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Enzyme Nomenclature
Information on EC 1.8.3.1 - sulfite oxidase
Word Map on EC 1.8.3.1
- 1.8.3.1
- molybdenum
- sulfur
- xanthine
- epr
- molybdopterin
-
molybdoenzymes
- tungsten
- moco
- thiosulfate
-
sulfur-containing
- pterin
-
molybdenum-containing
- s-sulfocysteine
-
hyperfine
- so2
-
eseem
-
low-ph
-
pyranopterins
-
dithiolene
-
amidoxime
-
high-ph
- analysis
- agriculture
- food industry
-
xanthinuria
-
oxidase-deficient
- medicine
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Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.8.3.1
-
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RECOMMENDED NAME
GeneOntology No.
sulfite oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sulfite + O2 + H2O = sulfate + H2O2
this direct reduction of O2 is prevented completely in presence of cytochrome c
-
sulfite + O2 + H2O = sulfate + H2O2
x-ray absorption spectroscopy of oxidation states
-
sulfite + O2 + H2O = sulfate + H2O2
mechanism and kinetics of electron transfer
-
sulfite + O2 + H2O = sulfate + H2O2
intramolecular electron transfer and effect of solution viscosity
-
sulfite + O2 + H2O = sulfate + H2O2
mechanism and kinetics of electron transfer
-
sulfite + O2 + H2O = sulfate + H2O2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
additional information
-
the enzyme also functions as a selenite oxidase
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
sulfite:oxygen oxidoreductase
A molybdohemoprotein.
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CAS REGISTRY NUMBER
COMMENTARY
9029-38-3
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
392995, 392996, 392997, 392998, 393000, 393001, 393002, 393003, 393004, 393005, 393006, 393007, 393008, 393009, 393011, 393012, 393016, 393019, 393020, 393021, 393022, 393027, 393029, 393037, 657738, 691180, 691671, 692681, 694617, 701313
-
-
-
392989, 392990, 392991, 392992, 392993, 393001, 393008, 393009, 393010, 393013, 393017, 393018, 393023, 393024, 393033, 393034, 393036, 393038, 393039, 694617
-
-
-
393028, 393029, 393030, 393032, 657446, 657738, 657961, 659231, 659319, 667632, 667714, 668938, 669050, 692611, 692613, 692744, 692747, 692772, 694023, 694371, 694617, 695142, 724332, 724810, 725556
-
-
three patients with isolated sulfite oxidase deficiency, who manifested intractable seizures and severe hypotonia in the immediate postnatal period with an unknown diagnosis, despite extensive workup
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
enzyme is able to couple efficiently to a cytochrome c isolated from the same organism despite being unable to efficiently reduce horse heart cytochrome c. Enzyme interacts with two small redox proteins, a cytochrome c and a Cu containing pseudoazurin, that are encoded in the same operon and are co-transcribed with the sorT gene. The pseudoazurin may act as an intermediate electron shuttle between. The protein system appears to couple directly to the respiratory chain, most likely to a cytochrome oxidase
physiological function
-
enzyme-deficient mutants are consistently negatively affected upon SO2 exposure at 600 nl/l for 60 h and show phenotypical symptoms of injury with small necrotic spots on the leaves. The mean g(H2O) is reduced by about 60% over the fumigation period, accompanied by a reduction of net CO2 assimilation and SO2 uptake of about 50 and 35%, respectively. Sulfur metabolism is completely distorted. Whereas sulfate pool is kept constant, thiol-levels strongly increase
physiological function
-
during extended dark, sulfite oxidase activity is enhanced in tomato wild-type leaves, while the other sulfite network components are down-regulated. RNA interference treated plants accumulate sulfite, resulting in leaf damage and mortality. Exogenous sulfite application induces up-regulation of the sulfite scavenger activities in dark-stressed or unstressed wild-type plants, while expression of the sulfite producer, adenosine 5'-phosphosulfate reductase, is down-regulated. Unstressed or dark-stressed wild-type plants are resistant to sulfite applications, but enzyme RNA interference plants show sensitivity and overaccumulation of sulfite. Under extended dark stress, SO activity is necessary to cope with rising endogenous sulfite levels. Under nonstressed conditions, the sulfite network can control sulfite levels in the absence of enzyme activity
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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
selenite + ferricyanide + H2O
? + ferrocyanide
-
approximately 5% of the observed sulfite activity
-
-
?
SO32- + H2O + 2 Fe(III)cytochrome c
SO42- + 2 Fe(II)cytochrome c + 2 H+
-
-
-
-
?
SO32- + H2O + 2 ferricytochrome c
SO42- + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
-
significantly slower activity than that observed with ferricyanide
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
-
-
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
-
genetic deficiency results in neurological abnormities
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
-
detoxification
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
-
-
-
-
-
sulfite + cytochrome c
sulfate + reduced cytochrome c
-
natural acceptor
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
substrates horse heart cytochrome c, and recombinant Starkeya novella cytochrome c are only reduced to about 40% while Sinorhizobium meliloti cytochrome c is almost completely reduced. Enzyme interacts with two small redox proteins, a cytochrome c and a Cu containing pseudoazurin, that are encoded in the same operon and are co-transcribed with the sorT gene
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
-
-
-
-
?
sulfite + H2O + A
SO42- + AH2
-
A: electron acceptor, i.e. O2, cytochrome c, K3[Fe(CN)6], 2,6-dichloroindophenol, methylene blue, highly specific for sulfite as electron donor
-
-
?
sulfite + H2O + A
SO42- + AH2
-
A: electron acceptor, i.e. O2, cytochrome c, K3[Fe(CN)6], 2,6-dichloroindophenol, methylene blue, highly specific for sulfite as electron donor
-
-
?
sulfite + H2O + A
SO42- + AH2
-
A: electron acceptor, i.e. O2, cytochrome c, K3[Fe(CN)6], 2,6-dichloroindophenol, methylene blue, highly specific for sulfite as electron donor
-
-
?
sulfite + H2O + A
SO42- + AH2
-
artificial A: tetramethylphenylenediamine, 2,6-dichloroindophenol, methylene blue
-
-
-
sulfite + H2O + A
SO42- + AH2
-
H2O2 acceptor only when respiratory chain is inhibited
-
-
?
sulfite + H2O + A
SO42- + AH2
-
A: electron acceptor, i.e. O2, cytochrome c, K3[Fe(CN)6], 2,6-dichloroindophenol, methylene blue, highly specific for sulfite as electron donor
-
-
?
sulfite + H2O + A
sulfate + AH2
-
the active site of the native enzyme can adopt both six-coordinate and five-coordinate geometries, which may be important in the catalytic mechanism, which may involve the binding of anions such as sulfite directly to Mo
-
-
?
sulfite + H2O + A
sulfate + AH2
-
the initial step in the oxygen-atom transfer reaction with HSO3- takes place by oxoanionic binding of the substrate to the MoVI center with the formation of a stable Michaelis complex
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
lack of active enzyme produces severe neurodegeneration and early death in humans
-
-
?
additional information
?
-
-
the enzyme is believed to detoxify excess sulfite that is produced during sulfur assimilation, or due to air pollution
-
-
-
additional information
?
-
-
No activity is found with cytochrome c as electron acceptor, since the heme domain known to mediate electron transfer between the molybdenum cofactor-domain and cytochrome c in rat hepatic SO is missing in the plant enzyme
-
-
-
additional information
?
-
-
the enzyme does not react with cytochrome c
-
-
-
additional information
?
-
-
the plant sulfite oxidase does not accept cyctochrome c as substrate
-
-
-
additional information
?
-
-
the plant sulfite oxidase does not accept cyctochrome c as substrate
-
-
-
additional information
?
-
-
The optimal substrate or precise physiological role for YedYZ in Escherichia coli and its well-conserved orthologs in other bacteria remains unknown.
-
-
-
additional information
?
-
R138, R190, and R450 contribute to a positively charged binding pocket, which stabilizes substrate/product binding
-
-
-
additional information
?
-
-
the plant sulfite oxidase does not accept cyctochrome c as substrate
-
-
-
additional information
?
-
-
the plant sulfite oxidase does not accept cyctochrome c as substrate
-
-
-
additional information
?
-
-
Oax-Mo-Sthiolate-C dihedral angles near 90° effectively eliminate covalency contributions to the Mo(xy) redox orbital from the thiolate sulfur. The Oax-Mo-Sthiolate-C dihedral angle is shown to have a pronounced effect on the relative intensity ratios of the XAS spin-allowed S(1s)fSv(p) + Mo-(xy) and S(1s)fSv(p) + Mo(xz,yz) transitions
-
-
-
additional information
?
-
-
the plant sulfite oxidase does not accept cyctochrome c as substrate
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
?
-
-
the enzyme is believed to detoxify excess sulfite that is produced during sulfur assimilation, or due to air pollution
-
-
-
sulfite + cytochrome c
sulfate + reduced cytochrome c
-
genetic deficiency results in neurological abnormities
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
-
detoxification
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
-
natural acceptor
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
lack of active enzyme produces severe neurodegeneration and early death in humans
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
-
interactions of residue H90 with a heme propionate group destabilize the Fe(III) state of the heme
additional information
-
the enzyme is lacking the heme domain that is known from vertebrate sulfite oxidase
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cl-
-
equatorial coordination of chloride in the enzyme. Chloride in low pH sulfite oxidase can only be weakly coordinated to the axial position, trans to the oxo ligand
Mo
Molybdenum
Sodium arsenate
-
up to a concentration of 5 mM, up to 2fold activation
Mo
-
coordination of sulfate to the Mo(V) center in the blocked form of sulfite oxidase
Mo
-
direct coordination of molybdenum by chloride. Increase in Mo-S/Cl ligation with reduced conditions of low-pH Cl- formation, relative to those of high-pH formation
Mo
-
the wild-type enzyme is five-coordinate with approximately square-based pyramidal geometry
Mo
-
the oxygen-atom transfer reactions involve the formation of the stable intermediate (MoO2HSO3)- through oxoanionic binding of HSO3- at the Mo center
Mo
-
the putative chlorine nucleus is, in all probability, weakly coordinated to the Mo(V) complex of the enzyme
Molybdenum
-
dimeric enzyme contains only a single molybdenum cofactor domain without an additional redox center
Molybdenum
-
molybdenum covalently bound to two sulfur atoms of a unique tricyclic pterin moiety referred to as molybdopterin, essential for dimerization of the enzyme
Molybdenum
-
consists of a single molybdenum atom coordinated through the dithiolene group of a single molybdopterin molecule
Molybdenum
-
sulfite oxidation occurs at the dioxomolybdenum center of the enzyme
Molybdenum
recombinant enzyme contains 0.69 molecules of Mo per protein subunit
Molybdenum
-
the addition of molybdenum to culture media at a concentration of 2.07 mM molybdate leads to a 4fold increase in activity
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
K2HPO4
-
at 26 mM 50% inhibition if cytochrome c or ferricyanide is electron acceptor
K2SO4
-
at 22 mM 50% inhibition if cytochrome c or ferricyanide is electron acceptor
KF
-
at 72 mM 50% inhibition if cytochrome c or ferricyanide is electron acceptor
KNCS
-
at 57 mM 50% inhibition if cytochrome c or ferricyanide is electron acceptor
N-cyclohexyl-N'-[2-(N-methylmorpholino)-ethyl]carbodiimide p-toluene sulfonate
-
CMC
sodium sulfite
-
a high initial concentration of sodium sulfite decreases dramatically the enzyme expression
sodium tungstate
-
at pH 7.5 sodium tungstate inhibits enzyme activity as follows: 1 mM 8% inhibition, 3 mM 36% inhibition, 10 mM 49% inhibition, 50 mM complete inhibition, stronger inhibition at pH 7.0 than at pH 3.0
KCl
-
at 95 mM 50% inhibition if cytochrome c or ferricyanide is electron acceptor
KNO3
-
at 78 mM 50% inhibition if cytochrome c or ferricyanide is electron acceptor
NaCl
-
at 100 mM 50% inhibition if cytochrome c or ferricyanide is electron acceptor
RNAi
-
abrogates sulfite oxidase expression, whereby accumulating relatively less sulfate after SO2 application and showing enhanced induction of senescence and wounding associated transcripts, leaf necrosis and chlorophyll bleaching
-
RNAi
-
abrogates sulfite oxidase expression, whereby accumulating relatively less sulfate after SO2 application and showing enhanced induction of senescence and wounding associated transcripts, leaf necrosis and chlorophyll bleaching
-
additional information
-
maintaining animals on high tungsten, low molybdenum diet, effectively induces SOX deficiency
-
additional information
-
maintaining the animal on low-molybdenum, high-tungsten diet, leads to an effective production of SOX deficiency
-
additional information
-
administration of high-tungsten/low molybdenum regimen leads to deficiency in SOX
-
additional information
-
is inactivated in the dark via a process in which a Ser residue (Ser543) in the hinge region connecting the Mo-PPT dimerization domain with the heme b5 domain is phosphorylated, followed by binding of the NIA inhibitor protein
-
additional information
-
inhibition at 400 mM salt concentrations; no inhibition by periodate or 80 mM sulfate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Molybdenum
-
the addition of molybdenum to culture media at a concentration of 2.07 mM molybdate leads to a 4fold increase in activity
Tris-acetate
-
up to a concentration of 70 mM, up to 2fold activation
additional information
-
SO is constitutively expressed and is not significantly induced by SO2, whereas the SiR transcript involved in sulfur assimilation is highly induced by SO2 in an SO-dependent manner
-
additional information
-
2fold increase in SO activity in fumigated leaf material as compared to non-fumigated plants
-
additional information
-
no variation in SO activity between fumigated and non-fumigated plants
-
additional information
-
electrocatalytic performance requires a sufficient SOx surface concentration in order to generate a catalytic current, and that the amount of cytochrome c within the assembly is high enough to provide a long-range electron transfer to connect the enzyme to the electrode
-
additional information
-
no variation in SO activity between fumigated and non-fumigated plants
-
additional information
-
4fold increase in sulfite oxidase activity in fumigated leaf material as compared to non-fumigated plants
-
additional information
-
SO is constitutively expressed and is not significantly induced by SO2, whereas the SiR transcript involved in sulfur assimilation is highly induced by SO2 in an SO-dependent manner
-
additional information
-
during extended dark, sulfite oxidase activity is enhanced in tomato wild-type leaves, while the other sulfite network components are down-regulated. Exogenous sulfite application induces up-regulation of the sulfite scavenger activities in dark-stressed or unstressed wild-type plants, while expression of the sulfite producer, adenosine 5'-phosphosulfate reductase, is down-regulated
-
additional information
-
molybdenum concentrations higher than 2.07 mM do not show increase of enzyme activity
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0214
sulfite
pH not specified in the publication, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.13
sulfite
Homo sapiens
-
mutant Y343N/R472Q, 25°C, pH 7.0; mutant Y343N/R472Q, 25°C, pH 9.0
26.9
sulfite
Homo sapiens
-
25°C, pH 8.5, 100 mM buffer, wild-type enzyme; 25°C, pH 8.5, 20 mM buffer, wild-type enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
90
additional information
additional information
-
activity in different organelles; comparison of activity in different cells and tissues
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
8.5
8.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
additional information
-
presence of coordinated sulfate in the sulfite reduced low-pH form of the plant enzyme
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
expression in all brain regions examined: cerebellum, cerebral cortex, medulla, spinal cord, ocipital pole, frontal lobe, amygdala, caudate nucleus, corpus callosum, hippocampus, thalamus, temporal lobe, putamen. The cerebral cortex shows the highest level of expression
-
SO shows constitutive expression without any pronounced diurnal rhythm. No difference at the protein level in younger or older rosette or stem leaves
-
rats maintained on standard rat chow and tap water exhibit high level of hepatic SOX activity
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
43300
45000
52000
-
1 * 52000, mutant G473D, calculation from amino acid sequence; 2 * 52000, wild type enzyme, sedimentation equilibrium analysis
53500
-
1 * 53500, mutant G473D, gel filtration and sedimentation equilibrium analysis
55000
66600
-
1 * 66600, double mutant R212A/G473D, sedimentation equilibrium analysis
115000 - 120000
45000
-
2 * 45000, the enzyme is inactive as monomer and dimerization depends on the presence of molybdenum
55000
-
? * 55000, SDS-PAGE, heterogenous behaviour in sedimentation equilibrium experiments
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
-
2 * 45000, the enzyme is inactive as monomer and dimerization depends on the presence of molybdenum
monomer
additional information
?
-
? * 55000, SDS-PAGE, heterogenous behaviour in sedimentation equilibrium experiments
monomer
-
1 * 52000, mutant G473D, calculation from amino acid sequence; 1 * 53500, mutant G473D, gel filtration and sedimentation equilibrium analysis; 1 * 54500, mutant G473W, sedimentation equilibrium analysis; 1 * 66600, double mutant R212A/G473D, sedimentation equilibrium analysis
additional information
-
after tryptic cleavage: 9500, heme-containing fragment, gel filtration with guanidine-HCl, 47400, molybdenum-containing fragment, SDS-PAGE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
vapor diffusion method, crystal structure of cytochrome b5 doamin at 1.2 A resolution
-
crystal structure of (3,5-dimethyltrispyrazol-1-yl)borate MoO(2-mercaptobenzyl alcohol), the first oxomolybdenum monothiolate to possess an Oax-Mo-Sthiolate-C dihedral angle of ca. 90°
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9.5
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45 - 60
-
half-lives of 10 min at 60°C, 30 min at 55°C, and 3 h at 45°C, respectively
50 - 80
-
The enzyme retains 100% of residual activity up to 7 h of incubation at 50°C. Half life times of the enzyme at 60, 70 and 80°C are respectively 8, 6.5 and 1.5 h. The enzyme retains 30% of activity at 25°C and 45% at 90°C.
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
trypsin inactivates
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; by cation-exchange adsorber and ultra filtration, 20fold purified
-
acetone fractionation, ion exchange chromatography and Sephadex gel filtration
-
DEAE 52 column chromatography, Superdex X26 gel filtration and hydroxyapatite column chromatography
-
nickelnitrilotriacetic acid superflow matrix followed by anion exchange chromatography on a SourceQ15 column
-
partial
phenyl-Sepharose column chromatography and Superdex 200 16/60 FPLC column gel filtration
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
constitutive overexpression
expressed in Escherichia coli strain TP1000
expressed in Escherichia coli strains BL21-CodonPlus(DE3)-RIL and TP1000
-
expression in Escherichia coli
His-tagged SO expressed in Escherichia coli TP1000 cells containing plasmid pTG718
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
sulfate oxidase SO activity and sulate-oxidase-dependent H2O2-generating activity in Hibiscus chlorotic ringspot virus-infected leaves increases about 4.5fold compared with that in mock-inoculated kenaf plants
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R138Q
-
the side chain nitrogen of the Gln appears to be within the coordination sphere of the Mo
Y322F/R450M
-
introduction of predicted catalytic site residues of assimilatory nitrate reductase, markedly decreased ability to bind sulfite at pH 8.5
A208D
D342K
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significant decrease in the intramolecular electron transfer rate constant, kcat value is higher than the corresponding intramolecular electron transfer rate constant values, and the redox potentials of both metal centers are affected
F57A
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the size and hydrophobicity of F57 play an important role in modulating the heme potential, residue F57 also affects the intramolecular electron transfer rate
F57Y
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the size and hydrophobicity of F57 play an important role in modulating the heme potential, residue F57 also affects the intramolecular electron transfer rate
F79A
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the size and hydrophobicity of F57 play an important role in modulating the heme potential, residue F57 also affects the intramolecular electron transfer rate
G473A
G473D
G473W
H90F
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interactions of H90 with a heme propionate group destabilize the Fe(III) state of the heme
H90Y
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interactions of H90 with a heme propionate group destabilize the Fe(III) state of the heme
R160K
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the intramolecular electron transfer rate constant for the mutant enzyme is about one-fourth that of the wild-type enzyme
R160Q
R212A/G473D
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mutant is able to oligomerize but has undetectable activity, significant random-coil formation
R472D
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significant decrease in the intramolecular electron transfer rate constant, and the redox potentials of both metal centers are affected
R472D/D342K
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mutation reverses the charges of the salt bridge components, large decrease in intramolecular electron transfer rate constant
R472M
R472Q
Y343F
Y343X
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isolated sulfite oxidase deficiency, shows early neonatal leukoencephalopathy and extensive symmetric cerebral injury especially white matter and basal ganglia
Y83A
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mutation is located on the surface of the heme domain, but not in direct contact with the heme or the propionate groups, little effect on either intramolecular electron transfer or the heme potential
Y83F
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mutation is located on the surface of the heme domain, but not in direct contact with the heme or the propionate groups, little effect on either intramolecular electron transfer or the heme potential
additional information
A208D
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the intramolecular electron transfer rate constants at pH 6.0 are decreased by 3 orders of magnitude relative to that of the wild type, the active site structure of the Mo(V) form of A208D is different from that of the wild type
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, the Mo(V) active site structure is similar to that of the wild type, and the IET rate constant is only 2.6fold smaller 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
R160Q
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the intramolecular electron transfer rate constant for the mutant enzyme at pH 6.0 is decreased by nearly 3 orders of magnitude relative to wild-type enzyme. The intramolecular electron transfer is rate-limiting in the catalytic cycle of the mutant, fatal impact of this mutation in patients with this genetic disorder
R160Q
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clinical mutant, has a six-coordinate pseudooctahedral active site with coordination of glutamine Oepsilon to molybdenum
R160Q
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at least three different Mo(V) species of R160Q exist as a function of pH (low pH type 1 and type 2, and high-pH). Mo(V) species with a blocked form of sulfite oxidase, with sulfate coordinated to the Mo center is the only species at pH higher or equal as 6 and remains a significant form at physiological pH, is six-coordinate and has a nearby exchangeable proton that is likely to be hydrogen-bonded to an oxygen of the sulfate ligand. The blocked structure of R160Q represents a catalytic dead end that contributes to the lethality of this mutant under physiological conditions
R160Q
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mutation increases the Km for sulfite and decreases the kcat, resulting in a 1000fold decrease in catalytic efficiency. Reveals an increase in coordination number for the Mo, from 5 to 6
R472M
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introduction of predicted catalytic site residues of assimilatory nitrate reductase, kinetic analysis
R472M
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significant decrease in the intramolecular electron transfer rate constant, kcat value is higher than the corresponding intramolecular electron transfer rate constant values, and the redox potentials of both metal centers are affected
R472Q
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introduction of predicted catalytic site residues of assimilatory nitrate reductase, kinetic analysis
R472Q
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significant decrease in the intramolecular electron transfer rate constant, kcat value is higher than the corresponding intramolecular electron transfer rate constant values, and the redox potentials of both metal centers are affected
Y343F
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increase in the Km-value for sulfite and a decrease in turnover number results in a 23fold attenuation in the specificity constant turnover (ratio of number to KM-value for sulfite) at optimum pH value of 8.25
Y343F
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in the mutant enzyme using cytochrome c as electron acceptor, turnover number is somewhat impaired, 34% of the wild-type activity at pH 8.5. The KM-value for the mutant enzyme shows a 5fold increase over wild-type. Reduction of the molybdenum center of the Y343 F variant by sulfite is more significantly impaired at high pH than at low pH
Y343F
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under low pH conditions the active site of Y343F is in the blocked form, with the Mo(V) center coordinated by sulfate. The Y343F mutation increases the apparent pKa of the transition from the low pH to high pH forms by ca. 2 pH units. An additional low pH form that has no exchangeable protons
additional information
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a 1 bp insertion located in exon 4 of the bovine SUOX gene (c.363-364insG) is the causative mutation for arachnomelia
additional information
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optimized expression in Escherichia coli, untagged and His-tagged enzyme, expression in presence of tungstate
additional information
isolated sulfite oxidase deficiency, extensive brain damage in the gray matter and more pronounced damage in the white matter, without subsequent recovery. Early onset of energetic and metabolic imbalance. Impaired energetic status and accumulated metabolites
additional information
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SUOX deficiency is typically inherited as a recessive autosomal trait for which there is no known therapy and typically results in death in infancy
additional information
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in tobacco mutants lacking the molybdenum cofactor and, therefore, also lacking active peroxisomal sulfite oxidase, the total sulfite oxidizing capacity of cell extracts decreased to 40% of the wild-type
additional information
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SOX activity is almost devoid in SOX-deficient rats with respect to controls. In SOX-deficient rats, plasma levels of selenium, iron, and zinc are unaffected by sulfite. Plasma level of Mn is decreasing, while plasma Cu level is increased. Treating SOX-deficient groups with sulfite does not alter plasma level of Mn but makes plasma level of Cu back to its normal level. In SOX-deficient rats, plasma ceruloplasmin ferroxidase activities are lower compared to normal control without sulfite treatment
additional information
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SOX activity in SOX-deficient animals is significantly reduced by 95-99%. In SOX-deficient rats, sulfite treatment causes a significant increase in the plasma lipid hydroperoxide and total oxidant status levels, while -SH content of rat plasma significantly decreases compared to the control. Significant decrease in plasma total antioxidant capacity level by sulfite treatment
additional information
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SOX-deficient rats, exposure to sulfite has no effect on hippocampus antioxidant enzymes superoxidase dismutase, catalase, and glutathione peroxidase
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in vitro insertion of molybdopterin into aposulfite oxidase and conversion of molybdopterin into molybdenum cofactor
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
over-expression in tobacco plants enhances their tolerance to sulfite stress. The plants show much less damage, less sulfite accumulation, but greater amounts of sulfate. H2O2 accumulation levels by histochemical detection and quantitative determination in the overexpressing plants are much less than those in the wild-type upon sulfite stress. Reductions of catalase levels detected in the overexpressing lines are considerably less than in the wild-type plants
analysis
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electroimmobilisation into polypyrrole film, use for amperometric detection of sulfite
food industry
medicine
additional information
food industry
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biosensor for detection of sulfite in food and beverages; useful for establishing biosensor systems for detection of sulfite in food and beverages considering the high sensitivity of biosensors and the increasing demand for such biosensor devices
food industry
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artificial ETC composed of cytochrome c and sulfite oxidase formed by the layer-by-layer technique using a polyelectrolyte. The multilayer technology, e.g. sulfite oxidase-cyt c multilayer electrode may act as an anode in a bio-fuel cell and furthermore such multilayers may be exploited as a biosensor for the detection of sulfite, which is used as a preservative in wine and other foodstuffs
medicine
magnetic resonance imaging and magnetic resonance spectroscopy measurements may help differentiate isolated sulfite oxidase deficiency from hypoxic-ischemic condition in patients in whom this diagnosis is not clinically suspected and may lead to further genetic antenatal inquiry that may prevent the birth of other infants affected with this severe and incurable congenital disease
medicine
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low plasma total homocysteine is a valuable early indicator of sulfite oxidase dysfunction, providing a crucial first-line screen, whereas plasma cystine is not always informative in the first few days of life
medicine
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deficiency in SO, due to either a defect in molybdopterin cofactor biosynthesis or a mutation in the apo-enzyme gene itself, leads to dramatic neurological problems that can cause death in early infancy
additional information
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sulfite treatment may cause oxidative stress, and SOX normal animal copes with this stressful condition due to oxidative/antioxidative balance, whereas SOX-deficent rats, which are an exaggerated model for the normal human situation, cannot handle the sulfite-dependent oxidative stress
additional information
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alternative functional model ([Mo(TmMe)(O)2Cl]) of the metalloenzyme sulfite oxidase undergoes oxygen atom transfer chemistry and performs the primary function of the enzyme, sulfite oxidation
additional information
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sulfite treatment may cause oxidative stress and competent animals in SOX cope with this stressful conditions by increase in all antioxidant enzyme activities
additional information
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layer-by-layer assembly of globular proteins is feasible without use of polymers as counterpolyelectrolyte, which is interesting for the construction of third-generation biosensors. The assembly is made by co-adsorption of the enzyme SOx and the electron transfer protein cytochrome c
additional information
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SO may play a role in protecting catalase from sulfite damage. SO may possibly serve as a safety valve to detoxify excess amounts of sulfite and protect the cell from sulfitolysis
additional information
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SO may possibly serve as a safety valve to detoxify excess amounts of sulfite and protect the cell from sulfitolysis
additional information
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sulfite oxidase may possibly serve as a safety valve to detoxify excess amounts of sulfite and protect the cell from sulfitolysis
additional information
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plants can utilize sulfite oxidase in a sulfite oxidative pathway to cope with sulfite overflow. Protects plants from toxic doses of SO2 gas
additional information
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plants can utilize sulfite oxidase in a sulfite oxidative pathway to cope with sulfite overflow. Protects plants from toxic doses of SO2 gas
LINKS TO OTHER DATABASES (specific for EC-Number 1.8.3.1)
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