Information on EC 1.8.2.1 - sulfite dehydrogenase

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

EC NUMBER
COMMENTARY hide
1.8.2.1
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RECOMMENDED NAME
GeneOntology No.
sulfite dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
sulfite + 2 ferricytochrome c + H2O = sulfate + 2 ferrocytochrome c + 2 H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
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redox reaction
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-
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
sulfite oxidation I (sulfite oxidoreductase)
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sulfate reduction
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Sulfur metabolism
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
sulfite:ferricytochrome-c oxidoreductase
Associated with cytochrome c-551.
CAS REGISTRY NUMBER
COMMENTARY hide
37256-47-6
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
enzyme enhances the thiosulfate oxidation activity of the core thiosulfate oxidizing multi-enzyme system TOMES with various cytochromes as electron acceptors, enzyme mediates electron transfer between the components of core TOMES and externally added cytochromes
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
SO32- + H2O + 2 oxidized cytochrome c
SO42- + 2 reduced cytochrome c + 2 H+
show the reaction diagram
-
-
-
-
?
sulfite + 2 ferricytochrome c + H2O
sulfate + 2 ferrocytochrome c + 2 H+
show the reaction diagram
in the absence of the core thiosulfate oxidizing multi-enzyme system, enzyme catalyzes sulfide-dependent reduction of Chlorobaculum tepidum cytochrome c-554
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
show the reaction diagram
sulfite + ferricyanide + H2O
sulfate + ferrocyanide + H+
show the reaction diagram
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c
show the reaction diagram
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
show the reaction diagram
sulfite + ferricytochrome c550 + H2O
sulfate + ferrocytochrome c
show the reaction diagram
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-
-
-
?
sulfite + H2O + acceptor
sulfate + reduced acceptor + 2 H+
show the reaction diagram
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-
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?
additional information
?
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present in taurine-grown cells and effectively absent in acetate grown cells, can be anticipated in both sulfite-generating pathways
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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
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c
show the reaction diagram
-
-
-
-
?
sulfite + ferricytochrome c + H2O
sulfate + ferrocytochrome c + H+
show the reaction diagram
sulfite + ferricytochrome c550 + H2O
sulfate + ferrocytochrome c
show the reaction diagram
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-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome c
cytochrome c-551
-
cytochrome c550
FAD
enzyme covalently binds one FAD
molybdenum cofactor
(molybdopterin-S,S)-oxo-molybdenum
molybdopterin
additional information
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independent of cytochrome c, assayed with ferricyanide as an electron acceptor
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
1 mM, 150% increase in activity
Mn2+
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1 mM, 127% increase in activity
Molybdenum
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
2,2'-bipyridyl
arsenite
HgCl2
HPO42-
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18% electrochemical activity at 100 mM inhibitor concentration, at 20 mM 50% inhibition
KCN
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2 mM, complete inhibition after 10 min
monoiodoacetate
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1 mM, 19% inhibition
NaAsO2
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31% inhibition
NaF
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0.01 mM, 17.5% inhibition
Ni2+
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1 mM, 32% inhibition
NO3-
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37% electrochemical activity at 100 mM inhibitor concentration, at 3 mM 50% inhibition
p-hydroxymercuribenzoate
phosphate
SO42-
Sodium deoxycholate
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1.0%, 80% inhibition
Triton X-100
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1.0%, 15% inhibition
Zn2+
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1 mM, 27% inhibition
additional information
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CaCl2, MgSO4, ZnSO4, CuSO4, FeCl3, NiCl2 and Na2MoO4 inhibits the reaction by 70% at 0.267 mM, this effect is apparently due to the non-enzymatic oxidation of sulfite with air
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosphate
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maximal actiovity at final substrate concentrations of 0.02-0.05 M at pH 7.8
Triton X-100
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increases activity
additional information
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SDH emerges at saturating substrate conditions and occurs at a potential of ca. +320 mV vs normal hydrogen electrode
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0023 - 0.019
cytochrome c
0.0025
cytochrome c550
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-
0.02 - 0.58
ferricyanide
0.0018 - 2.1
ferricytochrome c
0.000004 - 41.4
sulfite
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10880
cytochrome c
Starkeya novella
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recombinant enzyme
0.4 - 10880
sulfite
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.84 - 106000
sulfite
92
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.5
NaCl
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12 - 45
phosphate
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
139.5
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reaction with ferricyanide
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
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reaction with native cytochrome c
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9.4
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wild type enzyme
6 - 10
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7.2 - 8.64
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mutant enzyme Y236F
7.3 - 9.5
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90% of maximal activity at pH 7.3 and 9.5
8 - 10
less than 50% of maximal activity above and below
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39800
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sequence analysis
40700
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sequence analysis
41500
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nondenaturing PAGE
43000
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mutant enzyme Y236F, analytical ultracentrifugation
46000
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gel filtration
48000
gel filtration
54000
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sucrose density gradient method
67000
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gel filtration, SorA
101000
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wild type enzyme, sedimentation equilibrium analysis
190000
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native gradient PAGE
400000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
homodimer
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2 * 40000, SDS-PAGE
monomer
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the C185S variant is crystallized by the hanging drop vapor diffusion method using 15% (v/v) 2-methyl-2,4-pentanediol, 2% PEG 4000 (w/v), and 100 mM sodium acetate (pH 5.0) and in the presence of sulfite using 2% PEG 4000 (w/v), 10% MPD (v/v), 100 mM sodium acetate (pH 5.0) and 0.5 mM sodium sulfite. The C185A variant is crystallized by the sitting drop vapor diffusion method, using 15% (w/v) PEG 4000, 150 mM (NH4)2SO4, and 100 mM MES (pH 6.0)
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crystal structure
vapour diffusion method. Crystals belong to the space group P2(1)2(1)2, with unit-cell parameters a = 97.5, b = 92.5, c = 55.9
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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20C, 1 h, stable
394088
9
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20C, 1 h, about 20% loss of activity
394088
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
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1 week, about 35% loss of activity
30
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1 h, stable below
40
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1 h, about 20% loss of activity
50
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1 h, complete loss of activity
58
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rapid inactivation of oxidized enzyme, substrate-reduced enzyme remains active for more than 1 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
catalytic asctivity is retained upon immobilization of the enzyme on an edge oriented pyrolytic graphite working electrode
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proteolytic treatment with trypsin at room temperature for up to 5 h at trypsin to enzyme ratios of 1/20 and 1/1 does not affect the activity of the enzyme
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stable to repeated freezing and thawing
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thawing and refreezing has no effect
treatment with 1-2 mg trypsin per 1.5 mg of protein or 0.1-0.2 mg of pronase or 1.5 mg of protein at 25C causes decline of activity
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ethanol
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50%, significant loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, in presence of 20% glycerol stable for several days, without glycerol most of the activity is lost after 48 h
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-20C, MES, phosphate, Tris or CAPS buffer, pH 5.5-10.5, for at least 3 months
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-20C, no loss of activity after several months
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-20C, retains high activity for more than 6 months
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-20C, stable for several months
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4C, 10-20% loss of activity after 6 h at room temperature, 80% loss of activity after 5 days
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4C, 20% loss of activity after 1 month
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by anion-exchange chromatography and gel filtration, 270fold
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by anion-exchange chromatography and gel filtration, 320fold
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DEAE anion exchange column chromatography
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gel filtration
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Ni-NTA resin column chromatography
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phenyl Sepharose column chromatography and Superdex 200 gel filtration
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phenyl-Sepharose column chromatography and Superdex 200 16/60 column gel filtration
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phenyl-Sepharose column chromatography and Superdex-200 gel filtration
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protein is yellow in colour
purified from a heterologous expression system in Rhodobacter capsulatus
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain DH5alpha
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expressed in Escherichia coli strain TP1000
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expressed in Escherichia coli TP1000 cells
expressed in Rhodobacter capsulatus
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expression in Rhodobacter capsulatus
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heterologous expression in Rhodobacter capsulatus with the expression vector pDorEX, potentially useful for heterologous expression of multi-subunit proteins containing complex redox cofactors
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C185A
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the active site of the mutant is essentially catalytically inactive with ferricyctochrome c or ferricyanide as electron acceptor
C185S
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the active site of the mutant is essentially catalytically inactive with ferricyctochrome c or ferricyanide as electron acceptor
G473A
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mutant is able to dimerize and has steady-state activity comparable to that of the wild type, stopped-flow analysis of the reductive half-reaction of this variant yields a rate constant nearly 3 times higher than that of the wild type
G473D
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monomer, mutant is severely impaired both in the ability to bind sulfite and in catalysis, with a second-order rate constant 5 orders of magnitude lower than that of the wild type, significant random-coil formation
G473W
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monomer, mutant with 5fold higher activity than G473D and nearly wild-type activity at pH 7.0 when ferricyanide is the electron acceptor, significant random-coil formation
P105A
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the mutant enzyme shows increased catalytic efficiency compared to the wild type enzyme
P105A/P111A
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the mutant enzyme shows about 30% decreased catalytic efficiency compared to the wild type enzyme
P111A
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the mutant enzyme shows about 30% decreased catalytic efficiency compared to the wild type enzyme
R212A/G473D
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mutant is able to oligomerize but has undetectable activity, significant random-coil formation
R55K
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heme potential is similar to wild-type, the molybdenum redox potential is not affected. Wild-type and mutant show pH dependence of the electrochemical catalytic halfwave potential
R55Q
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heme potential is lowered from ca. 240 mV in wild-type to ca. 200 mV, the molybdenum redox potential is not affected
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
food industry
additional information
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