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Information on EC 1.8.5.4 - bacterial sulfide:quinone reductase and Organism(s) Homo sapiens and UniProt Accession Q9Y6N5
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1.8.5.4 bacterial sulfide:quinone reductaseIUBMB Comments
Contains FAD. Ubiquinone, plastoquinone or menaquinone can act as acceptor in different species. In some organisms the enzyme catalyses the formation of sulfur globules. It repeats the catalytic cycle without releasing the product, producing a polysulfide of up to 10 sulfur atoms. The reaction stops when the maximum length of the polysulfide that can be accommodated in the sulfide oxidation pocket is achieved. The enzyme also plays an important role in anoxygenic bacterial photosynthesis. cf. EC 1.8.5.8, sulfide quinone oxidoreductase.
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Word Map
- 1.8.5.4
- sulfur
- h2s
- thiosulfate
- persulfide
- polysulfide
- acidithiobacillus
- sulfurtransferase
-
sulfide-oxidizing
- rhodanese
-
sulfane
- ferrooxidans
- 3-mercaptopyruvate
-
anoxygenic
-
sulfur-oxidizing
-
chemolithotrophic
-
sulfide-dependent
-
echiuran
- unicinctus
- limnetica
-
urechis
-
monotopic
- oscillatoria
- tepidum
- chlorobaculum
-
sulfide-rich
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
sulfide:quinone oxidoreductase, sulfide quinone oxidoreductase, sqrdl, sulfide quinone reductase, sulfide-quinone reductase, sulfide-quinone oxidoreductase, ct1087, trsqrf, iii sqr, cpsqr, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
sulfide + sulfide + coenzyme Q
hydrogen disulfide + reduced coenzyme Q
-
-
-
?
sulfide + cysteine + coenzyme Q1
cysteine persulfide + reduced coenzyme Q1
-
-
-
-
?
sulfide + homocysteine + coenzyme Q1
homocysteine persulfide + reduced coenzyme Q1
-
-
-
-
?
sulfide + reduced glutathione + coenzyme Q1
glutathione persulfide + reduced coenzyme Q1
-
-
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
cyanide, sulfite, or sulfide can act as the sulfane sulfur acceptor in reactions that exhibit pH optima at 8.5, 7.5, or 7.0, respectively, and produce thiocyanate, thiosulfate, or a putative sulfur analogue of hydrogen peroxide, i.e. H2S2, respectively. Sulfite is the physiological acceptor of the sulfur and the reaction is the predominant source of the thiosulfate produced during H2S oxidation by mammalian tissues
-
-
?
additional information
?
-
-
cyanide, sulfite, or sulfide can act as the sulfane sulfur acceptor in reactions that exhibit pH optima at 8.5, 7.5, or 7.0, respectively, and produce thiocyanate, thiosulfate, or a putative sulfur analogue of hydrogen peroxide, i.e. H2S2, respectively. Sulfite is the physiological acceptor of the sulfur and the reaction is the predominant source of the thiosulfate produced during H2S oxidation by mammalian tissues
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cyanide
4.5fold increase in the rate of H2S oxidation in the presence of 1 mM cyanide
sulfite
13.6fold increase in the rate of H2S oxidation in the presence of 0.6 mM sulfite
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.014
coenzyme Q
with cyanide and sulfide as cosubstrates, at pH 8.0 and 25°C
0.019
coenzyme Q
with sulfite and sulfide as cosubstrates, at pH 8.0 and 25°C
0.65
cyanide
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
0.0109
Sulfide
with coenzyme Q and cyanide as cosubstrates, at pH 8.0 and 25°C
0.013
Sulfide
with coenzyme Q and sulfite as cosubstrates, at pH 8.0 and 25°C
0.174
sulfite
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
360
coenzyme Q
with cyanide and sulfide as cosubstrates, at pH 8.0 and 25°C
364
coenzyme Q
with sulfite and sulfide as cosubstrates, at pH 8.0 and 25°C
330
cyanide
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
343
Sulfide
with coenzyme Q and cyanide as cosubstrates, at pH 8.0 and 25°C
379
Sulfide
with coenzyme Q and sulfite as cosubstrates, at pH 8.0 and 25°C
368
sulfite
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
19000
coenzyme Q
with sulfite and sulfide as cosubstrates, at pH 8.0 and 25°C
27000
coenzyme Q
with cyanide and sulfide as cosubstrates, at pH 8.0 and 25°C
510
cyanide
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
29000
Sulfide
with coenzyme Q and sulfite as cosubstrates, at pH 8.0 and 25°C
31000
Sulfide
with coenzyme Q and cyanide as cosubstrates, at pH 8.0 and 25°C
2100
sulfite
with coenzyme Q and sulfide as cosubstrates, at pH 8.0 and 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
human sulfide quinone oxidoreductase uses glutathione as an acceptor forming glutathione persulfide (GSSH), which is preferentially converted to thiosulfate by human rhodanese
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel affinity column chromatography and Superdex 200 gel filtration
nickel affinity column chromatography and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression at low temperature in Escherichia coli by using an optimized synthetic gene and cold-adapted chaperonins
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jackson, M.; Melideo, S.; Jorns, M.
Human sulfide:Quinone oxidoreductase catalyzes the first step in hydrogen sulfide metabolism and produces a sulfane sulfur metabolite
Biochemistry
51
6804-6815
2012
Homo sapiens (Q9Y6N5), Homo sapiens
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
Mishanina, T.; Yadav, P.; Ballou, D.; Banerjee, R.
Transient kinetic analysis of hydrogen sulfide oxidation catalyzed by human sulfide quinone oxidoreductase
J. Biol. Chem.
290
25072-25080
2015
Homo sapiens (Q9Y6N5), Homo sapiens
Landry, A.; Ballou, D.; Banerjee, R.
H2S oxidation by nanodisc-embedded human sulfide quinone oxidoreductase
J. Biol. Chem.
292
11641-11649
2017
Homo sapiens (Q9Y6N5), Homo sapiens
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Release 2023.1 (January 2023)
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