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Literature summary extracted from

  • Dambe, T.; Quentmeier, A.; Rother, D.; Friedrich, C.; Scheidig, A.J.
    Structure of the cytochrome complex SoxXA of Paracoccus pantotrophus, a heme enzyme initiating chemotrophic sulfur oxidation (2005), J. Struct. Biol., 152, 229-234 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.8.5.2 hanging drop vapour diffusion method, the crystal structure of the c-type cytochrome complex SoxXA can be solved by molecular replacement and refined to a resolution of 1.9 A identifying the axial heme-iron coordination involving an unusual Cys-251 thiolate of heme2 Paracoccus pantotrophus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

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 part of the sulfur-oxidizing enzyme system which oxidizes hydrogen sulfide, sulfur, thiosulfate or sulfite and transfers the gained electrons to the respiratory chain [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 part of the sulfur-oxidizing enzyme system which oxidizes hydrogen sulfide, sulfur, thiosulfate or sulfite and transfers the gained electrons to the respiratory chain [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
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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 the enzyme is part of the sulfur-oxidizing enzyme system which oxidizes hydrogen sulfide, sulfur, thiosulfate or sulfite and transfers the gained electrons to the respiratory chain 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 covalently links the sulfur substrate to the thiol of the cysteine-138 residue of the SoxY protein of the SoxYZ complex 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 the enzyme is part of the sulfur-oxidizing enzyme system which oxidizes hydrogen sulfide, sulfur, thiosulfate or sulfite and transfers the gained electrons to the respiratory chain 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 covalently links the sulfur substrate to the thiol of the cysteine-138 residue of the SoxY protein of the SoxYZ complex 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 complex SoxXA
-
Paracoccus pantotrophus

Cofactor

EC Number Cofactor Comment Organism Structure
2.8.5.2 cytochrome c cytochrome c complex Paracoccus pantotrophus
2.8.5.2 heme distance measurements between the three heme groups Paracoccus pantotrophus

General Information

EC Number General Information Comment Organism
2.8.5.2 metabolism the enzyme is part of the sulfur-oxidizing enzyme system which oxidizes hydrogen sulfide, sulfur, thiosulfate or sulfite and transfers the gained electrons to the respiratory chain Paracoccus pantotrophus