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Literature summary for 2.8.5.2 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
Search for more literature for 2.8.5.2

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

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 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+
-
 ?
[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+
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 ?

Organism

Organism UniProt Comment Textmining
Paracoccus pantotrophus O33434 AND Q9LCV0 O33434: subunit SoxA, Q9LCV0: subunit SoxX
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[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+
-
 ?
[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+
-
 ?
[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+
-
 ?
[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

Subunits Comment Organism
heterodimer
-
 Paracoccus pantotrophus

Synonyms

Synonyms Comment Organism
complex SoxXA
-
 Paracoccus pantotrophus

Cofactor

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

General Information

General Information Comment Organism
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