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Information on EC 1.8.5.4 - bacterial sulfide:quinone reductase and Organism(s) Aquifex aeolicus and UniProt Accession O67931

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IUBMB Comments
Contains FAD. Ubiquinone, plastoquinone or menaquinone can act as acceptor in different species. In some organisms the enzyme catalyses the formation of sulfur globules. It repeats the catalytic cycle without releasing the product, producing a polysulfide of up to 10 sulfur atoms. The reaction stops when the maximum length of the polysulfide that can be accommodated in the sulfide oxidation pocket is achieved. The enzyme also plays an important role in anoxygenic bacterial photosynthesis. cf. EC 1.8.5.8, sulfide quinone oxidoreductase.
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Aquifex aeolicus
UNIPROT: O67931
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The taxonomic range for the selected organisms is: Aquifex aeolicus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
hide
n
HS-
+
n
quinone
=
polysulfide
+
n
quinol
n
+
n
=
polysulfide
+
n
Synonyms
sulfide:quinone oxidoreductase, sulfide quinone oxidoreductase, sqrdl, sulfide quinone reductase, sulfide-quinone reductase, sulfide-quinone oxidoreductase, ct1087, trsqrf, iii sqr, cpsqr, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sulfide:quinone oxidoreductase
-
sulfide quinone oxidoreductase
-
-
sulfide quinone reductase
-
-
sulfide:quinone oxidoreductase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
SYSTEMATIC NAME
IUBMB Comments
sulfide:quinone oxidoreductase
Contains FAD. Ubiquinone, plastoquinone or menaquinone can act as acceptor in different species. In some organisms the enzyme catalyses the formation of sulfur globules. It repeats the catalytic cycle without releasing the product, producing a polysulfide of up to 10 sulfur atoms. The reaction stops when the maximum length of the polysulfide that can be accommodated in the sulfide oxidation pocket is achieved. The enzyme also plays an important role in anoxygenic bacterial photosynthesis. cf. EC 1.8.5.8, sulfide quinone oxidoreductase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
sulfide + decylubiquinone
sulfur + decylubiquinol
show the reaction diagram
sulfide + quinone
sulfur + quinol
show the reaction diagram
-
-
-
?
sulfide + ubiquinone-1
sulfur + ubiquinol-1
show the reaction diagram
-
-
-
?
sulfide + ubiquinone-4
sulfur + ubiquinol-4
show the reaction diagram
-
-
-
?
sulfide + ubiquinone-9
sulfur + ubiquinol-9
show the reaction diagram
-
-
-
?
sulfide + decylubiquinone
sulfur + decylubiquinol
show the reaction diagram
sulfide + ubiquinone-1
sulfur + ubiquinol-1
show the reaction diagram
-
-
-
?
sulfide + ubiquinone-4
sulfur + ubiquinol-4
show the reaction diagram
-
-
-
?
sulfide + ubiquinone-9
sulfur + ubiquinol-9
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-heptylquinolin-4-ol 1-oxide
-
-
2-n-nonyl-4-hydroxyquinoline-N-oxide
-
-
Antimycin
competitive
antimycin A
-
-
aurachin C
-
-
myxothiazole
-
-
Stigmatellin
-
-
additional information
-
insensitive towards cyanide
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00216
decylubiquinone
in 50 mM Tris-HCl, pH 7.4, 40°C
0.00594
Sulfide
in 50 mM Tris-HCl, pH 7.4, 40°C
0.0054
ubiquinone-1
in 50 mM Tris-HCl, pH 7.4, 40°C
0.0016
ubiquinone-4
in 50 mM Tris-HCl, pH 7.4, 40°C
0.00643
ubiquinone-9
in 50 mM Tris-HCl, pH 7.4, 40°C
0.00216 - 0.005
decylubiquinone
0.00594 - 0.011
Sulfide
0.0054
ubiquinone-1
pH 7.4, temperature not specified in the publication
0.0016
ubiquinone-4
pH 7.4, temperature not specified in the publication
0.00643
ubiquinone-9
pH 7.4, temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015
Antimycin
Aquifex aeolicus
in 50 mM Tris-HCl, pH 7.4, 40°C
0.012
2-heptylquinolin-4-ol 1-oxide
Aquifex aeolicus
-
in 50 mM Bis-Tris (pH 7.0), at 20°C
0.006
2-n-nonyl-4-hydroxyquinoline-N-oxide
Aquifex aeolicus
-
in 50 mM Bis-Tris (pH 7.0), at 20°C
0.01
antimycin A
Aquifex aeolicus
-
in 50 mM Bis-Tris (pH 7.0), at 20°C
0.000014
aurachin C
Aquifex aeolicus
-
in 50 mM Bis-Tris (pH 7.0), at 20°C
0.043
myxothiazole
Aquifex aeolicus
-
in 50 mM Bis-Tris (pH 7.0), at 20°C
0.02
Stigmatellin
Aquifex aeolicus
-
in 50 mM Bis-Tris (pH 7.0), at 20°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
71.4
at 40°C, pH 7.4
3.5
-
in 50 mM Bis-Tris (pH 7.0), at 20°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
the activity is highest at 80°C (the highest temperature tested)
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 70
-
with 0.015 mM decylubqiuinone reduced/mg protein/min, the activity at 70°C is 5fold higher than the activity at 20°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
160000
analytical ultracentrifugation
47000
3 * 47000, SDS-PAGE
120000
gel filtration
16000
sedimentation equilibrium centrifugation
47000
x * 47000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotrimer
homotrimer
-
-
multimer
x * 47000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 2.0 M ammonium sulfate and 4% (v/v) PEG 400
crystallization in two crystal forms of hexagonal, prism shape and thin, elongated shape
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
the half-life at 80°C is 32 h
80
50% loss of activity after one day
95
-
the reaction with membranes that have been heated for more than 2 h at 95°C is negligible
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified protein in 3% (w/v) dodecyl-beta-D-maltoside either in the absence of salt or in the presence of N 1 M NaCl, six weeks, no loss of activity
80°C, purified protein in 3% (w/v) dodecyl-beta-D-maltoside either in the absence of salt or in the presence of N 1 M NaCl, one day, 50% loss of activity
4C, protein is stable and monodisperse in 50 mM dodecyl-D-maltoside for weeks, either in the absence of salt or in the presence of N 1 M NaCl
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
MonoQ column chromatography and TSK 4000 gel filtration
MonoQ column chromatography, TSK-1 gel filtration, and TSK-2 gel filtration
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Marcia, M.; Ermler, U.; Peng, G.; Michel, H.
The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration
Proc. Natl. Acad. Sci. USA
106
9625-9630
2009
Aquifex aeolicus (O67931), Aquifex aeolicus
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team