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[SoxY protein]-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-sulfosulfanyl-L-cysteine + 2 ferrocytochrome c + 2 H+
[SoxY protein]-S-sulfanyl-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + 2 ferrocytochrome c + 2 H+
[SoxY protein]-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-sulfosulfanyl-L-cysteine + 2 ferrocytochrome c + 2 H+
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-
-
?
[SoxY protein]-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-sulfosulfanyl-L-cysteine + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
[SoxY protein]-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-sulfosulfanyl-L-cysteine + 2 ferrocytochrome c + 2 H+
the enzyme is involved in chemotrophic sulfur-Oxidation
-
-
?
[SoxY protein]-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-sulfosulfanyl-L-cysteine + 2 ferrocytochrome c + 2 H+
the enzyme is involved in the oxidation of reduced inorganic sulfur compounds
-
-
?
[SoxY protein]-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-sulfosulfanyl-L-cysteine + 2 ferrocytochrome c + 2 H+
the enzyme is part of the Sox enzyme system, which participates in a bacterial thiosulfate oxidation pathway that produces sulfate
-
-
?
[SoxY protein]-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-sulfosulfanyl-L-cysteine + 2 ferrocytochrome c + 2 H+
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]-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-sulfosulfanyl-L-cysteine + 2 ferrocytochrome c + 2 H+
the enzyme catalyses two reactions in the pathway - early in the pathway it attaches a thiosulfate molecule to the sulfur atom of an L-cysteine of a SoxY protein; later it transfers a second thiosulfate molecule to a sulfane group that is already attached to the same cysteine residue
-
-
?
[SoxY protein]-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-sulfosulfanyl-L-cysteine + 2 ferrocytochrome c + 2 H+
the enzyme covalently links the sulfur substrate to the thiol of the cysteine-138 residue of the SoxY protein of the SoxYZ complex
-
-
?
[SoxY protein]-S-sulfanyl-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + 2 ferrocytochrome c + 2 H+
-
-
-
?
[SoxY protein]-S-sulfanyl-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
[SoxY protein]-S-sulfanyl-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + 2 ferrocytochrome c + 2 H+
the enzyme is involved in chemotrophic sulfur-Oxidation
-
-
?
[SoxY protein]-S-sulfanyl-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + 2 ferrocytochrome c + 2 H+
the enzyme is involved in the oxidation of reduced inorganic sulfur compounds
-
-
?
[SoxY protein]-S-sulfanyl-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + 2 ferrocytochrome c + 2 H+
the enzyme is part of the Sox enzyme system, which participates in a bacterial thiosulfate oxidation pathway that produces sulfate
-
-
?
[SoxY protein]-S-sulfanyl-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + 2 ferrocytochrome c + 2 H+
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-sulfanyl-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + 2 ferrocytochrome c + 2 H+
the enzyme catalyses two reactions in the pathway - early in the pathway it attaches a thiosulfate molecule to the sulfur atom of a L-cysteine of a SoxY protein; later it transfers a second thiosulfate molecule to a sulfane group that is already attached to the same cysteine residue
-
-
?
[SoxY protein]-S-sulfanyl-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + 2 ferrocytochrome c + 2 H+
the enzyme covalently links the sulfur substrate to the thiol of the cysteine-138 residue of the SoxY protein of the SoxYZ complex
-
-
?
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[SoxY protein]-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-sulfosulfanyl-L-cysteine + 2 ferrocytochrome c + 2 H+
[SoxY protein]-S-sulfanyl-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + 2 ferrocytochrome c + 2 H+
[SoxY protein]-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-sulfosulfanyl-L-cysteine + 2 ferrocytochrome c + 2 H+
the enzyme is involved in chemotrophic sulfur-Oxidation
-
-
?
[SoxY protein]-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-sulfosulfanyl-L-cysteine + 2 ferrocytochrome c + 2 H+
the enzyme is involved in the oxidation of reduced inorganic sulfur compounds
-
-
?
[SoxY protein]-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-sulfosulfanyl-L-cysteine + 2 ferrocytochrome c + 2 H+
the enzyme is part of the Sox enzyme system, which participates in a bacterial thiosulfate oxidation pathway that produces sulfate
-
-
?
[SoxY protein]-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-sulfosulfanyl-L-cysteine + 2 ferrocytochrome c + 2 H+
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-sulfanyl-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + 2 ferrocytochrome c + 2 H+
the enzyme is involved in chemotrophic sulfur-Oxidation
-
-
?
[SoxY protein]-S-sulfanyl-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + 2 ferrocytochrome c + 2 H+
the enzyme is involved in the oxidation of reduced inorganic sulfur compounds
-
-
?
[SoxY protein]-S-sulfanyl-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + 2 ferrocytochrome c + 2 H+
the enzyme is part of the Sox enzyme system, which participates in a bacterial thiosulfate oxidation pathway that produces sulfate
-
-
?
[SoxY protein]-S-sulfanyl-L-cysteine + thiosulfate + 2 ferricytochrome c
[SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + 2 ferrocytochrome c + 2 H+
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
-
-
?
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cytochrome
SoxXA is a heterodimeric c-type cytochrome
-
cytochrome c
cytochrome c complex
cytochrome c
SoxAX is a naturally occurring c-type cytochrome in which a thiolate-coordinated heme is identified
cytochrome c
SoxXA represents a novel type of periplasmic c-type cytochromes, with SoxX as a monoheme and SoxA as a hybrid diheme cytochrome c
heme
analysis of three heme sites. Heme-3 in the ferric state is characterized by a large EPR signal and has histidine and methionine axial heme iron ligands which are retained on reduction to the ferrous state. Heme-1 and heme-2 both have thiolate plus nitrogenous ligand sets in the ferric state and give rise to rhombic EPR spectra. Heme-1, whose ligands derive from cysteinate and histidine residues, remains ferric in the presence of dithionite ion. Ferric heme-2 exists with a preparation-dependent mixture of two different ligand sets, one being cysteinate/histidine, the other an unidentified pair with a weaker crystal-field strength. Upon reduction of the SoxAX complex with dithionite, a change occurs in the ligands of heme-2 in which the thiolate is either protonated or replaced by an unidentified ligand
heme
distance measurements between the three heme groups
heme
haemoprotein, the SoxAX active site contains a hemw with unprecedented cysteine persulfide (cysteine sulfane) coordination
heme
one heme is assigned to subunit SoxX and two hemes to subunit SoxA
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)
heme
SoxXA represents a novel type of periplasmic c-type cytochromes, with SoxX as a monoheme and SoxA as a hybrid diheme cytochrome c
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metabolism
the enzyme is involved in chemotrophic sulfur-Oxidation
metabolism
the enzyme is involved in the oxidation of reduced inorganic sulfur compounds
metabolism
the enzyme is involved in the pathway for thiosulphate oxidation
metabolism
the enzyme is involved in thiosulfate oxidation
metabolism
the enzyme is part of the Sox enzyme system, which participates in a bacterial thiosulfate oxidation pathway that produces sulfate
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
metabolism
the enzyme plays an essential role in photosynthetic thiosulfate and sulfide oxidation
metabolism
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the enzyme is involved in thiosulfate oxidation
-
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Cheesman, M.; Little, P.; Berks, B.
Novel heme ligation in a c-type cytochrome involved in thiosulfate oxidation EPR and MCD of SoxAX from Rhodovulum sulfidophilum
Biochemistry
40
10562-10569
2001
Rhodovulum sulfidophilum (Q939U1 AND Q939U4)
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brenda
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
Biochemistry
46
7804-7810
2007
Paracoccus pantotrophus (O33434 AND Q9LCV0), Paracoccus pantotrophus
brenda
Rother, D.; Friedrich, C.G.
The cytochrome complex SoxXA of Paracoccus pantotrophus is produced in Escherichia coli and functional in the reconstituted sulfur-oxidizing enzyme system
Biochim. Biophys. Acta
1598
65-73
2002
Paracoccus pantotrophus (O33434 AND Q9LCV0), Paracoccus pantotrophus
brenda
Bamford, V.; Bruno, S.; Rasmussen, T.; Appia-Ayme, C.; Cheesman, M.; Berks, B.; Hemmings, A.
Structural basis for the oxidation of thiosulfate by a sulfur cycle enzyme
EMBO J.
21
5599-5610
2002
Rhodovulum sulfidophilum (Q939U1 AND Q939U4), Rhodovulum sulfidophilum, Rhodovulum sulfidophilum DSM1374 (Q939U1 AND Q939U4)
brenda
Friedrich, C.G.; Quentmeier, A.; Bardischewsky, F.; Rother, D.; Kraft, R.; Kostka, S.; Prinz, H.
Novel genes coding for lithotrophic sulfur oxidation of Paracoccus pantotrophus GB17
J. Bacteriol.
182
4677-4687
2000
Paracoccus pantotrophus (O33434 AND Q9LCV0)
brenda
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
J. Struct. Biol.
152
229-234
2005
Paracoccus pantotrophus (O33434 AND Q9LCV0), Paracoccus pantotrophus
brenda
Hensen, D.; Sperling, D.; Trueper, H.G.; Brune, D.C.; Dahl, C.
Thiosulphate oxidation in the phototrophic sulphur bacterium Allochromatium vinosum
Mol. Microbiol.
62
794-810
2006
Allochromatium vinosum (Q1W3E4 AND Q1W3E5), Allochromatium vinosum
brenda
Grabarczyk, D.; Berks, B.
Intermediates in the Sox sulfur oxidation pathway are bound to a sulfane conjugate of the carrier protein SoxYZ
PLoS ONE
12
e0173395
2017
Paracoccus pantotrophus (O33434 AND Q9LCV0)
brenda
2.8.5.2 L-cysteine S-thiosulfotransferase
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