PMID:21147779

Zander U, Faust A, Klink BU, de Sanctis D, Panjikar S, Quentmeier A, Bardischewsky F, Friedrich CG, Scheidig AJ

Structural basis for the oxidation of protein-bound sulfur by the sulfur cycle molybdohemo-enzyme sulfane dehydrogenase SoxCD.

J Biol Chem 286:8349-60 (2011)
DOI:10.1074/jbc.M110.193631

Oxidoreductases;
Acting on a sulfur group of donors;
With a cytochrome as acceptor
BRITE hierarchy

[SoxY protein]-S-disulfanyl-L-cysteine:cytochrome-c oxidoreductase

[SoxY protein]-S-disulfanyl-L-cysteine + 6 ferricytochrome c + 3 H2O = [SoxY protein]-S-sulfosulfanyl-L-cysteine + 6 ferrocytochrome c + 6 H+ [RN:R11971]

R11971
Reaction

[SoxY protein]-S-disulfanyl-L-cysteine [CPD:C21814];
ferricytochrome c [CPD:C00125];
H2O [CPD:C00001]

The enzyme is part of the Sox enzyme system, which participates in a bacterial thiosulfate oxidation pathway that produces sulfate. The enzyme from the bacterium Paracoccus pantotrophus contains a molybdoprotein component and a diheme c-type cytochrome component. The enzyme successively oxidizes the outer sulfur atom in [SoxY protein]-S-disulfanyl-L-cysteine, using three water molecules and forming [SoxY protein]-S-sulfosulfanyl-L-cysteine. During the process, six electrons are transferred to the electron chain via cytochrome c.

EC 1.8.2.6 created 2018

1  [PMID:11425697]

Friedrich CG, Rother D, Bardischewsky F, Quentmeier A, Fischer J

Oxidation of reduced inorganic sulfur compounds by bacteria: emergence of a common mechanism?

Appl Environ Microbiol 67:2873-82 (2001)
DOI:10.1128/AEM.67.7.2873-2882.2001

2  [PMID:15865447]

Bardischewsky F, Quentmeier A, Rother D, Hellwig P, Kostka S, Friedrich CG

Sulfur dehydrogenase of Paracoccus pantotrophus: the heme-2 domain of the molybdoprotein cytochrome c complex is dispensable for catalytic activity.

Biochemistry 44:7024-34 (2005)
DOI:10.1021/bi047334b

3  [PMID:28257465]

Grabarczyk DB, Berks BC

Intermediates in the Sox sulfur oxidation pathway are bound to a sulfane conjugate of the carrier protein SoxYZ.

PLoS One 12:e0173395 (2017)
DOI:10.1371/journal.pone.0173395