BRENDA - Enzyme Database
show all sequences of 1.8.5.4

Characterization of the type III sulfide:quinone oxidoreductase from Caldivirga maquilingensis and its membrane binding

Lencina, A.M.; Ding, Z.; Schurig-Briccio, L.A.; Gennis, R.B.; Biochim. Biophys. Acta 1827, 266-275 (2013)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli; expression in Escherichia coli
Caldivirga maquilingensis
Engineering
Amino acid exchange
Commentary
Organism
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
Caldivirga maquilingensis
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%)
Caldivirga maquilingensis
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
Caldivirga maquilingensis
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
Caldivirga maquilingensis
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
Caldivirga maquilingensis
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
Caldivirga maquilingensis
Y383Q/F384K/L379D/M380N
the mutant protein is found entirely in the cytoplasmic fraction but there is no catalytic activity
Caldivirga maquilingensis
Inhibitors
Inhibitors
Commentary
Organism
Structure
aurachin C
250 nM, complete inhibition
Caldivirga maquilingensis
iodoacetamide
0.3 mM, complete inhibition
Caldivirga maquilingensis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.03
-
decylubiquinone
pH 7.5, 60°C, membrane-bound wild-type enzyme; pH 7.5, 60°C, wild-type enzyme
Caldivirga maquilingensis
0.032
-
decylubiquinone
pH 7.5, 60°C, membrane-bound mutant enzyme M380N
Caldivirga maquilingensis
0.033
-
decylubiquinone
pH 7.5, 60°C, membrane-bound mutant enzyme Y383Q/F384K
Caldivirga maquilingensis
0.036
-
decylubiquinone
pH 7.5, 60°C, cytoplasmic mutant enzyme Y383Q/F384K
Caldivirga maquilingensis
0.046
-
Sulfide
pH 7.5, 60°C, membrane-bound mutant enzyme Y383Q/F384K
Caldivirga maquilingensis
0.073
-
Sulfide
pH 7.5, 60°C, membrane-bound mutant enzyme M380N
Caldivirga maquilingensis
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
Caldivirga maquilingensis
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
the C-terminal amphiphilic helix is important for membrane binding
Caldivirga maquilingensis
16020
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
45000
-
x * 45000, SDS-PAGE
Caldivirga maquilingensis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Caldivirga maquilingensis
-
-
-
Caldivirga maquilingensis IC-167
-
-
-
Purification (Commentary)
Commentary
Organism
-
Caldivirga maquilingensis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
sulfide + decylubiquinone
-
727080
Caldivirga maquilingensis
polysulfide + decylubiquinol
-
-
-
?
sulfide + decylubiquinone
-
727080
Caldivirga maquilingensis IC-167
polysulfide + decylubiquinol
-
-
-
?
sulfide + decylubiquinone
-
727080
Caldivirga maquilingensis
sulfur + decylubiquinol
-
-
-
?
sulfide + decylubiquinone
-
727080
Caldivirga maquilingensis IC-167
sulfur + decylubiquinol
-
-
-
?
sulfide + duroquinone
23% compared to the activity with decylubiquinone
727080
Caldivirga maquilingensis
sulfur + duroquinol
-
-
-
?
sulfide + duroquinone
23% compared to the activity with decylubiquinone
727080
Caldivirga maquilingensis IC-167
sulfur + duroquinol
-
-
-
?
sulfide + duroquinone 23
% compared to the activity with decylubiquinone
727080
Caldivirga maquilingensis
sulfur + duroquinol 23
-
-
-
?
sulfide + menadione
25% compared to the activity with decylubiquinone
727080
Caldivirga maquilingensis
sulfur + menadiol
-
-
-
?
sulfide + menadione
25% compared to the activity with decylubiquinone
727080
Caldivirga maquilingensis IC-167
sulfur + menadiol
-
-
-
?
sulfide + menadione
25% compared to the activity with decylubiquinone
727080
Caldivirga maquilingensis
polysulfide + menadiol
-
-
-
?
sulfide + ubiquinone-1
15% compared to the activity with decylubiquinone
727080
Caldivirga maquilingensis
sulfur + ubiquinol-1
-
-
-
?
sulfide + ubiquinone-1
15% compared to the activity with decylubiquinone
727080
Caldivirga maquilingensis IC-167
sulfur + ubiquinol-1
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 45000, SDS-PAGE
Caldivirga maquilingensis
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
60
-
assay at
Caldivirga maquilingensis
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.6
-
decylubiquinone
pH 7.5, 60°C, membrane-bound wild-type enzyme
Caldivirga maquilingensis
0.6
-
Sulfide
pH 7.5, 60°C, membrane-bound wild-type enzyme
Caldivirga maquilingensis
0.62
-
decylubiquinone
pH 7.5, 60°C, membrane-bound mutant enzyme M380N
Caldivirga maquilingensis
0.62
-
Sulfide
pH 7.5, 60°C, membrane-bound mutant enzyme M380N
Caldivirga maquilingensis
0.82
-
decylubiquinone
pH 7.5, 60°C, membrane-bound mutant enzyme Y383Q/F384K
Caldivirga maquilingensis
0.82
-
Sulfide
pH 7.5, 60°C, membrane-bound mutant enzyme Y383Q/F384K
Caldivirga maquilingensis
1.2
-
decylubiquinone
pH 7.5, 60°C, cytoplasmic mutant enzyme Y383Q/F384K
Caldivirga maquilingensis
1.2
-
Sulfide
pH 7.5, 60°C, cytoplasmic mutant enzyme Y383Q/F384K
Caldivirga maquilingensis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Caldivirga maquilingensis
Cofactor
Cofactor
Commentary
Organism
Structure
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; is not covalently bound to the protein, the cofactor is in an apolar environment, one equivalent of FAD per sulfide:quinone xidoreductase polypeptide
Caldivirga maquilingensis
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli; expression in Escherichia coli
Caldivirga maquilingensis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
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; is not covalently bound to the protein, the cofactor is in an apolar environment, one equivalent of FAD per sulfide:quinone xidoreductase polypeptide
Caldivirga maquilingensis
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
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
Caldivirga maquilingensis
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%)
Caldivirga maquilingensis
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
Caldivirga maquilingensis
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
Caldivirga maquilingensis
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
Caldivirga maquilingensis
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
Caldivirga maquilingensis
Y383Q/F384K/L379D/M380N
the mutant protein is found entirely in the cytoplasmic fraction but there is no catalytic activity
Caldivirga maquilingensis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
aurachin C
250 nM, complete inhibition
Caldivirga maquilingensis
iodoacetamide
0.3 mM, complete inhibition
Caldivirga maquilingensis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.03
-
decylubiquinone
pH 7.5, 60°C, membrane-bound wild-type enzyme; pH 7.5, 60°C, wild-type enzyme
Caldivirga maquilingensis
0.032
-
decylubiquinone
pH 7.5, 60°C, membrane-bound mutant enzyme M380N
Caldivirga maquilingensis
0.033
-
decylubiquinone
pH 7.5, 60°C, membrane-bound mutant enzyme Y383Q/F384K
Caldivirga maquilingensis
0.036
-
decylubiquinone
pH 7.5, 60°C, cytoplasmic mutant enzyme Y383Q/F384K
Caldivirga maquilingensis
0.046
-
Sulfide
pH 7.5, 60°C, membrane-bound mutant enzyme Y383Q/F384K
Caldivirga maquilingensis
0.073
-
Sulfide
pH 7.5, 60°C, membrane-bound mutant enzyme M380N
Caldivirga maquilingensis
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
Caldivirga maquilingensis
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
the C-terminal amphiphilic helix is important for membrane binding
Caldivirga maquilingensis
16020
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
45000
-
x * 45000, SDS-PAGE
Caldivirga maquilingensis
Purification (Commentary) (protein specific)
Commentary
Organism
-
Caldivirga maquilingensis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
sulfide + decylubiquinone
-
727080
Caldivirga maquilingensis
polysulfide + decylubiquinol
-
-
-
?
sulfide + decylubiquinone
-
727080
Caldivirga maquilingensis IC-167
polysulfide + decylubiquinol
-
-
-
?
sulfide + decylubiquinone
-
727080
Caldivirga maquilingensis
sulfur + decylubiquinol
-
-
-
?
sulfide + decylubiquinone
-
727080
Caldivirga maquilingensis IC-167
sulfur + decylubiquinol
-
-
-
?
sulfide + duroquinone
23% compared to the activity with decylubiquinone
727080
Caldivirga maquilingensis
sulfur + duroquinol
-
-
-
?
sulfide + duroquinone
23% compared to the activity with decylubiquinone
727080
Caldivirga maquilingensis IC-167
sulfur + duroquinol
-
-
-
?
sulfide + duroquinone 23
% compared to the activity with decylubiquinone
727080
Caldivirga maquilingensis
sulfur + duroquinol 23
-
-
-
?
sulfide + menadione
25% compared to the activity with decylubiquinone
727080
Caldivirga maquilingensis
sulfur + menadiol
-
-
-
?
sulfide + menadione
25% compared to the activity with decylubiquinone
727080
Caldivirga maquilingensis IC-167
sulfur + menadiol
-
-
-
?
sulfide + menadione
25% compared to the activity with decylubiquinone
727080
Caldivirga maquilingensis
polysulfide + menadiol
-
-
-
?
sulfide + ubiquinone-1
15% compared to the activity with decylubiquinone
727080
Caldivirga maquilingensis
sulfur + ubiquinol-1
-
-
-
?
sulfide + ubiquinone-1
15% compared to the activity with decylubiquinone
727080
Caldivirga maquilingensis IC-167
sulfur + ubiquinol-1
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 45000, SDS-PAGE
Caldivirga maquilingensis
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
60
-
assay at
Caldivirga maquilingensis
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.6
-
decylubiquinone
pH 7.5, 60°C, membrane-bound wild-type enzyme
Caldivirga maquilingensis
0.6
-
Sulfide
pH 7.5, 60°C, membrane-bound wild-type enzyme
Caldivirga maquilingensis
0.62
-
decylubiquinone
pH 7.5, 60°C, membrane-bound mutant enzyme M380N
Caldivirga maquilingensis
0.62
-
Sulfide
pH 7.5, 60°C, membrane-bound mutant enzyme M380N
Caldivirga maquilingensis
0.82
-
decylubiquinone
pH 7.5, 60°C, membrane-bound mutant enzyme Y383Q/F384K
Caldivirga maquilingensis
0.82
-
Sulfide
pH 7.5, 60°C, membrane-bound mutant enzyme Y383Q/F384K
Caldivirga maquilingensis
1.2
-
decylubiquinone
pH 7.5, 60°C, cytoplasmic mutant enzyme Y383Q/F384K
Caldivirga maquilingensis
1.2
-
Sulfide
pH 7.5, 60°C, cytoplasmic mutant enzyme Y383Q/F384K
Caldivirga maquilingensis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Caldivirga maquilingensis
General Information
General Information
Commentary
Organism
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
Caldivirga maquilingensis
General Information (protein specific)
General Information
Commentary
Organism
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
Caldivirga maquilingensis
Other publictions for EC 1.8.5.4
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
742905
Landry
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Homo sapiens
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292
11641-11649
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3
1
-
-
-
2
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
2
-
-
-
1
-
-
-
1
-
-
-
-
3
1
-
-
-
2
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-
-
-
-
-
2
2
742387
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1
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1
-
-
-
-
-
-
-
-
4
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
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-
1
1
-
1
-
-
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-
-
-
-
-
1
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-
-
1
-
-
-
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-
-
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742540
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A sulfidequinone oxidoreducta ...
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363
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1
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3
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1
-
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1
-
1
1
-
-
-
1
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
1
-
-
1
-
-
-
-
1
-
-
1
-
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
742790
Han
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Sulfurimonas denitrificans, Sulfurimonas denitrificans DSM-1251
J. Bacteriol.
198
1260-1267
2016
-
-
1
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
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-
-
-
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-
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-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
742453
Harb
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Aquifex aeolicus
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38
110
2015
-
-
-
-
-
-
-
-
1
-
-
-
-
4
-
-
1
-
-
-
-
-
1
1
-
-
-
-
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-
-
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1
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Mechanism of sulfide-quinone r ...
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Cyanobacterial sulfide-quinone ...
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Sulfide-quinone reductase from ...
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1
-
-
7
-
-
-
1
-
-
-
7
8
-
-
1
-
-
-
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-