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Information on EC 1.13.11.55 - sulfur oxygenase/reductase
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1.13.11.55 sulfur oxygenase/reductaseIUBMB Comments
This enzyme, which is found in thermophilic microorganisms, contains one mononuclear none-heme iron centre per subunit. Elemental sulfur is both the electron donor and one of the two known acceptors, the other being oxygen. Thiosulfate is also observed as a product, but is likely formed non-enzymically by a reaction between sulfite and sulfur . This enzyme differs from EC 1.13.11.18, sulfur dioxygenase and EC 1.12.98.4, sulfhydrogenase, in that both activities occur simultaneously.
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Word Map
- 1.13.11.55
- ambivalens
- thiosulfate
- acidianus
-
thermoacidophilic
-
hollow
-
non-heme
-
disproportionation
- acidithiobacillus
-
acidophil
- sulfobacillus
- tetrathionate
- tokodaii
-
heterodisulfide
-
bioleaching
- degradation
-
low-potential
- caldus
- pharmacology
- industry
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
AaSOR, SAMN00768000_1627, SAMN00768000_1798, SOR, SOR protein, SOR-AT, sulfur oxygenase, sulfur oxygenase reductase, sulfur oxygenase reductases, sulfuroxygenasereductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SAMN00768000_1627
SAMN00768000_1798
SOR
SOR protein
sulfur oxygenase
sulfur oxygenase reductase
sulfur oxygenase reductases
sulfuroxygenasereductase
sulphur oxygenase reductase
TpSOR
TPY_0405
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4 sulfur + 4 H2O + O2 = 2 hydrogen sulfide + 2 sulfite
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
sulfur:oxygen oxidoreductase (hydrogen-sulfide- and sulfite-forming)
This enzyme, which is found in thermophilic microorganisms, contains one mononuclear none-heme iron centre per subunit. Elemental sulfur is both the electron donor and one of the two known acceptors, the other being oxygen. Thiosulfate is also observed as a product, but is likely formed non-enzymically by a reaction between sulfite and sulfur [1]. This enzyme differs from EC 1.13.11.18, sulfur dioxygenase and EC 1.12.98.4, sulfhydrogenase, in that both activities occur simultaneously.
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CAS REGISTRY NUMBER
COMMENTARY
120598-92-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
initial enzyme in the sulfur-oxidation pathway
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
in the presence of oxygen but not under a hydrogen atmosphere, the enzyme simultaneously produces sulfite, thiosulfate, and hydrogen sulfide from sulfur. Nonenzymatic control experiments show that thiosulfate is produced mainly in a chemical reaction between sulfite and sulfur. The ratio of sulfite to hydrogen sulfide production is 5:4 in the presence of zinc ions
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
in the presence of oxygen but not under a hydrogen atmosphere, the enzyme simultaneously produces sulfite, thiosulfate, and hydrogen sulfide from sulfur. Nonenzymatic control experiments show that thiosulfate is produced mainly in a chemical reaction between sulfite and sulfur. The ratio of sulfite to hydrogen sulfide production is 5:4 in the presence of zinc ions
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
initial enzyme in the sulfur-oxidation pathway
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
-
discoloration of 2,6-dichlorophenolindophenol (DCPIP) by H2S is followed as an alternative detection method
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
-
discoloration of 2,6-dichlorophenolindophenol (DCPIP) by H2S is followed as an alternative detection method
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
-
discoloration of 2,6-dichlorophenolindophenol (DCPIP) by H2S is followed as an alternative detection method
-
-
?
sulfur + H2O + O2
?
initial enzyme in the sulfur oxidation pathway
-
-
?
sulfur + H2O + O2
?
-
sulfur oxygenase reductase is responsible for the initial oxidation step of elemental sulfur in archaea
-
-
?
additional information
?
-
not active with tetrathionate
-
-
?
additional information
?
-
SOR catalyzes simultaneously oxidation and reduction of elementar sulfur to produce sulfite, thiosulfate and sulfide, in the presence of molecule oxygen
-
-
?
additional information
?
-
enzyme Sor catalyzes the oxygen dependent disproportionation of elemental sulfur, producing sulfite, thiosulfate and sulfide
-
-
?
additional information
?
-
enzyme Sor catalyzes the oxygen dependent disproportionation of elemental sulfur, producing sulfite, thiosulfate and sulfide
-
-
?
additional information
?
-
-
enzyme Sor catalyzes the oxygen dependent disproportionation of elemental sulfur, producing sulfite, thiosulfate and sulfide
-
-
?
additional information
?
-
enzyme Sor catalyzes the oxygen dependent disproportionation of elemental sulfur, producing sulfite, thiosulfate and sulfide
-
-
?
additional information
?
-
enzyme Sor catalyzes the oxygen dependent disproportionation of elemental sulfur, producing sulfite, thiosulfate and sulfide
-
-
?
additional information
?
-
-
at 50°C, nonenzymatic sulfur disproportionation is observed at pH 11 and above. At pH 12, the enzyme activity cannot be distinguished from the background anymore. At 50°C, sulfite exceeds thiosulfate production at all pH value, at 80°C, the main product is thiosulfate with only minor amounts of sulfite (maximum 6%)
-
-
?
additional information
?
-
-
at 50°C, nonenzymatic sulfur disproportionation is observed at pH 11 and above. At pH 12, the enzyme activity cannot be distinguished from the background anymore. At 50°C, sulfite exceeds thiosulfate production at all pH value, at 80°C, the main product is thiosulfate with only minor amounts of sulfite (maximum 6%)
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
SOR catalyzes simultaneously oxidation and reduction of elementar sulfur to produce sulfite, thiosulfate and sulfide, in the presence of molecule oxygen
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
initial enzyme in the sulfur-oxidation pathway
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
initial enzyme in the sulfur-oxidation pathway
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 bisulfite + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
-
-
-
-
?
4 sulfur + 4 H2O + O2
2 hydrogen sulfide + 2 HSO3- + 2 H+
-
-
-
-
?
sulfur + H2O + O2
?
initial enzyme in the sulfur oxidation pathway
-
-
?
sulfur + H2O + O2
?
-
sulfur oxygenase reductase is responsible for the initial oxidation step of elemental sulfur in archaea
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
iron content: 0.45 mol per mol subunit for recombinant wild-type enzyme, below 0.1 mol per mol subunit for mutant enzyme H86A, below 0.02 mol per mol subunit for mutant enzyme H90A, below 0.01 mol per mol subunit for mutant enzyme E114A, 0.02 mol per mol subunit for mutant enzyme E114D, 0.47 mol per mol subunit for mutant enzyme C31A, 0.42 mol per mol subunit for mutant enzyme C31S, 0.22 mol per mol subunit for mutant enzyme C101A, below 0.03 mol per mol subunit for mutant enzyme C101S, 0.19 mol per mol subunit for mutant enzyme C104A, 0.3 mol per mol subunit for mutant enzyme C104S, 0.56 mol per mol subunit for mutant enzyme C101A/C104A, 0.4 mol per mol subunit for mutant enzyme C101S/C104S
Fe2+
Iron
additional information
-
TpSOR activity depends on osmolyte concentrations and not on salt
Fe2+
non-heme iron. The iron site and the three conserved cysteine residues are located in an active site pocket that is connected to the inner cavity of the sphere by a narrow pore formed by two adjacent methionines and a phenylalanine
Fe2+
essential for activity, recombinant SOR had a molar ratio of 1.86:1 (iron to subunit of SOR), excesses of ferric and ferrous ions have inhibitory effect on SOR activity
Fe2+
-
low-potential mononuclear non-heme iron bound in the active site
Iron
low-potential mononuclear non-heme iron site ligated by a 2-His-1-carboxylate facial triad in a pocket of each subunit constitutes the active sites, accessible from the inside of the sphere. The iron is likely the site of both sulfur oxidation and sulfur reduction
Iron
the enzyme contains a low-potential mononuclear non-heme iron centre, which has a reduction potential of -268 mV at pH 6.5, one iron atom per subunit
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4,5-dihydroxy-meta-benzenedisulfonic acid
tiron, Fe3+-specific chelator, strong inhibition
glycine betaine
-
25% inhibition at 1 M NaCl, below 10% activity at 3 M, inactive at 4 M NaCl
NaCl
-
25% inhibition at 1 M NaCl, below 10% activity at 3 M, residual activities of 0.2% of the maximum at 5 M NaCl
Zn2+
0.5 mM, 95% inhibition of oxygenase reaction (formation of hydrogen sulfide), 84% inhibition of reductase reaction (formation of sulfite plus thiosulfate)
Zn2+
zinc binds far from the actIve sIte , Zn2+ interferes over a distance with the subunit pores in the outer shell, possibly by restriction of protein flexibility or substrate access or product exit
additional information
the enmzyme is not affected by CN-, N3-, or reduced glutathione
-
additional information
-
the enmzyme is not affected by CN-, N3-, or reduced glutathione
-
additional information
not inhibited by CN-, N2 and reduced glutathione
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
opening the putative substrate and product pathways in the outer shell leads to a significant increase in specific activity and to a shift in the stoichiometry of the products
-
additional information
-
opening the putative substrate and product pathways in the outer shell leads to a significant increase in specific activity and to a shift in the stoichiometry of the products
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2 - 3
sulfur
pH 7.2, 65°C, oxygenase reaction (formation of hydrogen sulfide)
13
sulfur
pH 7.2, 65°C, reductase reaction (formation of sulphite plus thiosulfate)
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
sulfur
pH 7.2, 65°C, reductase reaction (formation of sulfite plus thiosulfate)
2.2
sulfur
pH 7.2, 65°C, oxygenase reaction (formation of hydrogen sulfide)
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.03
0.05
crude enzyme extract, sulfur reductase activity, pH 7.5, 75°C
0.074
-
wild type in cellular lysate, formation of sulfite plus thiosulfate, 70°C
0.1078
-
wild type in supernatant, formation of sulfite plus thiosulfate, 70°C
0.22
crude enzyme extract, sulfur oxygenase activity, pH 7.5, 75°C
0.476
-
wild type in pellet, formation of sulfite plus thiosulfate, 70°C
10.6
28600
wild type, cell lysate, 65°C, 20 mM Tris-HCl, pH 8.0, formation of thiosulfate and sulfite
29700
wild type, cell lysate treated at 75°C for 15 min, 65°C, 20 mM Tris-HCl, pH 8.0, formation of thiosulfate and sulfite
308 - 454
-
purified recombinant enzyme, pH 9.0, 80°C, thiosulfate- and sulfite-producing oxygenase activity
3100
wild type, cell lysate, 65°C, 20 mM Tris-HCl, pH 8.0, formation of H2S
3300
wild type, cell lysate treated at 75°C for 15 min, 65°C, 20 mM Tris-HCl, pH 8.0, formation of H2S
45200
Escherichia coli HB101, cell lysate treated at 75°C for 15 min, 65°C, 20 mM Tris-HCl, pH 8.0, formation of H2S
6300
Escherichia coli HB101, cell lysate, 65°C, 20 mM Tris-HCl, pH 8.0, formation of H2S
75000
Escherichia coli HB101, cell lysate, 65°C, 20 mM Tris-HCl, pH 8.0, formation of thiosulfate and sulfite
753000
Escherichia coli HB101, cell lysate treated at 75°C for 15 min, 65°C, 20 mM Tris-HCl, pH 8.0, formation of thiosulfate and sulfite
additional information
0.03
-
purified recombinant enzyme, pH 9.0, 80°C, reductase activity
additional information
0% activity with 0.2 mM 2.2'-dipyridyl compared to activity without any treatment
additional information
0.3% activity with 1 mM Fe3+ compared to activity without any treatment
additional information
17.8% activity with 1.0 mM 8-hydroxyquinoline compared to activity without any treatment
additional information
199.4% activity with 10 mM 2.2'-dipyridyl after ultrafiltration compared to activity without any treatment, the SOR activity recovers after removal (washing/untrafiltration) of the excessive iron
additional information
21.1% activity with 0.04 mM 2.2'-dipyridyl compared to activity without any treatment
additional information
239.7% activity with 10 mM 4,5-dihydroxy-meta-benzenedisulfonic acid after ultrafiltration compared to activity without any treatment, the SOR activity recovers after removal (washing and ultrafiltration) of the excessive iron
additional information
31.5% activity with 1 mM Fe2+ compared to activity without any treatment
additional information
44% activity with 0.1 mM 8-hydroxyquinoline compared to activity without any treatment
additional information
52.8% activity with 1.0 mM 4,5-dihydroxy-meta-benzenedisulfonic acid compared to activity without any treatment
additional information
55% activity with 0.1 mM 4,5-dihydroxy-meta-benzenedisulfonic acid compared to activity without any treatment
additional information
-
recombinant Thioalkalivibrio paradoxus SOR has a very low reductase activity and H2S production
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE