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2 sulfide + ubiquinone-1
hydrogen disulfide + ubiquinol-1
-
-
-
?
HS- + quinone
polysulfide + quinol
-
-
-
-
?
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 + caldariellaquinone
sulfur + caldariellaquinol
-
-
-
-
?
sulfide + coenzyme Q
sulfane sulfur + reduced coenzyme Q
-
-
-
-
?
sulfide + coenzyme Q
sulfur + reduced coenzyme Q
-
-
-
-
?
sulfide + coenzyme Q1
sulfur + reduced coenzyme Q1
-
-
-
-
?
sulfide + coenzyme Q10
sulfur + reduced coenzyme Q10
-
-
-
-
?
sulfide + cyanide + coenzyme Q
thiocyanate + reduced coenzyme Q
-
-
-
-
?
sulfide + cyanide + ubiquinone-1
thiocyanate + ubiquinol-1
-
-
-
?
sulfide + cysteine + coenzyme Q1
cysteine persulfide + reduced coenzyme Q1
-
-
-
-
?
sulfide + decylubiquinone
polysulfide + decylubiquinol
sulfide + decylubiquinone
sulfur + decylubiquinol
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
sulfur + duroquinol
sulfide + duroquinone 23
sulfur + duroquinol 23
-
% compared to the activity with decylubiquinone
-
-
?
sulfide + glutathione
sulfur + reduced glutathione
-
-
-
-
?
sulfide + homocysteine + coenzyme Q1
homocysteine persulfide + reduced coenzyme Q1
-
-
-
-
?
sulfide + menadione
polysulfide + menadiol
-
25% compared to the activity with decylubiquinone
-
-
?
sulfide + menadione
sulfur + menadiol
sulfide + plastoquinone-1
sulfur + plastoquinol-1
sulfide + plastoquinone-2
sulfur + plastoquinol-2
-
highest activity
-
-
?
sulfide + quinone
elemental sulfur + quinol
-
-
-
-
?
sulfide + quinone
sulfur + quinol
sulfide + reduced glutathione + coenzyme Q1
glutathione persulfide + reduced coenzyme Q1
-
-
-
-
?
sulfide + sulfide + coenzyme Q
hydrogen disulfide + reduced coenzyme Q
-
-
-
-
?
sulfide + sulfite + coenzyme Q
thiosulfate + reduced coenzyme Q
-
-
-
-
?
sulfide + sulfite + ubiquinone-1
thiosulfate + ubiquinol-1
-
-
-
?
sulfide + ubiquinone
? + ubiquinol
sulfide + ubiquinone-1
sulfur + ubiquinol-1
sulfide + ubiquinone-2
sulfur + ubiquinol-2
sulfide + ubiquinone-4
sulfur + ubiquinol-4
-
-
-
?
sulfide + ubiquinone-9
sulfur + ubiquinol-9
-
-
-
?
additional information
?
-
sulfide + decylubiquinone

polysulfide + decylubiquinol
-
-
-
-
?
sulfide + decylubiquinone
polysulfide + decylubiquinol
-
-
-
-
?
sulfide + decylubiquinone
polysulfide + decylubiquinol
-
-
-
-
?
sulfide + decylubiquinone
polysulfide + decylubiquinol
-
-
-
-
?
sulfide + decylubiquinone

sulfur + decylubiquinol
-
-
-
-
?
sulfide + decylubiquinone
sulfur + decylubiquinol
-
-
-
?
sulfide + decylubiquinone
sulfur + decylubiquinol
-
-
-
-
?
sulfide + decylubiquinone
sulfur + decylubiquinol
-
-
-
-
?
sulfide + decylubiquinone
sulfur + decylubiquinol
-
-
-
?
sulfide + decylubiquinone
sulfur + decylubiquinol
-
-
-
-
?
sulfide + decylubiquinone
sulfur + decylubiquinol
-
-
-
-
?
sulfide + decylubiquinone
sulfur + decylubiquinol
-
-
-
-
?
sulfide + decylubiquinone
sulfur + decylubiquinol
-
-
-
?
sulfide + decylubiquinone
sulfur + decylubiquinol
-
-
-
-
?
sulfide + decylubiquinone
sulfur + decylubiquinol
-
-
-
-
?
sulfide + decylubiquinone
sulfur + decylubiquinol
-
-
-
-
?
sulfide + decylubiquinone
sulfur + decylubiquinol
-
-
-
-
?
sulfide + decylubiquinone
sulfur + decylubiquinol
-
-
-
?
sulfide + decylubiquinone
sulfur + decylubiquinol
-
-
-
-
?
sulfide + decylubiquinone
sulfur + decylubiquinol
-
-
-
-
?
sulfide + duroquinone

sulfur + duroquinol
-
-
-
-
?
sulfide + duroquinone
sulfur + duroquinol
-
23% compared to the activity with decylubiquinone
-
-
?
sulfide + duroquinone
sulfur + duroquinol
-
23% compared to the activity with decylubiquinone
-
-
?
sulfide + duroquinone
sulfur + duroquinol
-
-
-
-
?
sulfide + menadione

sulfur + menadiol
-
-
-
-
?
sulfide + menadione
sulfur + menadiol
-
25% compared to the activity with decylubiquinone
-
-
?
sulfide + menadione
sulfur + menadiol
-
25% compared to the activity with decylubiquinone
-
-
?
sulfide + menadione
sulfur + menadiol
-
-
-
-
?
sulfide + plastoquinone-1

sulfur + plastoquinol-1
-
-
-
?
sulfide + plastoquinone-1
sulfur + plastoquinol-1
-
-
-
-
?
sulfide + plastoquinone-1
sulfur + plastoquinol-1
-
-
-
-
?
sulfide + quinone

sulfur + quinol
-
-
-
-
?
sulfide + quinone
sulfur + quinol
-
-
-
-
?
sulfide + quinone
sulfur + quinol
-
-
-
?
sulfide + quinone
sulfur + quinol
-
-
-
?
sulfide + ubiquinone

? + ubiquinol
-
-
-
-
?
sulfide + ubiquinone
? + ubiquinol
-
-
-
-
?
sulfide + ubiquinone
? + ubiquinol
-
-
-
-
?
sulfide + ubiquinone
? + ubiquinol
-
-
-
?
sulfide + ubiquinone
? + ubiquinol
-
-
-
-
?
sulfide + ubiquinone-1

sulfur + ubiquinol-1
-
-
-
?
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
-
-
?
sulfide + ubiquinone-1
sulfur + ubiquinol-1
-
-
-
-
?
sulfide + ubiquinone-1
sulfur + ubiquinol-1
-
-
-
?
sulfide + ubiquinone-2

sulfur + ubiquinol-2
-
-
-
-
?
sulfide + ubiquinone-2
sulfur + ubiquinol-2
-
-
-
-
?
sulfide + ubiquinone-2
sulfur + ubiquinol-2
-
-
-
-
?
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
-
-
-
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2 - 3
cysteine
-
pH 7.4, 25°C
0.002 - 0.036
decylubiquinone
22
homocysteine
-
pH 7.4, 25°C
0.031 - 0.04
plastoquinone-1
22
reduced glutathione
-
pH 7.4, 25°C
0.0054 - 0.0199
ubiquinone-1
0.014
ubiquinone-2
-
apparent value, at pH 7.0, temperature not specified in the publication
0.0016
ubiquinone-4
-
in 50 mM Tris-HCl, pH 7.4, 40°C; pH 7.4, temperature not specified in the publication
0.00643
ubiquinone-9
-
in 50 mM Tris-HCl, pH 7.4, 40°C; pH 7.4, 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

-
cosubstrates sulfide, ubiquinone-1, pH 8.5, 25°C
0.65
cyanide
-
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
2.6
cyanide
-
20 mM Tris-HCl, pH 8.0, at 22°C
0.002
decylubiquinone

-
in 10 mM bis-Tris-HCl, pH 6.5, temperature not specified in the publication
0.00216
decylubiquinone
-
in 50 mM Tris-HCl, pH 7.4, 40°C; 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; 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
0.005
decylubiquinone
-
in 50 mM Bis-Tris (pH 7.0), at 20°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
0.0064
decylubiquinone
-
20 mM Tris-HCl, pH 8.0, at 22°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; pH 7.5, 60°C, 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
0.00297
Sulfide
-
wild type enzyme, at pH 7.0 and 23°C
0.005
Sulfide
-
wild type enzyme, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication
0.005
Sulfide
-
mutant enzyme H132A, at pH 7.0 and 23°C
0.00553
Sulfide
-
mutant enzyme C128S, at pH 7.0 and 23°C
0.0056
Sulfide
-
mutant enzyme C128A, at pH 7.0 and 23°C
0.00594
Sulfide
-
in 50 mM Tris-HCl, pH 7.4, 40°C; pH 7.4, temperature not specified in the publication
0.008
Sulfide
-
in 10 mM HEPES, pH 7.4, 10 mM MgCl, 10 mM KCl, at 22°C
0.0109
Sulfide
-
cosubstrates cyanide, ubiquinone-1, pH 8.5, 25°C
0.0109
Sulfide
-
with coenzyme Q and cyanide as cosubstrates, at pH 8.0 and 25°C
0.011
Sulfide
-
in 50 mM Bis-Tris (pH 7.0), at 20°C
0.011
Sulfide
-
mutant enzyme H131A, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication
0.013
Sulfide
-
cosubstrates sulfite, ubiquinone-1, pH 7.5, 25°C
0.013
Sulfide
-
with coenzyme Q and sulfite as cosubstrates, at pH 8.0 and 25°C
0.015
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
0.073
Sulfide
-
pH 7.5, 60°C, membrane-bound mutant enzyme M380N
0.077
Sulfide
-
pH 7.5, 60°C, cytoplasmic mutant enzyme Y383Q/F384K; pH 7.5, 60°C, membrane-bound wild-type enzyme; pH 7.5, 60°C, wild-type enzyme
0.23
Sulfide
-
20 mM Tris-HCl, pH 8.0, at 22°C
0.23
Sulfide
-
enzyme in nanodiscs, at pH 6.8 and 25°C
0.315
Sulfide
-
cosubstrates sulfide, ubiquinone-1, pH 7.0, 25°C
0.315
Sulfide
-
with coenzyme Q as cosubstrate, at pH 8.0 and 25°C
0.32
Sulfide
-
pH 7.4, 25°C
0.35
Sulfide
-
solubilized enzyme, at pH 6.8 and 25°C
0.4
Sulfide
-
Km above 0.4 mM, mutant enzyme V300D, in 250 mM Tris-HCl (pH 8.0), temperature not specified in the publication
1.95
Sulfide
recombinant enzyme, at pH 7.4 and 47°C
0.174
sulfite

-
cosubstrates sulfide, ubiquinone-1, pH 7.5, 25°C
0.174
sulfite
-
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
0.0054
ubiquinone-1

-
in 50 mM Tris-HCl, pH 7.4, 40°C; pH 7.4, temperature not specified in the publication
0.014
ubiquinone-1
-
cosubstrates cyanide, sulfide, pH 8.5, 25°C
0.0199
ubiquinone-1
-
cosubstrates sulfite, sulfide, pH 7.5, 25°C
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0.1
2,3-dimethyl-1,4-naphthoquinone
-
at 50°C, pH 6.5
0.43
caldariella quinone
-
at 50°C, pH 6.5
94
cysteine
-
pH 7.4, 25°C
0.38 - 1.2
decylubiquinone
92
homocysteine
-
pH 7.4, 25°C
0.15
menadione
-
at 50°C, pH 6.5
113
reduced glutathione
-
pH 7.4, 25°C
360
coenzyme Q

-
with cyanide and sulfide as cosubstrates, at pH 8.0 and 25°C
364
coenzyme Q
-
with sulfite and sulfide as cosubstrates, at pH 8.0 and 25°C
330
cyanide

-
cosubstrates sulfide, ubiquinone-1, pH 8.5, 25°C
330
cyanide
-
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
0.38
decylubiquinone

-
at 50°C, pH 6.5
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
0.1
Sulfide

-
mutant enzyme C160A, at pH 7.0 and 23°C; mutant enzyme C356S, at pH 7.0 and 23°C
0.3
Sulfide
-
mutant enzyme C198A, at pH 7.0 and 23°C
0.5
Sulfide
-
mutant enzyme C160S, at pH 7.0 and 23°C
0.6
Sulfide
-
pH 7.5, 60°C, membrane-bound wild-type enzyme
0.62
Sulfide
-
pH 7.5, 60°C, membrane-bound mutant enzyme M380N
0.82
Sulfide
-
pH 7.5, 60°C, membrane-bound mutant enzyme Y383Q/F384K
1
Sulfide
-
mutant enzyme C128A, at pH 7.0 and 23°C
1.2
Sulfide
-
pH 7.5, 60°C, cytoplasmic mutant enzyme Y383Q/F384K
1.4
Sulfide
-
mutant enzyme H132A, at pH 7.0 and 23°C
1.6
Sulfide
-
mutant enzyme C128S, at pH 7.0 and 23°C
6.5
Sulfide
-
wild type enzyme, at pH 7.0 and 23°C
18.5
Sulfide
-
with coenzyme Q as cosubstrate, at pH 8.0 and 25°C
54
Sulfide
recombinant enzyme, at pH 7.4 and 47°C
62
Sulfide
-
solubilized enzyme, at pH 6.8 and 25°C
65
Sulfide
-
cosubstrates sulfide, ubiquinone-1, pH 7.0, 25°C
65
Sulfide
-
with coenzyme Q as cosubstrate, at pH 8.0 and 25°C
74
Sulfide
-
pH 7.4, 25°C
84
Sulfide
-
enzyme in nanodiscs, at pH 6.8 and 25°C
343
Sulfide
-
cosubstrates cyanide, ubiquinone-1, pH 8.5, 25°C
343
Sulfide
-
with coenzyme Q and cyanide as cosubstrates, at pH 8.0 and 25°C
379
Sulfide
-
cosubstrates sulfite, ubiquinone-1, pH 7.5, 25°C
379
Sulfide
-
with coenzyme Q and sulfite as cosubstrates, at pH 8.0 and 25°C
368
sulfite

-
cosubstrates sulfide, ubiquinone-1, pH 7.5, 25°C
368
sulfite
-
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
360
ubiquinone-1

-
cosubstrates cyanide, sulfide, pH 8.5, 25°C
364
ubiquinone-1
-
cosubstrates sulfite, sulfide, pH 7.5, 25°C
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0.0005 - 0.012
2-heptylquinolin-4-ol 1-oxide
0.05
2-n-heptyl-4-hydroxy-quinone-N-oxide
Acidithiobacillus ferrooxidans
-
at pH 7.0, temperature not specified in the publication
0.00076 - 0.006
2-n-nonyl-4-hydroxyquinoline-N-oxide
0.015
Antimycin
Aquifex aeolicus
-
in 50 mM Tris-HCl, pH 7.4, 40°C
0.00096 - 0.22
antimycin A
0.000012 - 0.028
aurachin C
0.000038
aurachin D
Chlorobaculum thiosulfatiphilum
-
in 20 mM Tris-HCl, pH 7.8, at 24°C
0.004 - 0.039
Myxothiazol
0.043
myxothiazole
Aquifex aeolicus
-
in 50 mM Bis-Tris (pH 7.0), at 20°C
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
0.000005 - 0.02
Stigmatellin
0.0005
2-heptylquinolin-4-ol 1-oxide

Allochromatium vinosum
-
in 50 mM Tris-HCl (pH 7.5), temperature not specified in the publication
0.012
2-heptylquinolin-4-ol 1-oxide
Aquifex aeolicus
-
in 50 mM Bis-Tris (pH 7.0), at 20°C
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
0.00096
antimycin A

Chlorobaculum thiosulfatiphilum
-
in 20 mM Tris-HCl, pH 7.8, at 24°C
0.01
antimycin A
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
0.000012
aurachin C

Chlorobaculum thiosulfatiphilum
-
in 20 mM Tris-HCl, pH 7.8, at 24°C
0.000014
aurachin C
Aquifex aeolicus
-
in 50 mM Bis-Tris (pH 7.0), at 20°C
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
0.01
cyanide

Chlorobaculum thiosulfatiphilum
-
in 20 mM Tris-HCl, pH 7.8, at 24°C
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
0.006
Myxothiazol
Chlorobaculum thiosulfatiphilum
-
in 20 mM Tris-HCl, pH 7.8, at 24°C
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
0.000005
Stigmatellin

Chlorobaculum thiosulfatiphilum
-
in 20 mM Tris-HCl, pH 7.8, at 24°C
0.02
Stigmatellin
Paracoccus denitrificans
-
in 50 mM Bis-Tris (pH 6.5), temperature not specified in the publication
0.02
Stigmatellin
Aquifex aeolicus
-
in 50 mM Bis-Tris (pH 7.0), at 20°C
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C160S
-
the mutant shows strongly reduced activity compared to the wild type enzyme
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
-
all of the expressed protein is membrane-bound, the mutant enzyme is inactive; 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; 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; 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; 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; 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/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
-
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; 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/L379D/M380N
-
the mutant protein is found entirely in the cytoplasmic fraction but there is no catalytic activity
-
C127S
-
1.3% activity compared to the wild type enzyme
C159S
-
0.5% activity compared to the wild type enzyme
C353S
-
0.4% activity compared to the wild type enzyme
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
V300D
-
11% 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
C128A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
C128S

-
loss of activity in assay with decylubiquinone
C128S
-
the mutant shows strongly reduced activity compared to the wild type enzyme
C160A

-
inactive
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

-
about 40% of wild-type activity in assay with decylubiquinone
H132A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
H198A

-
about 60% of wild-type activity in assay with decylubiquinone
H198A
-
the mutant shows severely reduced activity compared to the wild type enzyme
C94S

-
active site mutant of the rhodanese domain
C94S
-
active site mutant of the rhodanese domain
-
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
-
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
-
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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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
Aphanothece halophytica, Aphanothece halophytica (Q9KI50), Pseudanabaena limnetica
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, Acidithiobacillus ferrooxidans (B7JBP8)
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, Schizosaccharomyces pombe (O94284), Solemya reidi
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, Aquifex aeolicus (O67931)
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, Homo sapiens (Q9Y6N5)
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, Acidithiobacillus ferrooxidans (B7JBP8), 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 sulfidequinone 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 sulfidequinone 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 sulfidequinone oxidoreductase and persulfide dioxygenase rapidly oxidises sulfide to sulfite and thiosulfate via a new pathway
Environ. Microbiol.
18
5123-5136
2016
Cupriavidus pinatubonensis, Cupriavidus pinatubonensis JMP134
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 sulfidequinone oxidoreductase from Chlorobaculum tepidum displays unusual kinetic properties
FEMS Microbiol. Lett.
363
1-8
2016
Chlorobaculum tepidum, Chlorobaculum tepidum (Q8KDG3)
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, Homo sapiens (Q9Y6N5)
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, Homo sapiens (Q9Y6N5)
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, Homo sapiens (Q9Y6N5)
brenda