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Information on EC 1.8.5.4 - bacterial sulfide:quinone reductase
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1.8.5.4 bacterial sulfide:quinone reductaseIUBMB 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.
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Word Map
- 1.8.5.4
- sulfur
- h2s
- thiosulfate
- persulfide
- polysulfide
- rhodanese
- acidithiobacillus
- sulfurtransferase
-
sulfane
-
sqors
-
sulfide-oxidizing
-
chemolithotrophic
-
sulfide-dependent
- ferrooxidans
- 3-mercaptopyruvate
-
sulfur-oxidizing
- chlorobaculum
-
echiuran
- oscillatoria
-
sulfide-rich
- tepidum
-
monotopic
- unicinctus
-
urechis
- limnetica
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
CT1087, SQOR, SQR, Sqrdl, Suden_1879, Suden_2082, Suden_619, sulfide quinone oxidoreductase, sulfide quinone oxidoreductase::, sulfide quinone reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SQR
Sqrdl
Suden_1879
Suden_2082
Suden_619
sulfide quinone oxidoreductase
sulfide-quinone reductase
sulfide:decylubiquinone oxidoreductase
sulfide:quinone oxidoreductase
sulfidequinone reductase-like protein
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
n HS- + n quinone = polysulfide + n quinol
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
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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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
sulfide + 2,3-dimethyl-1,4-naphthoquinone
sulfur + 2,3-dimethyl-1,4-naphthoquinol
-
-
-
-
?
sulfide + 2-methyl-3-methylthio-1,4-naphthoquinone
sulfur + 2-methyl-3-methylthio-1,4-naphthoquinol
-
lowest activity
-
-
?
sulfide + cysteine + coenzyme Q1
cysteine persulfide + reduced coenzyme Q1
-
-
-
-
?
sulfide + decylubiquinone + cyanide
sulfur + decylubiquinol + thiocyanate
-
-
-
-
?
sulfide + decylubiquinone + Escherichia coli thioredoxin
sulfur + decylubiquinol + ?
-
with Escherichia coli thioredoxin, SQR exhibits one-tenth of the cyanide-dependent activity
-
-
?
sulfide + decylubiquinone + sulfite
sulfur + decylubiquinol + ?
-
with sulfite, SQR exhibits one-tenth of the cyanide-dependent activity
-
-
?
sulfide + duroquinone 23
sulfur + duroquinol 23
-
% compared to the activity with decylubiquinone
-
-
?
sulfide + homocysteine + coenzyme Q1
homocysteine persulfide + reduced coenzyme Q1
-
-
-
-
?
sulfide + menadione
polysulfide + menadiol
-
25% compared to the activity with decylubiquinone
-
-
?
sulfide + plastoquinone-2
sulfur + plastoquinol-2
-
highest activity
-
-
?
sulfide + reduced glutathione + coenzyme Q1
glutathione persulfide + reduced coenzyme Q1
-
-
-
-
?
sulfide + sulfide + coenzyme Q
hydrogen disulfide + reduced coenzyme Q
-
-
-
?
sulfide + decylubiquinone
polysulfide + decylubiquinol
-
-
-
-
?
sulfide + decylubiquinone
polysulfide + decylubiquinol
-
-
-
-
?
sulfide + decylubiquinone
sulfur + decylubiquinol
-
-
-
?
sulfide + decylubiquinone
sulfur + decylubiquinol
-
-
-
?
sulfide + decylubiquinone
sulfur + decylubiquinol
-
-
-
-
?
sulfide + duroquinone
sulfur + duroquinol
-
23% compared to the activity with decylubiquinone
-
-
?
sulfide + duroquinone
sulfur + duroquinol
-
23% compared to the activity with decylubiquinone
-
-
?
sulfide + menadione
sulfur + menadiol
-
25% compared to the activity with decylubiquinone
-
-
?
sulfide + menadione
sulfur + menadiol
-
25% compared to the activity with decylubiquinone
-
-
?
sulfide + ubiquinone-1
sulfur + ubiquinol-1
-
15% compared to the activity with decylubiquinone
-
-
?
sulfide + ubiquinone-1
sulfur + ubiquinol-1
-
15% compared to the activity with decylubiquinone
-
-
?
additional information
?
-
the enzymatic reaction catalyzed by sulfide:quinone oxidoreductase includes the oxidation of sulfide compounds H2S, HS-, and S2- to soluble polysulfide chains or to elemental sulfur in the form of octasulfur rings
-
-
?
additional information
?
-
-
the enzymatic reaction catalyzed by sulfide:quinone oxidoreductase includes the oxidation of sulfide compounds H2S, HS-, and S2- to soluble polysulfide chains or to elemental sulfur in the form of octasulfur rings
-
-
?
additional information
?
-
-
no activity with vitamin K1
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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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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
?
-
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
-
-
?
additional information
?
-
-
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
the enzyme harbors one noncovalently bound FAD cofactor per monomer
FAD
-
FAD is not covalently bound to the protein. Activity is not increased by the addition of FAD (0.020 mM) to the assay buffer
FAD
-
is not covalently bound to the protein, the cofactor is in an apolar environment, one equivalent of FAD per sulfide:quinone xidoreductase polypeptide
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2n-nonyl-4-hydroxyquinoline-N-oxide
complete inhibition at 0.001 mM
2n-nonyl-4-hydroxyquinoline-N-oxide
-
complete inhibition at 0.001 mM
antimycin A
-
at 0.01 mM antimycin, residual sulfide:quinone oxidoreductase activity amounts to 53.4%
additional information
-
insentitive towards nonylhydroxyquinoline-N-oxide
-
additional information
-
not inhibited by 5n-undecyl-6-hydroxy-4,7-dioxobenzothiazole, 2-iodo-6-isopropyl-3-methyl-2'-4,4'-trinitrodiphenyl ether, and 3-(3',4'-dichlorophenyl)-1,1-dimelhylurea
-
additional information
-
insensitive to 3-(3'-4'-dichlorophenyl)-1,1-dimethylurea and 2-iodo-6-isopropyl-3-methyl-2',4,4'-trinitrodiphenyl ether
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
sulfite
13.6fold increase in the rate of H2S oxidation in the presence of 0.6 mM sulfite
cyanide
-
SQR isolated from yeast mitochondria reduces decyl-ubiquinone after the addition of sulfide only in the presence of cyanide
cyanide
4.5fold increase in the rate of H2S oxidation in the presence of 1 mM cyanide
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.014
ubiquinone-2
-
apparent value, at pH 7.0, temperature not specified in the publication
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
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
0.002
decylubiquinone
in 10 mM bis-Tris-HCl, pH 6.5, temperature not specified in the publication
0.00216
decylubiquinone
pH 7.4, temperature not specified in the publication
0.003
decylubiquinone
-
mutant enzyme H196A, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication
0.003
decylubiquinone
-
wild type enzyme, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication
0.0031
decylubiquinone
-
in 50 mM Bis-Tris (pH 6.5), temperature not specified in the publication
0.00343
decylubiquinone
wild type enzyme, at pH 7.0 and 23°C
0.00425
decylubiquinone
mutant enzyme C128A, at pH 7.0 and 23°C
0.0054
decylubiquinone
mutant enzyme H132A, at pH 7.0 and 23°C
0.00585
decylubiquinone
mutant enzyme C128S, at pH 7.0 and 23°C
0.022
decylubiquinone
in 50 mM 2-[bis(2-hydroxyethyl)amino]-2-(hydroxymethyl)propane-1,3-diol (pH 6.5), temperature not specified in the publication
0.027
decylubiquinone
-
mutant enzyme H131A, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication
0.028
decylubiquinone
-
Km above 0.028 mM, mutant enzyme V300D, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication
0.03
decylubiquinone
-
pH 7.5, 60°C, membrane-bound wild-type enzyme
0.032
decylubiquinone
-
pH 7.5, 60°C, membrane-bound mutant enzyme M380N
0.033
decylubiquinone
-
pH 7.5, 60°C, membrane-bound mutant enzyme Y383Q/F384K
0.036
decylubiquinone
-
pH 7.5, 60°C, cytoplasmic mutant enzyme Y383Q/F384K
0.031
plastoquinone-1
-
in 10 mM HEPES, pH 7.4, 10 mM MgCl, 10 mM KCl, at 22°C
0.04
plastoquinone-1
in 10 mM potassium HEPES (pH 7.4), 10 mM MgCl2, 10 mM KCl, temperature not specified in the publication
0.04
plastoquinone-1
-
in 10 mM potassium HEPES (pH 7.4), 10 mM MgCl2, 10 mM KCl, temperature not specified in the publication
0.002
Sulfide
in 10 mM bis-Tris-HCl, pH 6.5, temperature not specified in the publication
0.0028
Sulfide
in 50 mM 2-[bis(2-hydroxyethyl)amino]-2-(hydroxymethyl)propane-1,3-diol (pH 6.5), temperature not specified in the publication
0.005
Sulfide
-
wild type enzyme, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication
0.00553
Sulfide
mutant enzyme C128S, at pH 7.0 and 23°C
0.008
Sulfide
-
in 10 mM HEPES, pH 7.4, 10 mM MgCl, 10 mM KCl, at 22°C
0.0109
Sulfide
with coenzyme Q and cyanide as cosubstrates, at pH 8.0 and 25°C
0.011
Sulfide
-
mutant enzyme H131A, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication
0.013
Sulfide
with coenzyme Q and sulfite as cosubstrates, at pH 8.0 and 25°C
0.015
Sulfide
-
mutant enzyme H196A, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication
0.02
Sulfide
in 10 mM potassium HEPES (pH 7.4), 10 mM MgCl2, 10 mM KCl, temperature not specified in the publication
0.02
Sulfide
-
in 10 mM potassium HEPES (pH 7.4), 10 mM MgCl2, 10 mM KCl, temperature not specified in the publication
0.026
Sulfide
-
in 50 mM Bis-Tris (pH 6.5), temperature not specified in the publication
0.042
Sulfide
-
apparent value, at pH 7.0, temperature not specified in the publication
0.046
Sulfide
-
pH 7.5, 60°C, membrane-bound mutant enzyme Y383Q/F384K
0.077
Sulfide
-
pH 7.5, 60°C, cytoplasmic mutant enzyme Y383Q/F384K
0.4
Sulfide
-
Km above 0.4 mM, mutant enzyme V300D, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication
0.174
sulfite
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
0.0054
ubiquinone-1
pH 7.4, temperature not specified in the publication
0.0016
ubiquinone-4
pH 7.4, temperature not specified in the publication
0.00643
ubiquinone-9
pH 7.4, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
0.6
decylubiquinone
-
pH 7.5, 60°C, membrane-bound wild-type enzyme
0.62
decylubiquinone
-
pH 7.5, 60°C, membrane-bound mutant enzyme M380N
0.82
decylubiquinone
-
pH 7.5, 60°C, membrane-bound mutant enzyme Y383Q/F384K
1.2
decylubiquinone
-
pH 7.5, 60°C, cytoplasmic mutant enzyme Y383Q/F384K
0.82
Sulfide
-
pH 7.5, 60°C, membrane-bound mutant enzyme Y383Q/F384K
343
Sulfide
with coenzyme Q and cyanide as cosubstrates, at pH 8.0 and 25°C
379
Sulfide
with coenzyme Q and sulfite as cosubstrates, at pH 8.0 and 25°C
368
sulfite
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
240
decylubiquinone
mutant enzyme C128A, at pH 7.0 and 23°C
250
decylubiquinone
mutant enzyme H132A, at pH 7.0 and 23°C
270
decylubiquinone
mutant enzyme C128S, at pH 7.0 and 23°C
1890
decylubiquinone
wild type enzyme, at pH 7.0 and 23°C
29000
Sulfide
with coenzyme Q and sulfite as cosubstrates, at pH 8.0 and 25°C
31000
Sulfide
with coenzyme Q and cyanide as cosubstrates, at pH 8.0 and 25°C
2100
sulfite
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
2-n-heptyl-4-hydroxy-quinone-N-oxide
Acidithiobacillus ferrooxidans
-
at pH 7.0, temperature not specified in the publication
0.00014
n-nonyl-4-hydroxyquinoline-N-oxide
Pseudanabaena limnetica
-
in 10 mM HEPES, pH 7.4, 10 mM MgCl, 10 mM KCl, at 22°C
0.0005
2-heptylquinolin-4-ol 1-oxide
Allochromatium vinosum
-
in 50 mM Tris-HCl (pH 7.5), temperature not specified in the publication
0.00076
2-n-nonyl-4-hydroxyquinoline-N-oxide
Chlorobaculum thiosulfatiphilum
-
in 20 mM Tris-HCl, pH 7.8, at 24°C
0.006
2-n-nonyl-4-hydroxyquinoline-N-oxide
Aquifex aeolicus
-
in 50 mM Bis-Tris (pH 7.0), at 20°C
0.015
antimycin A
Paracoccus denitrificans
-
in 50 mM Bis-Tris (pH 6.5), temperature not specified in the publication
0.22
antimycin A
Acidithiobacillus ferrooxidans
-
at pH 7.0, temperature not specified in the publication
0.000049
aurachin C
Pseudanabaena limnetica
-
in 10 mM HEPES, pH 7.4, 10 mM MgCl, 10 mM KCl, at 22°C
0.028
aurachin C
Paracoccus denitrificans
-
in 50 mM Bis-Tris (pH 6.5), temperature not specified in the publication
0.5
cyanide
Allochromatium vinosum
-
in 50 mM Tris-HCl (pH 7.5), temperature not specified in the publication
0.54
cyanide
Acidithiobacillus ferrooxidans
-
at pH 7.0, temperature not specified in the publication
0.004
Myxothiazol
Allochromatium vinosum
-
in 50 mM Tris-HCl (pH 7.5), temperature not specified in the publication
0.022
Myxothiazol
Paracoccus denitrificans
-
in 50 mM Bis-Tris (pH 6.5), temperature not specified in the publication
0.039
Myxothiazol
Acidithiobacillus ferrooxidans
-
at pH 7.0, temperature not specified in the publication
0.02
Stigmatellin
Paracoccus denitrificans
-
in 50 mM Bis-Tris (pH 6.5), temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.018
-
enzyme from washed membrane, in 10 mM HEPES, pH 7.4, 10 mM MgCl, 10 mM KCl, at 22°C
0.1
crude extract, in 10 mM bis-Tris-HCl, pH 6.5, temperature not specified in the publication
0.11
-
cell-free extract, at pH 7.0, temperature not specified in the publication
0.127
-
using 2,3-dimethyl-1,4-naphthoquinone as cosubstrate, at 50°C, pH 6.5
1.88
-
after 105fold purification, in 10 mM HEPES, pH 7.4, 10 mM MgCl, 10 mM KCl, at 22°C
20.55
-
after 186.8fold purification, at pH 7.0, temperature not specified in the publication
3.5
55.4
-
in 50 mM Tris-HCl (pH 7.5), temperature not specified in the publication
3.5
after 35fold purification, in 10 mM bis-Tris-HCl, pH 6.5, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 70
-
with 0.015 mM decylubqiuinone reduced/mg protein/min, the activity at 70°C is 5fold higher than the activity at 20°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
enzyme mRNA expression during sulfide exposure in the body wall and hindgut increases in a time- and concentration-dependent manner that increases significantly at 12 h and continuously increases with time. At the protein level, enzyme expression in the two tissues increases significantly at 12 h after application of 50 microM sulfide and 6 h after 150 microM, and then continues to increase
brenda
-
enzyme mRNA expression during sulfide exposure in the body wall and hindgut increases in a time- and concentration-dependent manner that increases significantly at 12 h and continuously increases with time. At the protein level, enzyme expression in the two tissues increases significantly at 12 h after application of 50 microM sulfide and 6 h after 150 microM, and then continues to increase
brenda
-
in the brain, H2S signal termination occurs partially through protein sequestration and partially through catabolism not involving sulfide:quinone reductase
brenda
the number of Sqrdl transcripts in the brain increases with increasing age
brenda
-
termination of endogenous H2S signalling in the colonic muscularis externa occurs via catabolism to thiosulfate and sulfate partially via a mechanism involving sulfide:quinone reductase
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
periplasmic surface of the cytoplasmic membrane
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brenda
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periplasmic surface of the cytoplasmic membrane
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-
brenda
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the C-terminal amphiphilic helix is important for membrane binding
brenda
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the C-terminal amphiphilic helix is important for membrane binding
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brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
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SQR is involved in elemental sulfur oxidation in sulfur-grown cells
metabolism
the enzyme plays a key role in the sulfide-dependent respiration and anaerobic photosynthesis
metabolism
-
SQR is involved in elemental sulfur oxidation in sulfur-grown cells
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physiological function
-
SQR and the cytochrome bc complex are involved in sulfide-dependent respiration. Oxidation of sulfide by SQR is coupled, at least in part, to the proton-motive Q-cycle mechanism
physiological function
-
SQR is involved in sulfide detoxification, in sulfide-dependent energy conservation processes and potenatially in the homeostasis of the neurotransmitter sulfide
physiological function
SQR is involved in sulfide detoxification, in sulfide-dependent energy conservation processes and potentially in the homeostasis of the neurotransmitter sulfide
physiological function
-
sulfide-quinone reductase catalyzes anoxygenic photosynthesis in Oscillatoria limnetica
physiological function
sulfide-quinone reductase is essential for photoautotrophic growth on sulfide and is involved in energy conversion, but not in detoxification
physiological function
-
sulfide:quinone oxidoreductases are ubiquitous enzymes which have multiple roles: sulfide detoxification, energy generation by providing electrons to respiratory or photosynthetic electron transfer chains, and sulfide homeostasis
physiological function
-
human sulfide quinone oxidoreductase uses glutathione as an acceptor forming glutathione persulfide (GSSH), which is preferentially converted to thiosulfate by human rhodanese
physiological function
-
sulfide:quinone oxidoreductases are ubiquitous enzymes which have multiple roles: sulfide detoxification, energy generation by providing electrons to respiratory or photosynthetic electron transfer chains, and sulfide homeostasis
-
physiological function
-
sulfide-quinone reductase is essential for photoautotrophic growth on sulfide and is involved in energy conversion, but not in detoxification
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Show AA Sequence and Transmembrane Helices (107 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
47000
48000
57000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
homotrimer
monomer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 2.2 M NH4H2PO4 and 100 mM Tris-HCl, pH 8.5 (final pH of the solution is 4.5), or 2.2 M NH4H2PO4/K2HPO4 at pH 4.5
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crystal structures of the wild-type enzyme in complex with sodium selenide and gold(I) cyanide. Mechanism for the reduction of sulfides to elemental sulfur may involve nucleophilic attack of Cys356 on C4A atom of FAD or alternatively, an alternative anionic radical mechanism by direct electron transfer from Cys356 to the isoalloxazine ring of FAD
hanging drop vapor diffusion method, using 30% (w/v) PEG 600, 0.1 M bis-Tris pH 5.5, 0.1 M ammonium sulfate
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native or in complex with decylubiquinone, hanging drop vapor diffusion method, using 30% (w/v) polyethylene glycol 600, 0.1 M 2-[bis(2-hydroxyethyl)amino]-2-(hydroxymethyl)propane-1,3-diol (pH 5.5 or pH 6.5), 0.1 M magnesium sulfate, and 0.05% (w/v) n-dodecyl beta-D-maltoside
crystallization in two crystal forms of hexagonal, prism shape and thin, elongated shape
hanging drop vapor diffusion method, using 2.0 M ammonium sulfate and 4% (v/v) PEG 400
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C128A
C128S
C160A
C160S
the mutant shows strongly reduced activity compared to the wild type enzyme
C356S
H132A
H198A
S126A
about 35% of wild-type activity in assay with decylubiquinone
C128A
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about 35% of wild-type activity in assay with decylubiquinone
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C160A
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loss of activity in assay with decylubiquinone, about 35% of wild-type activity for reduction of FAD fluorescence by Na2S
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H132A
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about 40% of wild-type activity in assay with decylubiquinone
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H198A
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about 60% of wild-type activity in assay with decylubiquinone
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S126A
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about 35% of wild-type activity in assay with decylubiquinone
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L379D
L379D/M380N
L379N
M380N
Y383Q/F384K
Y383Q/F384K/L379D/M380N
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the mutant protein is found entirely in the cytoplasmic fraction but there is no catalytic activity
L379D/M380N
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both the membrane-bound and soluble forms of this protein are inactive
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Y383Q/F384K
Y383Q/F384K/L379D/M380N
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the mutant protein is found entirely in the cytoplasmic fraction but there is no catalytic activity
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H131A
-
20% activity at pH 6.5 and 27% activity at (optimum) pH 4.5 compared to the wild type enzyme
H196A
-
38% activity at pH 6.5 and 40% activity at (optimum) pH 6.2 compared to the wild type enzyme
additional information
C128A
the mutant shows strongly reduced activity compared to the wild type enzyme
C128A
in the decylubiquinone assay, the mutant shows 30-35% activity compared to the wild type enzyme. However, in the FAD reduction assay, both the wild type and the Cys128Ala variant are fully active (100%)
C128A
about 35% of wild-type activity in assay with decylubiquinone
C128S
the mutant shows strongly reduced activity compared to the wild type enzyme
C160A
loss of activity in assay with decylubiquinone, about 35% of wild-type activity for reduction of FAD fluorescence by Na2S
C160A
the mutant shows severely reduced activity compared to the wild type enzyme
C356S
loss of activity in assay with decylubiquinone, loss of activity for reduction of FAD fluorescence by Na2S
C356S
the mutant shows severely reduced activity compared to the wild type enzyme
H132A
the mutant shows strongly reduced activity compared to the wild type enzyme
H132A
about 40% of wild-type activity in assay with decylubiquinone
H198A
about 60% of wild-type activity in assay with decylubiquinone
H198A
the mutant shows severely reduced activity compared to the wild type enzyme
L379D
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all of the expressed protein is membrane-bound, the mutant enzyme is inactive
L379D
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inactive mutant enzyme, all of the expressed protein is membrane-bound
L379D/M380N
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both the membrane-bound and soluble forms of this protein are inactive
L379D/M380N
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the mutant protein is found in both the cytoplasmic and membrane fractions in equal proportions after disruption of the Escherichia coli cells, and each fraction has the same FAD content as the membrane bound wild type enzyme (about 50%)
L379N
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all of the expressed protein is membrane-bound, the mutant enzyme is inactive
L379N
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the mutant enzyme is inactive due to a perturbation of the decylubiquinone binding site
M380N
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mutation results in protein that is entirely membrane-bound, but which has the same activity as wild type enzyme
M380N
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this is one of the two mutations in the L379D/M380N double mutant. The M380N mutation by itself results in protein that is entirely membrane-bound, but which has the same activity as wild type enzyme
Y383Q/F384K
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both the soluble and membrane-bound versions of this double-mutant are catalytically active. The membrane-bound mutant enzyme has a specific activity about 30% higher than the wild type enzyme and the Km for sulfide is about half of the value found for the wild type enzyme. The water-soluble version of this mutant enzyme is twice as active as the wild type enzyme and the Km values for both sulfide and decylubiquinone are about the same as the wild type, membrane-bound form
Y383Q/F384K
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this mutant protein is expressed in a yield similar to the wild type enzyme and is found equally in the cytoplasmic and membrane fractions after cell disruption. The isolated proteins from each fraction contain FAD to the same extent as the wild type enzyme. Both the soluble and membrane bound versions of this double-mutant are catalytically active. The membrane-bound mutant enzyme has a specific activity about 30% higher than the wild type enzyme and the Km for sulfide is about half of the value found for the wild type (0.046 mM vs.0.077 mM). The water-soluble version of this mutant enzyme is twice as active as the wild type SQR (1.20 vs. 0.60 nmol quinone reduced/s* nM FAD) and the Km values for both sulfide and decylubiquinone are about the same as the wild type, membrane-bound form
Y383Q/F384K
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both the soluble and membrane-bound versions of this double-mutant are catalytically active. The membrane-bound mutant enzyme has a specific activity about 30% higher than the wild type enzyme and the Km for sulfide is about half of the value found for the wild type enzyme. The water-soluble version of this mutant enzyme is twice as active as the wild type enzyme and the Km values for both sulfide and decylubiquinone are about the same as the wild type, membrane-bound form
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Y383Q/F384K
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this mutant protein is expressed in a yield similar to the wild type enzyme and is found equally in the cytoplasmic and membrane fractions after cell disruption. The isolated proteins from each fraction contain FAD to the same extent as the wild type enzyme. Both the soluble and membrane bound versions of this double-mutant are catalytically active. The membrane-bound mutant enzyme has a specific activity about 30% higher than the wild type enzyme and the Km for sulfide is about half of the value found for the wild type (0.046 mM vs.0.077 mM). The water-soluble version of this mutant enzyme is twice as active as the wild type SQR (1.20 vs. 0.60 nmol quinone reduced/s* nM FAD) and the Km values for both sulfide and decylubiquinone are about the same as the wild type, membrane-bound form
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additional information
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in the truncation mutant SQRT1 a stop codon is introduced to eliminate the last 21 amino acids from the C-terminus, removing one putative amphiphilic helix. In construct SQRT2, the last 45 amino acids are removed, thus eliminating both of the amphiphilic helices. Both SQRT1 and SQRT2 when expressed in Escherichia coli result in water-soluble proteins. In each case the yield of protein is nearly 5-fold higher than the wild type construct, in which the recombinant protein is bound to the membrane. The FAD content of each of the truncated proteins, as well as the characteristics of the absorption spectra, is identical to those of the detergent-solubilized, wild type enzyme. No sulfide:decylubiquinone oxidoreductase activity is observed in either case
additional information
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in the truncation mutant SQRT1 a stop codon is introduced to eliminate the last 21 amino acids from the C-terminus, removing one putative amphiphilic helix. In construct SQRT2, the last 45 amino acids are removed, thus eliminating both of the amphiphilic helices. Both SQRT1 and SQRT2 when expressed in Escherichia coli result in water-soluble proteins. In each case the yield of protein is nearly 5-fold higher than the wild type construct, in which the recombinant protein is bound to the membrane. The FAD content of each of the truncated proteins, as well as the characteristics of the absorption spectra, is identical to those of the detergent-solubilized, wild type enzyme. No sulfide:decylubiquinone oxidoreductase activity is observed in either case
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additional information
no SQR activity is found in membranes from mutants F14 and 22/11. Membranes of strain F14sn show 6-7times the activity of the membranes from the wild type strain
additional information
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no SQR activity is found in membranes from mutants F14 and 22/11. Membranes of strain F14sn show 6-7times the activity of the membranes from the wild type strain
additional information
-
no SQR activity is found in membranes from mutants F14 and 22/11. Membranes of strain F14sn show 6-7times the activity of the membranes from the wild type strain
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 45
the recombinant enzyme is highly stable when incubated at 0°C, 4°C, 23°C or 30°C with more than 90% of the activity remaining after 7 h. It is less stable at 37°C and loses about 40% of the activity in the first 7.5 h. The activity of the enzyme decreases more rapidly at 45°C with a half-life of approximately 5 h
80
95
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the reaction with membranes that have been heated for more than 2 h at 95°C is negligible
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, protein is stable and monodisperse in 50 mM dodecyl-D-maltoside for weeks, either in the absence of salt or in the presence of N 1 M NaCl
4°C, purified protein in 3% (w/v) dodecyl-beta-D-maltoside either in the absence of salt or in the presence of N 1 M NaCl, six weeks, no loss of activity
80°C, purified protein in 3% (w/v) dodecyl-beta-D-maltoside either in the absence of salt or in the presence of N 1 M NaCl, one day, 50% loss of activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Hi-Trap column chromatography, and Superdex 200 gel filtration
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ammonium sulfate precipitation, phenyl-Toyopearl column chromatography, and TSKgel G3000 gel filtration
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ammonium sulfate precipitation, phenyl-TSK column chromatography, T SK-gel filtration and analytical gel filtration
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DEAE-cellulose column chromatography and Mono Q column chromatography
MonoQ column chromatography, TSK-1 gel filtration, and TSK-2 gel filtration
Ni-NTA 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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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) or Rosetta-gami(DE3) cells as a thioredoxin-fusion protein in inclusion bodies in an inactive form
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expressed in the Rhodobacter capsulatus SB1003 sqr deletion mutant
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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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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme mRNA expression during sulfide exposure in the body wall and hindgut increases in a time- and concentration-dependent manner that increases significantly at 12 h and continuously increases with time
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SQR activity is induced for 2 h in the presence of 1.25 mM sulfide and light
the number of Sqrdl transcripts in the brain increases with increasing age
SQR activity is induced for 2 h in the presence of 1.25 mM sulfide and light
SQR activity is induced for 2 h in the presence of 1.25 mM sulfide and light
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
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termination of endogenous H2S signalling in the colonic muscularis externa occurs via catabolism to thiosulfate and sulfate partially via a mechanism involving sulfide:quinone reductase. In the brain, H2S signal termination occurs partially through protein sequestration and partially through catabolism not involving sulfide:quinone reductase
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhang, Y.; Cherney, M.M.; Solomonson, M.; Liu, J.; James, M.N.; Weiner, J.H.
Preliminary X-ray crystallographic analysis of sulfide:quinone oxidoreductase from Acidithiobacillus ferrooxidans
Acta Crystallogr. Sect. F
F65
839-842
2009
Acidithiobacillus ferrooxidans
brenda
Schuetz, M.; Klughammer, C.; Griesbeck, C.; Quentmeier, A.; Friedrich, C.G.; Hauska, G.
Sulfide-quinone reductase activity in membranes of the chemotrophic bacterium Paracoccus denitrificans GB17
Arch. Microbiol.
170
353-360
1998
Paracoccus denitrificans, Paracoccus denitrificans GB17
-
brenda
Reinartz, M.; Tschape, J.; Bruser, T.; Truper, H.G.; Dahl, C.
Sulfide oxidation in the phototrophic sulfur bacterium Chromatium vinosum
Arch. Microbiol.
170
59-68
1998
Allochromatium vinosum
brenda
Nuebel, T.; Klughammer, C.; Huber, R.; Hauska, G.; Schuetz, M.
Sulfide:quinone oxidoreductase in membranes of the hyperthermophilic bacterium Aquifex aeolicus (VF5)
Arch. Microbiol.
173
233-244
2000
Aquifex aeolicus
brenda
Griesbeck, C.; Schuetz, M.; Schoedl, T.; Bathe, S.; Nausch, L.; Mederer, N.; Vielreicher, M.; Hauska, G.
Mechanism of sulfide-quinone reductase investigated using site-directed mutagenesis and sulfur analysis
Biochemistry
41
11552-11565
2002
Rhodobacter capsulatus
brenda
Brito, J.A.; Sousa, F.L.; Stelter, M.; Bandeiras, T.M.; Vonrhein, C.; Teixeira, M.; Pereira, M.M.; Archer, M.
Structural and functional insights into sulfide:quinone oxidoreductase
Biochemistry
48
5613-5622
2009
Acidianus ambivalens
brenda
Marcia, M.; Langer, J.D.; Parcej, D.; Vogel, V.; Peng, G.; Michel, H.
Characterizing a monotopic membrane enzyme. Biochemical, enzymatic and crystallization studies on Aquifex aeolicus sulfide:quinone oxidoreductase
Biochim. Biophys. Acta
1798
2114-2123
2010
Aquifex aeolicus, Aquifex aeolicus (O67931)
brenda
Wakai, S.; Tsujita, M.; Kikumoto, M.; Manchur, M.A.; Kanao, T.; Kamimura, K.
Purification and characterization of sulfide:quinone oxidoreductase from an acidophilic iron-oxidizing bacterium, Acidithiobacillus ferrooxidans
Biosci. Biotechnol. Biochem.
71
2735-2742
2007
Acidithiobacillus ferrooxidans, Acidithiobacillus ferrooxidans NASF-1
brenda
Theissen, U.; Martin, W.
Sulfide:quinone oxidoreductase (SOR) from the lugworm Arenicola marina shows cyanide- and thioredoxin-dependent activity
FEBS J.
275
1131-1139
2008
Arenicola marina
brenda
Shahak, Y.; Arieli, B.; Padan, E.; Hauska, G.
Sulfide quinone reductase (SQR) activity in Chlorobium
FEBS Lett.
299
127-130
1992
Chlorobaculum thiosulfatiphilum
brenda
Schuetz, M.; Maldener, I.; Griesbeck, C.; Hauska, G.
Sulfide-quinone reductase from Rhodobacter capsulatus: requirement for growth, periplasmic localization, and extension of gene sequence analysis
J. Bacteriol.
181
6516-6523
1999
Rhodobacter capsulatus (Q52722), Rhodobacter capsulatus, Rhodobacter capsulatus DSM Z 155 (Q52722)
brenda
Bronstein, M.; Schuetz, M.; Hauska, G.; Padan, E.; Shahak, Y.
Cyanobacterial sulfide-quinone reductase: cloning and heterologous expression
J. Bacteriol.
182
3336-3344
2000
Pseudanabaena limnetica, Aphanothece halophytica (Q9KI50), Aphanothece halophytica
brenda
Arieli, B.; Shahak, Y.; Taglicht, D.; Hauska, G.; Padan, E.
Purification and characterization of sulfide-quinone reductase, a novel enzyme driving anoxygenic photosynthesis in Oscillatoria limnetica
J. Biol. Chem.
269
5705-5711
1994
Pseudanabaena limnetica
brenda
Schuetz, M.; Shahak, Y.; Padan, E.; Hauska, G.
Sulfide-quinone reductase from Rhodobacter capsulatus. Purification, cloning, and expression
J. Biol. Chem.
272
9890-9894
1997
Rhodobacter capsulatus (Q52722), Rhodobacter capsulatus, Rhodobacter capsulatus DSM 155 (Q52722), Rhodobacter capsulatus DSM 155
brenda
Cherney, M.M.; Zhang, Y.; Solomonson, M.; Weiner, J.H.; James, M.N.
Crystal structure of sulfide:quinone oxidoreductase from Acidithiobacillus ferrooxidans: insights into sulfidotrophic respiration and detoxification
J. Mol. Biol.
398
292-305
2010
Acidithiobacillus ferrooxidans (B7JBP8), Acidithiobacillus ferrooxidans
brenda
Theissen, U.; Hoffmeister, M.; Grieshaber, M.; Martin, W.
Single eubacterial origin of eukaryotic sulfide:quinone oxidoreductase, a mitochondrial enzyme conserved from the early evolution of eukaryotes during anoxic and sulfidic times
Mol. Biol. Evol.
20
1564-1574
2003
Arenicola marina, Geukensia demissa, Heteromastus filiformis, Solemya reidi, Schizosaccharomyces pombe (O94284)
brenda
Marcia, M.; Ermler, U.; Peng, G.; Michel, H.
The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration
Proc. Natl. Acad. Sci. USA
106
9625-9630
2009
Aquifex aeolicus (O67931), Aquifex aeolicus
brenda
Marcia, M.; Ermler, U.; Peng, G.; Michel, H.
A new structure-based classification of sulfide:quinone oxidoreductases
Proteins
78
1073-1083
2010
Acidianus ambivalens, Aquifex aeolicus (O67931)
brenda
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
Linden, D.; Furne, J.; Stoltz, G.; Abdel-Rehim, M.; Levitt, M.; Szurszewski, J.
Sulphide quinone reductase contributes to hydrogen sulphide metabolism in murine peripheral tissues but not in the CNS
Br. J. Pharmacol.
165
2178-2190
2012
Mus musculus
brenda
Cherney, M.; Zhang, Y.; James, M.; Weiner, J.
Structure-activity characterization of sulfide:quinone oxidoreductase variants
J. Struct. Biol.
178
319-328
2012
Acidithiobacillus ferrooxidans (B7JBP8), Acidithiobacillus ferrooxidans, Acidithiobacillus ferrooxidans DSM 14882 (B7JBP8)
brenda
Ma, Y.; Zhang, Z.; Shao, M.; Kang, K.; Shi, X.; Dong, Y.; Li, J.
Response of sulfide: quinone oxidoreductase to sulfide exposure in the echiuran worm Urechis unicinctus
Mar. Biotechnol.
14
245-251
2012
Urechis unicinctus
brenda
Ackermann, M.; Kubitza, M.; Maier, K.; Brawanski, A.; Hauska, G.; Pina, A.L.
The vertebrate homolog of sulfide-quinone reductase is expressed in mitochondria of neuronal tissues
Neuroscience
199
1-12
2011
Rattus norvegicus (B0BMT9)
brenda
Lencina, A.M.; Ding, Z.; Schurig-Briccio, L.A.; Gennis, R.B.
Characterization of the type III sulfide:quinone oxidoreductase from Caldivirga maquilingensis and its membrane binding
Biochim. Biophys. Acta
1827
266-275
2013
Caldivirga maquilingensis, Caldivirga maquilingensis IC-167
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
Zhang, Y.; Weiner, J.
Characterization of the kinetics and electron paramagnetic resonance spectroscopic properties of Acidithiobacillus ferrooxidans sulfide quinone oxidoreductase (SQR)
Arch. Biochem. Biophys.
564
110-119
2014
Acidithiobacillus ferrooxidans (B7JBP8)
brenda
Ackermann, M.; Kubitza, M.; Hauska, G.; Pina, A.L.
The vertebrate homologue of sulfide-quinone reductase in mammalian mitochondria
Cell Tissue Res.
358
779-792
2014
Mus musculus, Rattus norvegicus
brenda
Bauzai, A.; Quinonero, D.; Deya, P.; Frontera, A.
On the importance of anion-pi interactions in the mechanism of sulfide quinone oxidoreductase
Chem. Asian J.
8
2708-2713
2013
Acidithiobacillus ferrooxidans (B7JBP8)
brenda
Xin, Y.; Liu, H.; Cui, F.; Liu, H.; Xun, L.
Recombinant Escherichia coli with sulfide quinone oxidoreductase and persulfide dioxygenase rapidly oxidises sulfide to sulfite and thiosulfate via a new pathway
Environ. Microbiol.
18
5123-5136
2016
Cupriavidus pinatubonensis
brenda
Harb, F.; Prunetti, L.; Giudici-Orticoni, M.T.; Guiral, M.; Tinland, B.
Insertion and self-diffusion of a monotopic protein, the Aquifex aeolicus sulfide quinone reductase, in supported lipid bilayers
Eur. Phys. J. E Soft Matter
38
110
2015
Aquifex aeolicus
brenda
Shuman, K.; Hanson, T.
A sulfide quinone oxidoreductase from Chlorobaculum tepidum displays unusual kinetic properties
FEMS Microbiol. Lett.
363
1-8
2016
Chlorobaculum tepidum (Q8KDG3), Chlorobaculum tepidum
brenda
Han, Y.; Perner, M.
Sulfide consumption in Sulfurimonas denitrificans and heterologous expression of its three sulfide-quinone reductase homologs
J. Bacteriol.
198
1260-1267
2016
Sulfurimonas denitrificans, Sulfurimonas denitrificans DSM-1251
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
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