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2 sulfide + ubiquinone-1
hydrogen disulfide + ubiquinol-1
-
-
-
?
HS- + quinone
polysulfide + quinol
-
-
-
-
?
n H2S + n quinone
polysulfide + n quinol
n H2S + n ubiquinone
polysulfide + n ubiquinol
-
-
-
?
n Na2S + n decylubiquinone
polysulfide + n decylubiquinol + 2 Na+
-
-
-
-
?
n Na2S + n ubiquinone
polysulfide + n ubiquinol
-
-
-
?
n S2- + n decylubiquinone
polysulfide + n decylubiquinol
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 + 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
?
-
n H2S + n quinone
polysulfide + n quinol
-
-
-
-
?
n H2S + n quinone
polysulfide + n quinol
-
-
-
-
?
n H2S + n quinone
polysulfide + n quinol
-
-
-
-
?
n H2S + n quinone
polysulfide + n quinol
-
-
-
-
?
n H2S + n quinone
polysulfide + n quinol
-
-
-
?
n H2S + n quinone
polysulfide + n quinol
-
-
-
?
n H2S + n quinone
polysulfide + n quinol
-
-
-
?
n H2S + n quinone
polysulfide + n quinol
-
-
-
?
n H2S + n quinone
polysulfide + n quinol
-
-
-
?
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
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
?
-
-
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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2 - 3
cysteine
-
pH 7.4, 25°C
0.002 - 0.036
decylubiquinone
0.0274 - 0.0419
duroquinone
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
additional information
additional information
-
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
pH 7.4, temperature not specified in the publication
0.00216
decylubiquinone
in 50 mM Tris-HCl, pH 7.4, 40°C
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
0.005
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, wild-type enzyme
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
0.0275
duroquinone
recombinant mutant C49A, 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
0.155
Na2S
recombinant mutant C332A, pH 8.0, 25°C
0.183
Na2S
recombinant mutant C272A, pH 8.0, 25°C
0.209
Na2S
recombinant wild-type enzyme, pH 8.0, 25°C
0.34
Na2S
recombinant mutant C49A, 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
0.00297
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
pH 7.4, temperature not specified in the publication
0.00594
Sulfide
in 50 mM Tris-HCl, pH 7.4, 40°C
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, wild-type enzyme
0.077
Sulfide
-
pH 7.5, 60°C, cytoplasmic mutant enzyme Y383Q/F384K
0.077
Sulfide
-
pH 7.5, 60°C, membrane-bound 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
pH 7.4, temperature not specified in the publication
0.0054
ubiquinone-1
in 50 mM Tris-HCl, pH 7.4, 40°C
0.014
ubiquinone-1
cosubstrates cyanide, sulfide, pH 8.5, 25°C
0.0199
ubiquinone-1
cosubstrates sulfite, sulfide, pH 7.5, 25°C
0.0016
ubiquinone-4
pH 7.4, temperature not specified in the publication
0.0016
ubiquinone-4
in 50 mM Tris-HCl, pH 7.4, 40°C
0.00643
ubiquinone-9
pH 7.4, temperature not specified in the publication
0.00643
ubiquinone-9
in 50 mM Tris-HCl, pH 7.4, 40°C
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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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
0.19
duroquinone
recombinant mutant C332A, pH 8.0, 25°C
1.01
duroquinone
recombinant mutant C272A, pH 8.0, 25°C
1.64
duroquinone
recombinant wild-type enzyme, pH 8.0, 25°C
2.46
duroquinone
recombinant mutant C49A, pH 8.0, 25°C
0.19
Na2S
recombinant mutant C332A, pH 8.0, 25°C
1.01
Na2S
recombinant mutant C272A, pH 8.0, 25°C
1.64
Na2S
recombinant wild-type enzyme, pH 8.0, 25°C
2.46
Na2S
recombinant mutant C49A, pH 8.0, 25°C
0.1
Sulfide
mutant enzyme C160A, at pH 7.0 and 23°C
0.1
Sulfide
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
0.015 - 0.134
iodoacetamide
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
0.015
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
0.006
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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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)
-
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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
-
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/L379D/M380N
-
the mutant protein is found entirely in the cytoplasmic fraction but there is no catalytic activity
-
C94S
-
active site mutant of the rhodanese domain
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
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
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
C128S
loss of activity in assay with decylubiquinone
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
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
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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
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in the truncation mutant SQRT1 a stop codon is introduced to eliminate the last 21 amino acids from the C-terminus, removing one putative amphiphilic helix. In construct SQRT2, the last 45 amino acids are removed, thus eliminating both of the amphiphilic helices. Both SQRT1 and SQRT2 when expressed in Escherichia coli result in water-soluble proteins. In each case the yield of protein is nearly 5-fold higher than the wild type construct, in which the recombinant protein is bound to the membrane. The FAD content of each of the truncated proteins, as well as the characteristics of the absorption spectra, is identical to those of the detergent-solubilized, wild type enzyme. No sulfide:decylubiquinone oxidoreductase activity is observed in either case
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additional information
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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
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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
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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
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no SQR activity is found in membranes from mutants F14 and 22/11. Membranes of strain F14sn show 6-7times the activity of the membranes from the wild type strain
additional information
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no SQR activity is found in membranes from mutants F14 and 22/11. Membranes of strain F14sn show 6-7times the activity of the membranes from the wild type strain
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additional information
construction and analysis of an enzyme knockout strain DELTAsqr, phenotypes, overview
additional information
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construction and analysis of an enzyme knockout strain DELTAsqr, phenotypes, overview
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additional information
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construction and analysis of an enzyme knockout strain DELTAsqr, phenotypes, overview
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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
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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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