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Literature summary extracted from

  • Reijerse, E.J.; Sommerhalter, M.; Hellwig, P.; Quentmeier, A.; Rother, D.; Laurich, C.; Bothe, E.; Lubitz, W.; Friedrich, C.G.
    The unusal redox centers of SoxXA, a novel c-type heme-enzyme essential for chemotrophic sulfur-oxidation of Paracoccus pantotrophus (2007), Biochemistry, 46, 7804-7810 .
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.8.5.2 [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+
-
 ?
2.8.5.2 [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

EC Number Organism UniProt Comment Textmining
2.8.5.2 Paracoccus pantotrophus O33434 AND Q9LCV0 O33434: subunit SoxA, Q9LCV0: subunit SoxX
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.8.5.2
-
 Paracoccus pantotrophus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.5.2 [SoxY protein]-L-cysteine + thiosulfate + 2 ferricytochrome c
-
 Paracoccus pantotrophus [SoxY protein]-S-sulfosulfanyl-L-cysteine + 2 ferrocytochrome c + 2 H+
-
 ?
2.8.5.2 [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+
-
 ?
2.8.5.2 [SoxY protein]-S-sulfanyl-L-cysteine + thiosulfate + 2 ferricytochrome c
-
 Paracoccus pantotrophus [SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + 2 ferrocytochrome c + 2 H+
-
 ?
2.8.5.2 [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

EC Number Subunits Comment Organism
2.8.5.2 heterodimer
-
 Paracoccus pantotrophus

Synonyms

EC Number Synonyms Comment Organism
2.8.5.2 SoxXA
-
 Paracoccus pantotrophus

Cofactor

EC Number Cofactor Comment Organism Structure
2.8.5.2 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

EC Number General Information Comment Organism
2.8.5.2 metabolism the enzyme is involved in chemotrophic sulfur-Oxidation Paracoccus pantotrophus