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EC Tree
IUBMB Comments Contains FAD. Ubiquinone, plastoquinone or menaquinone can act as acceptor in different species. In some organisms the enzyme catalyses the formation of sulfur globules. It repeats the catalytic cycle without releasing the product, producing a polysulfide of up to 10 sulfur atoms. The reaction stops when the maximum length of the polysulfide that can be accommodated in the sulfide oxidation pocket is achieved. The enzyme also plays an important role in anoxygenic bacterial photosynthesis. cf. EC 1.8.5.8, sulfide quinone oxidoreductase.
The taxonomic range for the selected organisms is: Homo sapiens The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
sulfide:quinone oxidoreductase, sulfide quinone oxidoreductase, sqrdl, sulfide quinone reductase, sulfide-quinone reductase, sulfide-quinone oxidoreductase, ct1087, trsqrf, iii sqr, cpsqr,
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sulfide quinone oxidoreductase
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sulfide: quinone oxidoreductase
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sulfide:quinone oxidoreductase
Contains FAD. Ubiquinone, plastoquinone or menaquinone can act as acceptor in different species. In some organisms the enzyme catalyses the formation of sulfur globules. It repeats the catalytic cycle without releasing the product, producing a polysulfide of up to 10 sulfur atoms. The reaction stops when the maximum length of the polysulfide that can be accommodated in the sulfide oxidation pocket is achieved. The enzyme also plays an important role in anoxygenic bacterial photosynthesis. cf. EC 1.8.5.8, sulfide quinone oxidoreductase.
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2 sulfide + ubiquinone-1
hydrogen disulfide + ubiquinol-1
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-
-
?
sulfide + coenzyme Q
sulfane sulfur + reduced coenzyme Q
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-
-
?
sulfide + coenzyme Q
sulfur + reduced coenzyme Q
-
-
-
?
sulfide + coenzyme Q1
sulfur + reduced coenzyme Q1
-
-
-
?
sulfide + coenzyme Q10
sulfur + reduced coenzyme Q10
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-
-
?
sulfide + cyanide + coenzyme Q
thiocyanate + reduced coenzyme Q
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-
-
?
sulfide + cyanide + ubiquinone-1
thiocyanate + ubiquinol-1
-
-
-
?
sulfide + cysteine + coenzyme Q1
cysteine persulfide + reduced coenzyme Q1
-
-
-
-
?
sulfide + decylubiquinone
sulfur + decylubiquinol
-
-
-
?
sulfide + glutathione
sulfur + reduced glutathione
-
-
-
?
sulfide + homocysteine + coenzyme Q1
homocysteine persulfide + reduced coenzyme Q1
-
-
-
-
?
sulfide + reduced glutathione + coenzyme Q1
glutathione persulfide + reduced coenzyme Q1
-
-
-
-
?
sulfide + sulfide + coenzyme Q
hydrogen disulfide + reduced coenzyme Q
-
-
-
?
sulfide + sulfite + coenzyme Q
thiosulfate + reduced coenzyme Q
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-
-
?
sulfide + sulfite + ubiquinone-1
thiosulfate + ubiquinol-1
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-
-
?
sulfide + ubiquinone-1
sulfur + ubiquinol-1
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-
-
?
additional information
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additional information
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cyanide, sulfite, or sulfide can act as the sulfane sulfur acceptor in reactions that exhibit pH optima at 8.5, 7.5, or 7.0, respectively, and produce thiocyanate, thiosulfate, or a putative sulfur analogue of hydrogen peroxide, i.e. H2S2, respectively. Sulfite is the physiological acceptor of the sulfur and the reaction is the predominant source of the thiosulfate produced during H2S oxidation by mammalian tissues
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?
additional information
?
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cyanide, sulfite, or sulfide can act as the sulfane sulfur acceptor in reactions that exhibit pH optima at 8.5, 7.5, or 7.0, respectively, and produce thiocyanate, thiosulfate, or a putative sulfur analogue of hydrogen peroxide, i.e. H2S2, respectively. Sulfite is the physiological acceptor of the sulfur and the reaction is the predominant source of the thiosulfate produced during H2S oxidation by mammalian tissues
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-
?
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sulfide + coenzyme Q
sulfane sulfur + reduced coenzyme Q
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-
-
?
sulfide + glutathione
sulfur + reduced glutathione
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-
-
?
sulfide + ubiquinone-1
sulfur + ubiquinol-1
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-
-
?
additional information
?
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additional information
?
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cyanide, sulfite, or sulfide can act as the sulfane sulfur acceptor in reactions that exhibit pH optima at 8.5, 7.5, or 7.0, respectively, and produce thiocyanate, thiosulfate, or a putative sulfur analogue of hydrogen peroxide, i.e. H2S2, respectively. Sulfite is the physiological acceptor of the sulfur and the reaction is the predominant source of the thiosulfate produced during H2S oxidation by mammalian tissues
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-
?
additional information
?
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cyanide, sulfite, or sulfide can act as the sulfane sulfur acceptor in reactions that exhibit pH optima at 8.5, 7.5, or 7.0, respectively, and produce thiocyanate, thiosulfate, or a putative sulfur analogue of hydrogen peroxide, i.e. H2S2, respectively. Sulfite is the physiological acceptor of the sulfur and the reaction is the predominant source of the thiosulfate produced during H2S oxidation by mammalian tissues
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?
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FAD
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FAD
protein contains noncovalently bound FAD
FAD
the enzyme contains 0.82 mol FAD per mol protein
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cyanide
4.5fold increase in the rate of H2S oxidation in the presence of 1 mM cyanide
sulfite
13.6fold increase in the rate of H2S oxidation in the presence of 0.6 mM sulfite
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Heart Failure
Discovery of a first-in-class inhibitor of sulfide:quinone oxidoreductase that protects against adverse cardiac remodeling and heart failure.
Leigh Disease
Pathogenic variants in SQOR encoding sulfide:quinone oxidoreductase are a potentially treatable cause of Leigh disease.
Metabolic Syndrome
Lipogenesis is decreased by grape seed proanthocyanidins according to liver proteomics of rats fed a high fat diet.
Osteoporosis
Association of the I264T variant in the sulfide quinone reductase-like (SQRDL) gene with osteoporosis in Korean postmenopausal women.
Osteoporosis
Genetic susceptibility of postmenopausal osteoporosis on sulfide quinone reductase-like gene.
Osteoporosis, Postmenopausal
Association of the I264T variant in the sulfide quinone reductase-like (SQRDL) gene with osteoporosis in Korean postmenopausal women.
Osteoporosis, Postmenopausal
Genetic susceptibility of postmenopausal osteoporosis on sulfide quinone reductase-like gene.
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2 - 3
cysteine
-
pH 7.4, 25°C
22
homocysteine
-
pH 7.4, 25°C
22
reduced glutathione
-
pH 7.4, 25°C
0.014 - 0.0199
ubiquinone-1
0.014
coenzyme Q
with cyanide and sulfide as cosubstrates, at pH 8.0 and 25°C
0.019
coenzyme Q
with sulfite and sulfide as cosubstrates, at pH 8.0 and 25°C
0.65
cyanide
cosubstrates sulfide, ubiquinone-1, pH 8.5, 25°C
0.65
cyanide
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
0.0109
Sulfide
cosubstrates cyanide, ubiquinone-1, pH 8.5, 25°C
0.0109
Sulfide
with coenzyme Q and cyanide as cosubstrates, at pH 8.0 and 25°C
0.013
Sulfide
cosubstrates sulfite, ubiquinone-1, pH 7.5, 25°C
0.013
Sulfide
with coenzyme Q and sulfite as cosubstrates, at pH 8.0 and 25°C
0.23
Sulfide
enzyme in nanodiscs, at pH 6.8 and 25°C
0.315
Sulfide
cosubstrates sulfide, ubiquinone-1, pH 7.0, 25°C
0.315
Sulfide
with coenzyme Q as cosubstrate, at pH 8.0 and 25°C
0.32
Sulfide
-
pH 7.4, 25°C
0.35
Sulfide
solubilized enzyme, at pH 6.8 and 25°C
0.174
sulfite
cosubstrates sulfide, ubiquinone-1, pH 7.5, 25°C
0.174
sulfite
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
0.014
ubiquinone-1
cosubstrates cyanide, sulfide, pH 8.5, 25°C
0.0199
ubiquinone-1
cosubstrates sulfite, sulfide, pH 7.5, 25°C
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94
cysteine
-
pH 7.4, 25°C
92
homocysteine
-
pH 7.4, 25°C
113
reduced glutathione
-
pH 7.4, 25°C
360
coenzyme Q
with cyanide and sulfide as cosubstrates, at pH 8.0 and 25°C
364
coenzyme Q
with sulfite and sulfide as cosubstrates, at pH 8.0 and 25°C
330
cyanide
cosubstrates sulfide, ubiquinone-1, pH 8.5, 25°C
330
cyanide
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
18.5
Sulfide
with coenzyme Q as cosubstrate, at pH 8.0 and 25°C
62
Sulfide
solubilized enzyme, at pH 6.8 and 25°C
65
Sulfide
cosubstrates sulfide, ubiquinone-1, pH 7.0, 25°C
65
Sulfide
with coenzyme Q as cosubstrate, at pH 8.0 and 25°C
74
Sulfide
-
pH 7.4, 25°C
84
Sulfide
enzyme in nanodiscs, at pH 6.8 and 25°C
343
Sulfide
cosubstrates cyanide, ubiquinone-1, pH 8.5, 25°C
343
Sulfide
with coenzyme Q and cyanide as cosubstrates, at pH 8.0 and 25°C
379
Sulfide
cosubstrates sulfite, ubiquinone-1, pH 7.5, 25°C
379
Sulfide
with coenzyme Q and sulfite as cosubstrates, at pH 8.0 and 25°C
368
sulfite
cosubstrates sulfide, ubiquinone-1, pH 7.5, 25°C
368
sulfite
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
360
ubiquinone-1
cosubstrates cyanide, sulfide, pH 8.5, 25°C
364
ubiquinone-1
cosubstrates sulfite, sulfide, pH 7.5, 25°C
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4.1
cysteine
-
pH 7.4, 25°C
4.2
homocysteine
-
pH 7.4, 25°C
5.1
reduced glutathione
-
pH 7.4, 25°C
19000 - 27000
ubiquinone-1
19000
coenzyme Q
with sulfite and sulfide as cosubstrates, at pH 8.0 and 25°C
27000
coenzyme Q
with cyanide and sulfide as cosubstrates, at pH 8.0 and 25°C
510
cyanide
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
5100
cyanide
cosubstrates sulfide, ubiquinone-1, pH 8.5, 25°C
2.3
Sulfide
-
pH 7.4, 25°C
180
Sulfide
solubilized enzyme, at pH 6.8 and 25°C
210
Sulfide
with coenzyme Q as cosubstrate, at pH 8.0 and 25°C
370
Sulfide
enzyme in nanodiscs, at pH 6.8 and 25°C
2100
Sulfide
cosubstrates sulfide, ubiquinone-1, pH 7.0, 25°C
29000
Sulfide
cosubstrates sulfite, ubiquinone-1, pH 7.5, 25°C
29000
Sulfide
with coenzyme Q and sulfite as cosubstrates, at pH 8.0 and 25°C
31000
Sulfide
cosubstrates cyanide, ubiquinone-1, pH 8.5, 25°C
31000
Sulfide
with coenzyme Q and cyanide as cosubstrates, at pH 8.0 and 25°C
2100
sulfite
cosubstrates sulfide, ubiquinone-1, pH 7.5, 25°C
2100
sulfite
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
19000
ubiquinone-1
cosubstrates sulfite, sulfide, pH 7.5, 25°C
27000
ubiquinone-1
cosubstrates cyanide, sulfide, pH 8.5, 25°C
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1.17
unpurified enzyme, at pH 8.0 and 25°C
580.8
purified enzyme, at pH 8.0 and 25°C
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UniProt
brenda
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brenda
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UniProt
brenda
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brenda
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physiological function
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human sulfide quinone oxidoreductase uses glutathione as an acceptor forming glutathione persulfide (GSSH), which is preferentially converted to thiosulfate by human rhodanese
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SQOR_HUMAN
450
0
49961
Swiss-Prot
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homodimer
2 * 47000, SDS-PAGE
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HiTrap IMAC column chromatography and Q Sepharose column chromatography
nickel affinity column chromatography and Superdex 200 gel filtration
nickel affinity column chromatography and Superdex 200 gel filtration
nickel affinity column chromatography and Superdex 200 gel filtration
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expressed in Escherichia coli BL21(DE3) cells
expression at low temperature in Escherichia coli by using an optimized synthetic gene and cold-adapted chaperonins
expression in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
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Jackson, M.; Melideo, S.; Jorns, M.
Human sulfide:Quinone oxidoreductase catalyzes the first step in hydrogen sulfide metabolism and produces a sulfane sulfur metabolite
Biochemistry
51
6804-6815
2012
Homo sapiens (Q9Y6N5), Homo sapiens
brenda
Libiad, M.; Yadav, P.; Vitvitsky, V.; Martinov, M.; Banerjee, R.
Organization of the human mitochondrial hydrogen sulfide oxidation pathway
J. Biol. Chem.
289
30901-30910
2014
Homo sapiens
brenda
Mishanina, T.; Yadav, P.; Ballou, D.; Banerjee, R.
Transient kinetic analysis of hydrogen sulfide oxidation catalyzed by human sulfide quinone oxidoreductase
J. Biol. Chem.
290
25072-25080
2015
Homo sapiens (Q9Y6N5), Homo sapiens
brenda
Landry, A.; Ballou, D.; Banerjee, R.
H2S oxidation by nanodisc-embedded human sulfide quinone oxidoreductase
J. Biol. Chem.
292
11641-11649
2017
Homo sapiens (Q9Y6N5), Homo sapiens
brenda
Jackson, M.R.; Melideo, S.L.; Jorns, M.S.
Role of human sulfide quinone oxidoreductase in H2S metabolism
Methods Enzymol.
554
255-270
2015
Homo sapiens (Q9Y6N5), Homo sapiens
brenda