme is involved in chemotrophic sulfur-Oxidation | [SoxY protein]-S-sulfosulfanyl-L-cysteine + 2 ferrocytochrome c + 2 H+ | - |
? | |
[SoxY protein]-S-sulfanyl-L-cysteine + thiosulfate + 2 ferricytochrome c | Paracoccus pantotrophus | the enzyme is involved in chemotrophic sulfur-Oxidation | [SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + 2 ferrocytochrome c + 2 H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Paracoccus pantotrophus | O33434 AND Q9LCV0 | O33434: subunit SoxA, Q9LCV0: subunit SoxX | - |
Purification (Comment) | Organism |
---|---|
- |
Paracoccus pantotrophus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
[SoxY protein]-L-cysteine + thiosulfate + 2 ferricytochrome c | - |
Paracoccus pantotrophus | [SoxY protein]-S-sulfosulfanyl-L-cysteine + 2 ferrocytochrome c + 2 H+ | - |
? | |
[SoxY protein]-L-cysteine + thiosulfate + 2 ferricytochrome c | the enzyme is involved in chemotrophic sulfur-Oxidation | Paracoccus pantotrophus | [SoxY protein]-S-sulfosulfanyl-L-cysteine + 2 ferrocytochrome c + 2 H+ | - |
? | |
[SoxY protein]-S-sulfanyl-L-cysteine + thiosulfate + 2 ferricytochrome c | - |
Paracoccus pantotrophus | [SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + 2 ferrocytochrome c + 2 H+ | - |
? | |
[SoxY protein]-S-sulfanyl-L-cysteine + thiosulfate + 2 ferricytochrome c | the enzyme is involved in chemotrophic sulfur-Oxidation | Paracoccus pantotrophus | [SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + 2 ferrocytochrome c + 2 H+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
heterodimer | - |
Paracoccus pantotrophus |
Synonyms | Comment | Organism |
---|---|---|
SoxXA | - |
Paracoccus pantotrophus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | presence of three heme groups, one of which (heme 3) has a His/Met axial coordination and is located on the SoxX subunit. Heme 1 and heme 2 are located on the SoxA subunit, both of which have EPR parameters characteristic for an axial His/thiolate coordination. The midpoint potentials of heme 3 (Em3: +189 mV) and heme 2 (Em2: -432 mV) are determined. Heme 1 is not reducible even with 20 mM titanium(III) citrate. The Em2 midpoint potential is pH dependent. It is proposed that heme 2 participates in the catalysis and that the cysteine persulfide ligation leads to the unusually low redox potential (-436 mV) | Paracoccus pantotrophus |
General Information | Comment | Organism |
---|---|---|
metabolism | the enzyme is involved in chemotrophic sulfur-Oxidation | Paracoccus pantotrophus |