Information on EC 1.8.99.3 - hydrogensulfite reductase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
1.8.99.3
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RECOMMENDED NAME
GeneOntology No.
hydrogensulfite reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S(SO3-)2 + acceptor + 2 H2O + OH- = 3 HSO3- + reduced acceptor
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Microbial metabolism in diverse environments
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Nitrotoluene degradation
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non-pathway related
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sulfate reduction V (dissimilatory)
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Sulfur metabolism
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SYSTEMATIC NAME
IUBMB Comments
trithionate:acceptor oxidoreductase
Methylviologen can act as acceptor. A group of sirohemoproteins containing iron-sulfur centres (P-582).
CAS REGISTRY NUMBER
COMMENTARY hide
42612-25-9
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85876-01-3
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9045-15-2
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9059-42-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
sulfite reductase, no desulfoviridin
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain 5ac10
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Manually annotated by BRENDA team
strain 5ac10
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Manually annotated by BRENDA team
desulforibidin
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Manually annotated by BRENDA team
Benghazi, NCIB 8401
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Manually annotated by BRENDA team
strain Essex
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Manually annotated by BRENDA team
Norway strain
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Manually annotated by BRENDA team
strain ThAc01, desulfoviridin
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Manually annotated by BRENDA team
strain ThAc01, desulfoviridin
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Manually annotated by BRENDA team
Desulfovibrio vulgaris Hildenborough
strain Hildenborough
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Manually annotated by BRENDA team
strain Miyazaki
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Manually annotated by BRENDA team
Desulfovibrio vulgaris Miyazaki F
Miyazaki F
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Manually annotated by BRENDA team
subunit alpha and subunit beta
Q69I16 and Q69I15
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
bisulfite + electron donor
? + oxidized electron donor
show the reaction diagram
bisulfite + reduced acceptor
trithionate + acceptor + H2O + OH-
show the reaction diagram
hydroxylamine + electron donor
NH3 + H2O + oxidized electron donor
show the reaction diagram
nitrite + electron donor
NH3 + H2O + oxidized electron donor
show the reaction diagram
sulfide + electron acceptor
?
show the reaction diagram
sulfide + electron acceptor
? + oxidized electron donor
show the reaction diagram
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
sulfite + methyl viologen
trithionate + thiosulfate + sulfide + oxidized methyl viologen
show the reaction diagram
sulfite + reduced ferredoxin-I
trithionate + ferredoxin-I + H2O + OH-
show the reaction diagram
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-
-
?
sulfite + reduced pyruvate-ferredoxin oxidoreductase
trithionate + pyruvate-ferredoxin oxidoreductase + H2O + OH-
show the reaction diagram
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-
-
?
thiosulfate + electron donor
sulfate + sulfur + oxidized electron donor
show the reaction diagram
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-
-
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?
trimethylamine N-oxide + electron donor
? + oxidized electron donor
show the reaction diagram
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-
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?
additional information
?
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catalyzes the formation of sulfide from sulfite
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
bisulfite + reduced acceptor
trithionate + acceptor + H2O + OH-
show the reaction diagram
sulfide + electron acceptor
? + oxidized electron donor
show the reaction diagram
sulfite + electron donor
? + oxidized electron donor
show the reaction diagram
sulfite + electron donor
trithionate + thiosulfate + sulfide + polythionate + oxidized electron donor
show the reaction diagram
Q93UT1
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additional information
?
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catalyzes the formation of sulfide from sulfite
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(7S,8S,12S,13S)-3,8,13,17-tetrakis(carboxymethyl)-8,13-dimethyl-7,8,12,13-tetrahydroporphyrin-2,7,12,18-tetrapropionic acid
isoforms Dsr-I and DsrII contain two flat sirohydrochlorins; isoforms Dsr-I and DsrII contain two flat sirohydrochlorins
Ferredoxin
heme
Q59110 and Q59109
only the alpha subunit binds a siroheme-[4Fe-4S] complex. Chemical analyses shows the presence of only two sirohemes per alpha2beta2 enzyme molecule
siroheme
[3Fe-4S]-center
isoform Dsr-II contains a [3Fe-4S] cluster in addition to the [4Fe-4S] cluster; isoform Dsr-II contains a [3Fe-4S] cluster in addition to the [4Fe-4S] cluster
[4Fe-4S]-center
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
[4Fe-4S]-center
Q59110 and Q59109
only the alpha subunit binds a sirohaem-[4Fe-4S] complex. Chemical analyses shows the presence of only two sirohemes per alpha2beta2 enzyme molecule and the presence of six [4Fe-4S] clusters per alpha2beta2 enzyme molecule, two of which would be expected to be associated with siroheme while the other four could bind to the ferredoxin-like sites
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
arsenite
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10 mM, 68% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cyanide
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1 mM, slight activation
additional information
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active form of enzyme binds and catalyzes substrate reduction, inactive enzyme form exists in resting cells
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
48
hydroxylamine
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0.028
nitrite
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0.06 - 3.6
sulfite
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.041
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soluble enzyme
0.128
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membranous enzyme
240
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mutant DELTAdsrJ
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 6.5
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pH 5.0: about 70% of maximal activity, pH 6.5: about 60% of maximal activity, reduction of sulfite
6 - 8
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pH 6.0: about 50% of maximal activity, pH 8.0: about 90% of maximal activity, reduction of hydroxylamine
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85
Q59110 and Q59109
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 70
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35C: very low activity below 35C, 65-70C: maximal activity at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.2
Q59110 and Q59109
analytical isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Desulfomicrobium norvegicum (strain DSM 1741 / NCIMB 8310)
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26650
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gel filtration
160000
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gel filtration
167000
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equilibrium sedimentation
178200
Q59110 and Q59109
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180000
190000
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equilibrium sedimentation
200000
215100
gel filtration
280000
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gel filtration
285000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 13327, gel filtration
heterodimer
heterohexamer
x-ray crystallography
hexamer
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alpha2beta2gamma2, 2 * 50000 + 2 * 42500 + 2 * 12000, SDS-PAGE
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method
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bound to two DsrC proteins, hanging drop vapor diffusion method, using 20% (w/v) PEG 3350, 0.1 M Bis-Tris propane pH 7.5, and 0.2 M K/Na tartrate
hanging drop vapor diffusion method, using PEG6000 (23% (w/v) for isoform Dsr-I and 25% (w/v) for isoform Dsr-II) and sodium chloride (200 mM) in MES buffer (100 mM) at pH 5.5; hanging drop vapor diffusion method, using PEG6000 (23% (w/v) for isoform Dsr-I and 25% (w/v) for isoform Dsr-II) and sodium chloride (200 mM) in MES buffer (100 mM) at pH 5.5
crystal structure determined at 1.2 by the single isomorphous replacement method
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large crystals, obtained by the sitting-drop vapour-diffussion method followed by macroseeding, are used for a neutron diffraction experiment
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
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stable to, rapidly denatured above
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 1 month, no loss of activity
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-20C, 6 months, stable
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4C, 1 month, 60% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DE52 ion exchange column chromatography, Mono Q column chromatography, and Superdex-200 gel filtration; DE52 ion exchange column chromatography, Mono Q column chromatography, and Superdex-200 gel filtration
DEAE-Sepharose column chromatography, Q-Sepharose column chromatography, Mono Q column chromatography, and Sephacryl S-200 gel filtration
MonoQ HR 5/5 column chromatography
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Q-Sepharose Hi-Load column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
Q59110 and Q59109
expressed in Escherichia coli
into the pCR2.1-TOPO plasmid vector for transformation into Escherichia coli TOP10 cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTAdsrJ
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mutant with in frame deletion, unable to oxidize stored sulfur
DELTAdsrK
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mutant with in frame deletion, unable to oxidize stored sulfur
DELTAdsrL
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in frame deletion mutant, that is indispensable for sulfur oxidation
DELTAdsrM
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mutant with in frame deletion, unable to oxidize stored sulfur
DELTAdsrN
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in frame deletion mutants, sulfur oxidation rate is reduced to 15% of the oxidation rate of the wild type enzyme
DELTAdsrO
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mutant with in frame deletion, unable to oxidize stored sulfur
DELTAdsrP
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mutant with in frame deletion, unable to oxidize stored sulfur
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
industry
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quick detection and accurate quantification of sulfate-reducing bacteria in oil fields are crucial for the design of a process to prevent H2S from being formed and to control reservoir souring
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