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Literature summary for 1.8.2.6 extracted from

  • Bardischewsky, F.; Quentmeier, A.; Rother, D.; Hellwig, P.; Kostka, S.; Friedrich, C.G.
    Sulfur dehydrogenase of Paracoccus pantotrophus the heme-2 domain of the molybdoprotein cytochrome c complex is dispensable for catalytic activity (2005), Biochemistry, 44, 7024-7034 .
    View publication on PubMed

Protein Variants

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 [Da] Molecular Weight Maximum [Da] Comment Organism
180000
-
density-gradient gel electrophoresis Paracoccus pantotrophus

Organism

Organism UniProt Comment Textmining
Paracoccus pantotrophus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
purification in presece of phenylmethylsulfonyl fluoride Paracoccus pantotrophus

Substrates and Products (Substrate)

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

Subunits Comment Organism
tetramer 2 * 43000, subunit SoxC, plus 2 * 47000, subunit SoxD, SDS-PAGE Paracoccus pantotrophus

Cofactor

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