Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of a mutant lacking the heme-2 domain. Exclusively the heme-1 domain of SoxD is required for activity, substrate specificity, and electron yield of the sulfur-oxidizing system, kinetic data are similar to wild-type | Paracoccus pantotrophus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
180000 | - |
density-gradient gel electrophoresis | Paracoccus pantotrophus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Paracoccus pantotrophus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
purification in presece of phenylmethylsulfonyl fluoride | Paracoccus pantotrophus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the complete sulfur-oxidizing enzyme system reconstituted from subunits Sox(CD)2, SoxYZ, SoxXA, and SoxB accepts hydrogen sulfide, sulfur, thiosulfate, and sulfite for reduction of horse cytochrome c | Paracoccus pantotrophus | ? | - |
? | |
[SoxY protein]-S-disulfanyl-L-cysteine + 6 ferricytochrome c + 3 H2O | - |
Paracoccus pantotrophus | [SoxY protein]-S-sulfosulfanyl-L-cysteine + 6 ferrocytochrome c + 6 H+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | 2 * 43000, subunit SoxC, plus 2 * 47000, subunit SoxD, SDS-PAGE | Paracoccus pantotrophus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | subunit SoxD harbors two heme domains. 3.65 mol of heme per mol of enzyme tetramer. Exclusively the heme-1 domain of SoxD is required for activity, substrate specificity, and electron yield of the sulfur-oxidizing system | Paracoccus pantotrophus |