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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
- acidithiobacillus
- sulfurtransferase
-
sulfide-oxidizing
- rhodanese
-
sulfane
- ferrooxidans
- 3-mercaptopyruvate
-
anoxygenic
-
sulfur-oxidizing
-
chemolithotrophic
-
sulfide-dependent
-
echiuran
- unicinctus
- limnetica
-
urechis
-
monotopic
- oscillatoria
- tepidum
- chlorobaculum
-
sulfide-rich
- medicine
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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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CmSQR
HMT2
III SQR
SQR
Sqrdl
Suden_1879
Suden_2082
Suden_619
sulfide quinone oxidoreductase
sulfide-quinone oxidoreductase
sulfide-quinone reductase
sulfide: quinone oxidoreductase
sulfide:decylubiquinone oxidoreductase
sulfide:quinone oxidoreductase
sulfidequinone reductase-like protein
type III sulfide:quinone oxidoreductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
n HS- + n quinone = polysulfide + n quinol
-
-
-
-
n HS- + n quinone = polysulfide + n quinol
reaction mechanism, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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PATHWAY SOURCE
PATHWAYS
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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
n Na2S + n decylubiquinone
polysulfide + n decylubiquinol + 2 Na+
-
-
-
-
?
Na2S + duroquinone
polysulfide + duroquinol + 2 Na+
-
-
-
?
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
-
-
-
?
n S2- + n decylubiquinone
polysulfide + n decylubiquinol
-
Na2S
-
-
?
n S2- + n decylubiquinone
polysulfide + n decylubiquinol
-
Na2S
-
-
?
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
?
-
-
quinone binding site structure analysis and binding mechanism by CmSQR, overview
-
-
-
additional information
?
-
-
quinone binding site structure analysis and binding mechanism by CmSQR, overview
-
-
-
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
-
-
?
additional information
?
-
SQR oxidizes sulfide to polysulfide, which spontaneously reacts with glutathione (GSH) to produce glutathione persulfide (GSSH), PDO oxidizes GSSH to sulfite, which spontaneously reacts with polysulfide to produce thiosulfate
-
-
-
additional information
?
-
sulfide-dependent duroquinone-reducing activity of purified wild-type and single cysteine mutant TrSqrF variants, overview
-
-
-
additional information
?
-
-
sulfide-dependent duroquinone-reducing activity of purified wild-type and single cysteine mutant TrSqrF variants, overview
-
-
-
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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
-
-
?
additional information
?
-
SQR oxidizes sulfide to polysulfide, which spontaneously reacts with glutathione (GSH) to produce glutathione persulfide (GSSH), PDO oxidizes GSSH to sulfite, which spontaneously reacts with polysulfide to produce thiosulfate
-
-
-
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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
FAD
-
residues Gly12, Gly16, Ala77, and Pro44 are determined to be important for flavin binding, binding structure analysis, overview
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NaHS
the growth of the DELTAsqr mutant is fully inhibited while the wild-type and the complementation strain are partly inhibited after treatment with 4-5 mM NaHS
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%
iodoacetamide
can irreversibly inactivate TrSqrF but only if substrates are present and the enzyme is actively catalyzing its reaction. When the enzyme is inhibited by iodoacetamide, the FAD cofactor is released. The inhibition studies support a mechanism that entails opening and reforming of the heterodisulfide bridge during the catalytic cycle of TrSqrF
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
-
additional information
detailed structure-function analysis of the type VI SQR enzyme which enables the proposal of a distinct mechanism of sulfide oxidation for this class. For catalysis of sulfide oxidation, all SQRs require FAD cofactor and a redox-active centre in the active site, usually formed between conserved essential cysteines. SQRs of different types have variation in the number and position of cysteines, highlighting the potential for diverse catalytic mechanisms. The photosynthetic purple sulfur bacterium, Thiocapsa roseopersicina contains a type VI SQR enzyme (TrSqrF) having unusual catalytic parameters and four cysteines likely involved in the catalysis. TrSqrF homology structure modeling, the A chains of three structures of SqrE and SqrA enzymes of Acidianus ambivalens and Aquifex aeolicus, respectively, are selected for model building (PDB IDs 3H8L, 3HYW and 3HYV). The TrSqrF has four cysteines in the primary sequence: Cys332 is ubiquitous, while Cys121 is identified in type I, IV, V and VI SQRs and they correspond to the highly conserved Cys347 and Cys124 of Aquifex aeolicus SQR, respectively. There is no matching residue to the Cys156 of Aquifex aeolicus enzyme in the Thiocapsa roseopersicina and all other type VI SQR proteins. The Cys272 is a unique, characteristic conserved cysteine of the type VI SQRs. Based on the available SQR structures, the corresponding amino acids of this cysteine in type I and type V SQR proteins are localized in a surface loop. The TrSqrF also contains a cysteine residue (Cys49) which is not conserved within any SQR type
-
additional information
-
detailed structure-function analysis of the type VI SQR enzyme which enables the proposal of a distinct mechanism of sulfide oxidation for this class. For catalysis of sulfide oxidation, all SQRs require FAD cofactor and a redox-active centre in the active site, usually formed between conserved essential cysteines. SQRs of different types have variation in the number and position of cysteines, highlighting the potential for diverse catalytic mechanisms. The photosynthetic purple sulfur bacterium, Thiocapsa roseopersicina contains a type VI SQR enzyme (TrSqrF) having unusual catalytic parameters and four cysteines likely involved in the catalysis. TrSqrF homology structure modeling, the A chains of three structures of SqrE and SqrA enzymes of Acidianus ambivalens and Aquifex aeolicus, respectively, are selected for model building (PDB IDs 3H8L, 3HYW and 3HYV). The TrSqrF has four cysteines in the primary sequence: Cys332 is ubiquitous, while Cys121 is identified in type I, IV, V and VI SQRs and they correspond to the highly conserved Cys347 and Cys124 of Aquifex aeolicus SQR, respectively. There is no matching residue to the Cys156 of Aquifex aeolicus enzyme in the Thiocapsa roseopersicina and all other type VI SQR proteins. The Cys272 is a unique, characteristic conserved cysteine of the type VI SQRs. Based on the available SQR structures, the corresponding amino acids of this cysteine in type I and type V SQR proteins are localized in a surface loop. The TrSqrF also contains a cysteine residue (Cys49) which is not conserved within any SQR type
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Rhodanese
speeds up the reaction of polysulfide with glutathione (GSH) to produce glutathione persulfide (GSSH)
-
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
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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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
0.0274
duroquinone
recombinant wild-type enzyme, pH 8.0, 25°C
0.0358
duroquinone
recombinant mutant C332A, pH 8.0, 25°C
0.0419
duroquinone
recombinant mutant C272A, pH 8.0, 25°C
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
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten steady-state kinetic study of the mutant versus wild-type enzymes
-
additional information
additional information
-
Michaelis-Menten steady-state kinetic study of the mutant versus wild-type enzymes
-
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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
1.64
duroquinone
recombinant wild-type enzyme, pH 8.0, 25°C
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
59.85
duroquinone
recombinant wild-type enzyme, pH 8.0, 25°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
0.015
iodoacetamide
Thiocapsa roseopersicina
recombinant mutant C332A, pH 8.0, 25°C
0.086
iodoacetamide
Thiocapsa roseopersicina
recombinant mutant C272A, pH 8.0, 25°C
0.131
iodoacetamide
Thiocapsa roseopersicina
recombinant mutant C49A, pH 8.0, 25°C
0.134
iodoacetamide
Thiocapsa roseopersicina
recombinant wild-type enzyme, pH 8.0, 25°C
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
2 - 10
-
activity range, SQR activity decreases rapidly at the pH above 8.0 and also below pH 5.0. There is no SQR activity found at pH above 10.0 and at pH below 2.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
40
80
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 60
-
SQR activity is gradually decreased at temperature below 30°C and above 40°C
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
CpSQR is located on the cytoplasmic side of the membrane
-
brenda
additional information
localization of SQR and PDO inside the cytoplasm in the vicinity of the membrane
-
brenda
periplasmic surface of the cytoplasmic membrane
-
brenda
-
periplasmic surface of the cytoplasmic membrane
-
-
brenda
-
the C-terminal amphiphilic helix is important for membrane binding
brenda
-
CmSQR oligomerization is necessary for membrane binding, analysis of the binding of recombiant hetero-oligomers of differentially tagged CmSQR mutant variants
brenda
-
the C-terminal amphiphilic helix is important for membrane binding
-
brenda
-
CmSQR oligomerization is necessary for membrane binding, analysis of the binding of recombiant hetero-oligomers of differentially tagged CmSQR mutant variants
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
SQR proteins are classified into six types (types I-VI, SqrA-F). The photosynthetic purple sulfur bacterium, Thiocapsa roseopersicina contains a type VI SQR enzyme (TrSqrF) having unusual catalytic parameters and four cysteines likely involved in the catalysis. Multiple sequence alignment of selected representative SQR proteins with conserved cysteines in the primary sequence of various sulfide:quinone oxidoreductases (Aquifex aeolicus and Thiocapsa roseopersicina residue numbering) with approximate location of conserved cysteines in relation to the isoalloxazine ring of FAD, based on the structures of various sulfide:quinone oxidoreductases, overview
evolution
-
SQRs belong to the two-dinucleotide-binding-domains flavoprotein (tDBDF) superfamily, characterized by the presence of two Rossmann fold domains known to stabilize the adenosine moieties of dinucleotides (e.g. FAD and NADH). SQRs are typically oligomeric flavoproteins with multiple copies of a single subunit of molecular mass of about 50 kDa. SQRs are associated with the prokaryotic cytoplasmic or periplasmic membrane or the inner mitochondrial membrane
evolution
-
SQRs belong to the two-dinucleotide-binding-domains flavoprotein (tDBDF) superfamily, characterized by the presence of two Rossmann fold domains known to stabilize the adenosine moieties of dinucleotides (e.g. FAD and NADH). SQRs are typically oligomeric flavoproteins with multiple copies of a single subunit of molecular mass of about 50 kDa. SQRs are associated with the prokaryotic cytoplasmic or periplasmic membrane or the inner mitochondrial membrane
-
malfunction
a DELTAsqr mutant contains less cellular sulfur (S0) and has increased expression of key genes involved in photosynthesis, but it is less competitive than the wild-type in cocultures. Strain PCC7002 uses SQR to detoxify exogenous sulfide, enabling it to survive better than its DELTAsqr mutant in sulfide-rich environments. The wild-type strain PCC7002 and the complementation strain PCC7002DELTAsqr::sqr do not accumulate sulfide, but the mutant DELTAsqr does. The DELTAsqr mutant has a higher oxygen evolution rate than the wild-type. The increased oxygen evolution rate upon the DELTAsqr mutant is consistent with an acceleration of H2O oxidation to make up for the loss of H2S oxidation, phenotype, overview
malfunction
enzyme Sqr knockout leads to morphological changes and functional deficiencies of mitochondria and apoptosis in Schizosaccharomyces pombe. The Sqr knockout strain displays the same phenotypes as the cysteine-synthesis-deficient strain. Cysteine addition complements the effects caused by Sqr knockout. Sqr knockout also results in physiological changes. The DELTAsqr strain shows reduced cell viability compared to the wild-type strain when cultivated in YES medium. There are more cells of early apoptosis in DELTAsqr culture than that in wild-type culture. Sqr knockout impaires mitochondrial health. Phenotypes and transcription and metabolism changes caused by sqr knockout, overview
malfunction
-
enzyme Sqr knockout leads to morphological changes and functional deficiencies of mitochondria and apoptosis in Schizosaccharomyces pombe. The Sqr knockout strain displays the same phenotypes as the cysteine-synthesis-deficient strain. Cysteine addition complements the effects caused by Sqr knockout. Sqr knockout also results in physiological changes. The DELTAsqr strain shows reduced cell viability compared to the wild-type strain when cultivated in YES medium. There are more cells of early apoptosis in DELTAsqr culture than that in wild-type culture. Sqr knockout impaires mitochondrial health. Phenotypes and transcription and metabolism changes caused by sqr knockout, overview
-
malfunction
-
enzyme Sqr knockout leads to morphological changes and functional deficiencies of mitochondria and apoptosis in Schizosaccharomyces pombe. The Sqr knockout strain displays the same phenotypes as the cysteine-synthesis-deficient strain. Cysteine addition complements the effects caused by Sqr knockout. Sqr knockout also results in physiological changes. The DELTAsqr strain shows reduced cell viability compared to the wild-type strain when cultivated in YES medium. There are more cells of early apoptosis in DELTAsqr culture than that in wild-type culture. Sqr knockout impaires mitochondrial health. Phenotypes and transcription and metabolism changes caused by sqr knockout, overview
-
metabolism
-
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
in Schizosaccharomyces pombe, Sqr is the main reactive sulfur species (RSS) producer in mitochondria, and RSS instead of H2S is used by cysteine synthase to synthesize cysteine. In terms of RSS metabolism, Schizosaccharomyces pombe does not contain genes encoding cystathionine beta-synthase (Cbs), cystathionine gamma-lyase (Cse), cysteinyl-tRNA synthetase 2 (Crs2), or persulfide dioxygenase (Pdo)
metabolism
mammalian mitochondria and heterotrophic bacteria oxidize sulfide via a pathway involving two key enzymes, sulfide:quinone oxidoreductase (SQR) and persulfide dioxygenase (PDO, EC 1.13.11.18). SQR oxidizes sulfide to polysulfide, which spontaneously reacts with glutathione (GSH) to produce glutathione persulfide (GSSH), PDO oxidizes GSSH to sulfite, which spontaneously reacts with polysulfide to produce thiosulfate. This pathway is common in heterotrophic bacteria. The relative electron transport rate (rETR) increases in the mutant
metabolism
-
in Schizosaccharomyces pombe, Sqr is the main reactive sulfur species (RSS) producer in mitochondria, and RSS instead of H2S is used by cysteine synthase to synthesize cysteine. In terms of RSS metabolism, Schizosaccharomyces pombe does not contain genes encoding cystathionine beta-synthase (Cbs), cystathionine gamma-lyase (Cse), cysteinyl-tRNA synthetase 2 (Crs2), or persulfide dioxygenase (Pdo)
-
metabolism
-
in Schizosaccharomyces pombe, Sqr is the main reactive sulfur species (RSS) producer in mitochondria, and RSS instead of H2S is used by cysteine synthase to synthesize cysteine. In terms of RSS metabolism, Schizosaccharomyces pombe does not contain genes encoding cystathionine beta-synthase (Cbs), cystathionine gamma-lyase (Cse), cysteinyl-tRNA synthetase 2 (Crs2), or persulfide dioxygenase (Pdo)
-
metabolism
-
SQR is involved in elemental sulfur oxidation in sulfur-grown cells
-
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
in bacteria, sulfide:quinone oxidoreductase (SQR) oxidizes sulfide to polysulfide, rhodanese speeds up the reaction of polysulfide with glutathione (GSH) to produce glutathione persulfide (GSSH), and persulfide dioxygenase (PDO) oxidizes GSSH to sulfite, which spontaneously reacts with polysulfide to produce thiosulfate. Ubiquinone is a cosubstrate in the reaction
physiological function
-
sulfide:quinone oxidoreductase (SQR) is a monotopic membrane flavoprotein present in all domains of life, with multiple roles including sulfide detoxification, homeostasis and energy generation by providing electrons to respiratory or photosynthetic electron transport chains
physiological function
sulfide:quinone oxidoreductase (Sqr), which oxidizes hydrogen sulfide to reactive sulfur species (RSS), is indispensable to mitochondria health in the eukaryotic model microorganism Schizosaccharomyces pombe. RSS play critical functions in the cell, such as signaling, redox homeostasis maintenance, and metabolic regulation
physiological function
the toxic effect of sulfide is well known, inhibiting respiration by acting on cytochrome c oxidase in heterotrophic bacteria and photosynthesis by binding to metalloproteins of photosynthesis system II (PSII). Sulfide can reach high concentrations in specific habitats, such as hydrothermal vents and seeps and coastal mudflats. Synechococcus sp. strain PCC 7002 uses sulfide:quinone oxidoreductase to detoxify exogenous sulfide and to convert endogenous sulfide to cellular sulfane sulfur. SQR plays a detoxification role. Strain PCC7002 with SQR and persulfide dioxygenase (PDO, EC 1.13.11.18) oxidizes exogenous sulfide to tolerate high sulfide levels. Common presence of SQR in cyanobacteria. SQRs are widely distributed in microorganisms as well as in animal mitochondria. SQR oxidizes sulfide to polysulfide and transfers electrons into the electron transport chain in mitochondria, heterotrophic bacteria, chemolithotrophic bacteria, and photolithotrophic bacteria
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 oxidoreductase (SQR) is a monotopic membrane flavoprotein present in all domains of life, with multiple roles including sulfide detoxification, homeostasis and energy generation by providing electrons to respiratory or photosynthetic electron transport chains
-
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 oxidoreductase (Sqr), which oxidizes hydrogen sulfide to reactive sulfur species (RSS), is indispensable to mitochondria health in the eukaryotic model microorganism Schizosaccharomyces pombe. RSS play critical functions in the cell, such as signaling, redox homeostasis maintenance, and metabolic regulation
-
physiological function
-
sulfide:quinone oxidoreductase (Sqr), which oxidizes hydrogen sulfide to reactive sulfur species (RSS), is indispensable to mitochondria health in the eukaryotic model microorganism Schizosaccharomyces pombe. RSS play critical functions in the cell, such as signaling, redox homeostasis maintenance, and metabolic regulation
-
additional information
reactive sulfur species (RSS) include inorganic polysulfide (HSnH, n>2), organic polysulfide (RSnH, n>2), and polysulfane (RSnR, n>2)
additional information
-
residue Gly299 is only important for quinone reduction despite its proximity to bound FAD. Residues Phe337 and Phe362 are also important for quinone binding apparently by direct interaction with the quinone ring, whereas Lys359, postulated to hydrogen bond to the quinone, seems to have a more structural role. Three-dimensional homology model of Caldivirga maquilingensis SQR
additional information
structure homology modelling, molecular mechanics and molecular dynamics calculations, overview. Analysis of interactions between the protein and ligands, calculation of solvent accessible surface (SAS) and energy value. The structural stability of the alpha-helix in the C-terminus of enzyme SQR has an important influence on the structural stability of the whole protein
additional information
sulfane sulfur is zero valence sulfur in various forms, such as persulfide (RSSH), polysulfide (RSSnH and RSSnR, nx022), and elemental sulfur. Sulfane sulfur can act as either an electrophile or a nucleophile. The nucleophilic property allows cells to resist reactive oxygenspecies, and the electrophilic property causes protein persulfidation, affecting enzyme activities or signaling
additional information
-
residue Gly299 is only important for quinone reduction despite its proximity to bound FAD. Residues Phe337 and Phe362 are also important for quinone binding apparently by direct interaction with the quinone ring, whereas Lys359, postulated to hydrogen bond to the quinone, seems to have a more structural role. Three-dimensional homology model of Caldivirga maquilingensis SQR
-
additional information
-
reactive sulfur species (RSS) include inorganic polysulfide (HSnH, n>2), organic polysulfide (RSnH, n>2), and polysulfane (RSnR, n>2)
-
additional information
-
reactive sulfur species (RSS) include inorganic polysulfide (HSnH, n>2), organic polysulfide (RSnH, n>2), and polysulfane (RSnR, n>2)
-
Show AA Sequence and Transmembrane Helices (131 entries)
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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
oligomer
oligomer
-
oligomerization of CmSQR does not involve the membrane binding domain, importance of the C-terminal region for oligomerization. CmSQR oligomerization is necessary for membrane binding
oligomer
-
oligomerization of CmSQR does not involve the membrane binding domain, importance of the C-terminal region for oligomerization. CmSQR oligomerization is necessary for membrane binding
-
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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
-
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
-
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
-
about 35% of wild-type activity in assay with decylubiquinone
-
C160A
-
loss of activity in assay with decylubiquinone, about 35% of wild-type activity for reduction of FAD fluorescence by Na2S
-
H132A
-
about 40% of wild-type activity in assay with decylubiquinone
-
H198A
-
about 60% of wild-type activity in assay with decylubiquinone
-
S126A
-
about 35% of wild-type activity in assay with decylubiquinone
-
L379D
L379D/M380N
L379N
M380N
Y383Q/F384K
Y383Q/F384K/L379D/M380N
-
the mutant protein is found entirely in the cytoplasmic fraction but there is no catalytic activity
L379D/M380N
-
both the membrane-bound and soluble forms of this protein are inactive
-
Y383Q/F384K
Y383Q/F384K/L379D/M380N
-
the mutant protein is found entirely in the cytoplasmic fraction but there is no catalytic activity
-
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
C121A
site-directed mutagenesis of gene sqrF, inactive mutant
C272A
site-directed mutagenesis of gene sqrF, the mutant is more sensitive to iodoacetamide inhibition compared to wild-type. The kcat of the C272A variant slightly decreases, and the affinity of the C272A mutant for duroquinone is lower (increased Km) than those of the wild-type TrSqrF enzyme, but the mutated enzyme has a similar affinity for the sulfide substrate
C332A
site-directed mutagenesis of gene sqrF, the mutant is much more sensitive to iodoacetamide inhibition compared to wild-type. The kcat and the Vmax values for the C332A variant catalyzed reaction are each one order of magnitude smaller than those data obtained with the wild-type enzyme which coincides with the significantly diminished specific activity measured for this mutant enzyme
C49A
site-directed mutagenesis of gene sqrF, the C49A enzyme has slightly increased Vmax and kcat values as compared to those of wild-type TrSqrF, but decreased affinity for the sulfide substrate
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
-
all of the expressed protein is membrane-bound, the mutant enzyme is inactive
L379D
-
inactive mutant enzyme, all of the expressed protein is membrane-bound
L379D/M380N
-
both the membrane-bound and soluble forms of this protein are inactive
L379D/M380N
-
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
-
all of the expressed protein is membrane-bound, the mutant enzyme is inactive
L379N
-
the mutant enzyme is inactive due to a perturbation of the decylubiquinone binding site
M380N
-
mutation results in protein that is entirely membrane-bound, but which has the same activity as wild type enzyme
M380N
-
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
-
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
-
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
-
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
-
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
-
additional information
-
sulfide present in the up-flow anaerobic sludge blanket (UASB)-treated post tanning wastewater is oxidized into elemental sulfur using sulfide:quinone oxidoreductase (SQR) immobilized on functionalized carbon-silica matrix (FCSM) in a packed bed reactor. Optimum conditions for immobilization of SQR onto FCSM are pH, 7.0, 40°C, and 10mg/g SQR during 240 min. The immobilization of SQR onto FCSM obeys the Langmuir isotherm model. The maximum sulfide oxidation is 99% at HRT of 15 h with residual sulfide of 2.4 mg/l. The formation of elemental Sulphur is confirmed by XRD studies. Enzyme immobilization method evaluation and optimization, adsorption kinetics and thermodynamics, detailed overview
additional information
-
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
-
construction of soluble mutant variants, unable to bind to the membrane, lacking either four hydrophobic residues from the last C-terminal helix (quadruple-mutant or YL), the complete last C-terminal helix (truncated 1 or T1) or the last two C-terminal helices (truncated 2 or T2). Localization study of tagged wild-type and mutant enzymes and enzyme fragments in Escherichia coli cells, overview
additional information
-
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
-
construction of soluble mutant variants, unable to bind to the membrane, lacking either four hydrophobic residues from the last C-terminal helix (quadruple-mutant or YL), the complete last C-terminal helix (truncated 1 or T1) or the last two C-terminal helices (truncated 2 or T2). Localization study of tagged wild-type and mutant enzymes and enzyme fragments in Escherichia coli cells, overview
-
additional information
for analysis of the membrane association of CpSQR: construction of C-terminally truncated CpSQR mutants containing the N-terminal fragment sx, where x stands for the number of amino acid residues from the N terminus (x = 26, 49, 71, 83, 107, 115, 128, 157, 176, 230, 359, or 450). Generation of a CpSQR-PhoA fusion protein and comparison with the TolB-PhoA fusion protein. Cells with the fusion of CpSQR and PhoA show SQR activity, while other fusions with SQR fragments have no SQR activity, full-length PhoA and TolB-PhoA are used as the positive controls
additional information
-
preparation and analysis of sulfide:quinone oxidoreductase immobilized carbon matrix for the treatment of sulfide rich post-tanning wastewater. Enzyme production is optimized using respone surface methodology. Optimized conditions for enzyme immobilization from cell-free enzyme exract on carbon silica matrix (CSM) are pH 7.0, 40°C, and enzyme protein concentration of 7 mg/g over 300 min, while on functionalized carbon silica matrix (FCSM) they are pH 7.0, 40°C, and enzyme protein concentration of 10 mg/g over 240 min. The CSM-SQR packed bed reactors remove 99% with residual 3 mg/l sulfide at optimum hydraulic retention time (HRT) of 15 h, the FCSM-SQR packed bed reactors remove 99% with residual 2.5 mg/l sulfide at optimum hydraulic retention time (HRT) of 9 h. Method development and evaluation, overview
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
-
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
-
additional information
construction and analysis of an enzyme knockout strain DELTAsqr, phenotypes, overview
additional information
-
construction and analysis of an enzyme knockout strain DELTAsqr, phenotypes, overview
-
additional information
-
construction and analysis of an enzyme knockout strain DELTAsqr, phenotypes, overview
-
additional information
recombinant Escherichia coli expressing SQR and PDO from strain PCC7002 oxidizes sulfide to sulfite and thiosulfate
additional information
construction of enzyme mutants with reduced activity compared to wild-type
additional information
construction of a Thiocapsa roseopersicina fcc, sqrD, and sqrF deletion mutant strain FOQRON from wild-type strain FOQR. Results with the C332A mutant TrSqrF variant are immediately more evident than the C49 and C272 mutations
additional information
-
construction of a Thiocapsa roseopersicina fcc, sqrD, and sqrF deletion mutant strain FOQRON from wild-type strain FOQR. Results with the C332A mutant TrSqrF variant are immediately more evident than the C49 and C272 mutations
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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
-
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
-
ammonium sulfate precipitation, phenyl-Toyopearl column chromatography, and TSKgel G3000 gel filtration
-
ammonium sulfate precipitation, phenyl-TSK column chromatography, T SK-gel filtration and analytical gel filtration
-
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
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain C43(DE3) by nickel affinity chromatography, dialysis, ultracentrifugation at 230000 x g, followed by solubilization with dodecyl-beta-D-maltoside and another step of nickel affinity chromatography
-
recombinant His6-tagged wild-type enzyme and mutants from Escherichia coli by nickel affinity chromatography
recombinant StrepII-tagged enzyme point mutants from Thiocapsa roseopersicina cells by affinity chromatography to homogeneity
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
-
expressed in the Rhodobacter capsulatus SB1003 sqr deletion mutant
-
expression at low temperature in Escherichia coli by using an optimized synthetic gene and cold-adapted chaperonins
expression in Escherichia coli
gene sqr, recombinant expression of GFP-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene sqr, recombinant expression of His- or FLAG-tagged wild-type and mutant enzymes in Escherichia coli strain C43(DE3)
-
gene sqr, recombinant expression of His6-tagged wild-type enzyme and mutants in Escherichia coli
gene sqrF, recombinant expression of StrepII-tagged enzyme point mutants in Escherichia coli S17-1 lambda pir cell line and in Thiocapsa roseopersicina cells
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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
-
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
environmental protection
-
anaerobic treatment of sulphate rich wastewater results in high amount of sulfide in liquid phase and gaseous phase. Sulfide is malodorous in gaseous phase and toxic even at very low concentrations in liquid phase and causes objectionable environmental issues. Sulfide present in the up-flow anaerobic sludge blanket (UASB)-treated post tanning wastewater is oxidized into elemental sulfur using sulfide:quinone oxidoreductase (SQR) immobilized on functionalized carbon-silica matrix (FCSM) in a packed bed reactor. Optimum conditions for immobilization of SQR onto FCSM are pH, 7.0, 40°C, and 10mg/g SQR during 240 min. The immobilization of SQR onto FCSM obeys the Langmuir isotherm model. The maximum sulfide oxidation is 99% at HRT of 15 h with residual sulfide of 2.4 mg/l. The formation of elemental Sulphur is confirmed by XRD studies
medicine
-
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
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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
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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
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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
Gao, R.; Liu, H.; Xun, L.
Cytoplasmic localization of sulfide quinone oxidoreductase and persulfide dioxygenase of Cupriavidus pinatubonensis JMP134
Appl. Environ. Microbiol.
83
e01820-17
2017
Cupriavidus pinatubonensis (Q46V88)
brenda
Mahesh, M.; Swarnalatha, S.; Gnanamani, A.; Sekaran, G.
Preparation and characterization of sulfide quinone oxidoreductase immobilized carbon matrix for the treatment of sulphide rich post-tanning wastewater
Biocatal. Agricult. Biotechnol.
23
101457
2020
Exiguobacterium aurantiacum
-
brenda
Mannacharaju, M.; Chittybabu, S.; Sheikh John, S.; Somasundaram, S.; Ganesan, S.
Bio catalytic oxidation of sulphide laden wastewater from leather industry using sulfide Quinone oxidoreductase immobilized bio reactor
Biocatal. Biotransform.
38
123-137
2020
Alkalihalobacillus clausii
-
brenda
Lencina, A.M.; Gennis, R.B.; Schurig-Briccio, L.A.
The oligomeric state of the Caldivirga maquilingensis type III sulfide quinone oxidoreductase is required for membrane binding
Biochim. Biophys. Acta
1861
148132
2020
Caldivirga maquilingensis, Caldivirga maquilingensis IC-167
brenda
Duzs, A.; Miklovics, N.; Paragi, G.; Rakhely, G.; Toth, A.
Insights into the catalytic mechanism of type VI sulfide quinone oxidoreductases
Biochim. Biophys. Acta
1862
148337
2021
Thiocapsa roseopersicina (A0A1Z2RRG1), Thiocapsa roseopersicina
brenda
Liu, D.; Zhang, J.; Lue, C.; Xia, Y.; Liu, H.; Jiao, N.; Xun, L.; Liu, J.
Synechococcus sp. strain PCC 7002 uses sulfide quinone oxidoreductase to detoxify exogenous sulfide and to convert endogenous sulfide to cellular sulfane sulfur
mBio
11
e03420-19
2020
Synechococcus sp. PCC 7002 (B1XRD0)
brenda
Chen, X.; Meng, Z.; Luo, Y.; Rong, X.; Li, S.
Structure and activity of sulfide quinone oxidoreductase and its mutants from Thiobacillus denitrificans ATCC 25259
Mod. Food Sci. Technol.
33
46-55
2017
Thiobacillus denitrificans (Q8KQ39)
-
brenda
Zhang, X.; Xin, Y.; Chen, Z.; Xia, Y.; Xun, L.; Liu, H.
Sulfide-quinone oxidoreductase is required for cysteine synthesis and indispensable to mitochondrial health
Redox Biol.
47
102169
2021
Schizosaccharomyces pombe (O94284), Schizosaccharomyces pombe ATCC 24843 (O94284), Schizosaccharomyces pombe 972 (O94284)
brenda
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