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nitrite + ferricytochrome c
nitric oxide + ferrocytochrome c
-
the enzyme can oxidize sulfite, and direct the electrons to reducing nitrite, to yield nitric oxide in the mitochondria
-
-
?
nitrite + H2O + porcine ferricytochrome c
nitric oxide + porcine ferrocytochrome c
the nitrite reduction mechanism involves sulfite oxidation, sulfate release and nitrite coordination at molybdenum with protonation-dependent nitric oxide and molybdenum V release. The highest nitric oxide production occurs between 0.01 and 0.0375 mM sulfite, with a dose-dependent inhibition of nitric oxide formation at higher sulfite concentrations
-
-
?
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 ferricyanide
SO42- + 2 ferrocyanide + 2 H+
-
-
-
-
?
SO32- + H2O + 2 ferricytochrome c
SO42- + 2 ferrocytochrome c + 2 H+
-
-
-
-
?
SO32- + H2O + O2
SO42- + H2O2
sodium sulfite + H2O + A
NaSO42- + AH2
-
-
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
sulfite + ferricyanide + H+
sulfate + reduced ferricyanide
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
sulfite + H2O + A
SO42- + AH2
sulfite + H2O + A
sulfate + AH2
sulfite + H2O + ferricyanide
sulfate + ferrocyanide
-
-
-
-
ir
sulfite + H2O + O2
sulfate + hydrogen peroxide
-
-
-
-
?
sulfite + H2O + porcine ferricyanide
sulfate + porcine ferrocyanide
-
-
-
?
sulfite + H2O + porcine ferricytochrome c
sulfate + porcine ferrocytochrome c
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
sulfite + O2 + H2O
sulfate + hydrogen peroxide
-
-
-
-
?
additional information
?
-
SO32- + H2O + O2
SO42- + H2O2
-
-
-
-
?
SO32- + H2O + O2
SO42- + H2O2
-
-
-
?
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
-
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
-
catalytic cycle
-
-
?
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 + cytochrome c
sulfate + reduced cytochrome c
-
-
-
-
?
sulfite + cytochrome c
sulfate + reduced cytochrome c
-
detoxification
-
-
?
sulfite + ferricyanide + H+
sulfate + reduced ferricyanide
-
-
-
?
sulfite + ferricyanide + H+
sulfate + reduced ferricyanide
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
-
-
-
-
?
sulfite + ferricyanide + H2O
sulfate + ferrocyanide
-
-
-
?
sulfite + H2O + A
SO42- + AH2
-
-
-
-
?
sulfite + H2O + A
SO42- + AH2
-
-
-
-
?
sulfite + H2O + A
SO42- + AH2
-
-
-
?
sulfite + H2O + A
SO42- + AH2
-
-
-
-
?
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
-
-
-
-
?
sulfite + H2O + A
SO42- + AH2
-
-
-
-
?
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
-
-
-
-
?
sulfite + H2O + A
SO42- + AH2
-
-
-
-
?
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
-
-
-
-
?
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
SO42- + AH2
-
-
-
-
?
sulfite + H2O + A
SO42- + AH2
-
-
-
-
?
sulfite + H2O + A
SO42- + AH2
-
-
-
-
?
sulfite + H2O + A
sulfate + AH2
-
-
-
-
?
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
-
-
-
-
?
sulfite + H2O + A
sulfate + AH2
-
-
-
-
?
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
-
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
lack of active enzyme produces severe neurodegeneration and early death in humans
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
sulfite is the physiological substrate
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
the enzyme catalyzes the oxidation of sulfite to sulfate using ferricytochrome c as the physiological electron acceptor
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
under normal physiological conditions, SO catalyzes the oxidation of sulfite to sulfate with cytochrome c (cyt c) as oxidizing substrate
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
during the sulfite-sulfite oxidase-cytochrome c catalytic cycle, movement between the molybdenum and heme domain is required to enable efficient single-electron transfer from molybdenum via the heme b5 cofactor to cytochrome c
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
usage of Fe3+ oxidized cytochrome c from horse heart
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
-
-
-
r
sulfite + O2 + H2O
sulfate + H2O2
-
-
-
-
r
sulfite + O2 + H2O
sulfate + H2O2
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
-
-
?
sulfite + O2 + H2O
sulfate + H2O2
-
-
-
?
additional information
?
-
the enzyme is believed to detoxify excess sulfite that is produced during sulfur assimilation, or due to air pollution
-
-
?
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
?
-
sulfite ligand docking study, arginine residues particularly Arg374 is crucial for SOX-sulfite binding and two other residues Arg51 and Arg103 are also implicated to be important for SOX-sulfite bindings in plants
-
-
?
additional information
?
-
-
sulfite ligand docking study, arginine residues particularly Arg374 is crucial for SOX-sulfite binding and two other residues Arg51 and Arg103 are also implicated to be important for SOX-sulfite bindings in plants
-
-
?
additional information
?
-
-
the plant sulfite oxidase does not accept cyctochrome c as substrate
-
-
?
additional information
?
-
sulfite ligand docking study
-
-
?
additional information
?
-
-
sulfite ligand docking study
-
-
?
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
?
-
mechanism of oxidation of sulfite and radical generation by ferric cytochrome c (Fe3+ cyt c) in the absence and presence of H2O2, oxidation of sulfite by the Fe3+ cyt c increased with sulfite concentration, overview
-
-
?
additional information
?
-
-
mechanism of oxidation of sulfite and radical generation by ferric cytochrome c (Fe3+ cyt c) in the absence and presence of H2O2, oxidation of sulfite by the Fe3+ cyt c increased with sulfite concentration, overview
-
-
?
additional information
?
-
reduced sulfite oxidase catalyzes single-electron transfer at molybdenum domain to reduce nitrite to nitric oxide. At physiological concentrations of nitrite, sulfite oxidase functions as nitrite reductase in the presence of a one-electron donor, exhibiting redox coupling of substrate oxidation and nitrite reduction to form NO. With sulfite, the physiological substrate, sulfite oxidase only facilitates one turnover of nitrite reduction. Nitrite reduction occurs at the molybdenum center via coupled oxidation of Mo(IV) to Mo(V). Reaction rates of nitrite to NO decreased in the presence of a functional heme domain, mediated by steric and redox effects of this domain. Nitrite binds to and is reduced at the molybdenum site of mammalian sulfite oxidase, which may be allosterically regulated by heme and molybdenum domain interactions, and contributes to the mammalian nitrate-nitrite-NO signaling pathway in human fibroblasts. Using phenosafranine or sulfite as reducing substrate, the Mo-domain shows much faster nitrite reduction to NO than holo-sulfite oxidase, catalytic Mo(IV) to Mo(V) nitrite reduction cycle, overview
-
-
?
additional information
?
-
-
reduced sulfite oxidase catalyzes single-electron transfer at molybdenum domain to reduce nitrite to nitric oxide. At physiological concentrations of nitrite, sulfite oxidase functions as nitrite reductase in the presence of a one-electron donor, exhibiting redox coupling of substrate oxidation and nitrite reduction to form NO. With sulfite, the physiological substrate, sulfite oxidase only facilitates one turnover of nitrite reduction. Nitrite reduction occurs at the molybdenum center via coupled oxidation of Mo(IV) to Mo(V). Reaction rates of nitrite to NO decreased in the presence of a functional heme domain, mediated by steric and redox effects of this domain. Nitrite binds to and is reduced at the molybdenum site of mammalian sulfite oxidase, which may be allosterically regulated by heme and molybdenum domain interactions, and contributes to the mammalian nitrate-nitrite-NO signaling pathway in human fibroblasts. Using phenosafranine or sulfite as reducing substrate, the Mo-domain shows much faster nitrite reduction to NO than holo-sulfite oxidase, catalytic Mo(IV) to Mo(V) nitrite reduction cycle, overview
-
-
?
additional information
?
-
regeneration of the enzyme includes two, one-electron intramolecular electron transfers (IET) from the molybdenum (Mo) to the heme Fe and two, one-electron intermolecular electron transfers from the Fe to external ferricytochrome c
-
-
?
additional information
?
-
-
regeneration of the enzyme includes two, one-electron intramolecular electron transfers (IET) from the molybdenum (Mo) to the heme Fe and two, one-electron intermolecular electron transfers from the Fe to external ferricytochrome c
-
-
?
additional information
?
-
the sulfite oxidase catalyzes single-electron transfer at molybdenum domain to reduce nitrite to nitric oxide. The SO Moco binding domain has the ability to oxidize sulfite in the presence of artificial electron acceptors like ferricyanide. The two-electron oxidation of sulfite to sulfate occurs at the molybdenum site, which is reduced from Mo(VI) to Mo(IV), followed by intramolecular electron transfer to the cytb5 site, with cytochrome c serving as the terminal electron acceptor. The movement of domains between the Moco domain and the cytb5 domain facilitated by the flexible linker is essential for efficient electron transfer between the heme and the Moco
-
-
?
additional information
?
-
-
the sulfite oxidase catalyzes single-electron transfer at molybdenum domain to reduce nitrite to nitric oxide. The SO Moco binding domain has the ability to oxidize sulfite in the presence of artificial electron acceptors like ferricyanide. The two-electron oxidation of sulfite to sulfate occurs at the molybdenum site, which is reduced from Mo(VI) to Mo(IV), followed by intramolecular electron transfer to the cytb5 site, with cytochrome c serving as the terminal electron acceptor. The movement of domains between the Moco domain and the cytb5 domain facilitated by the flexible linker is essential for efficient electron transfer between the heme and the Moco
-
-
?
additional information
?
-
sulfite ligand docking study
-
-
?
additional information
?
-
-
sulfite ligand docking study
-
-
?
additional information
?
-
-
the plant sulfite oxidase does not accept cyctochrome c as substrate
-
-
?
additional information
?
-
sulfite ligand docking study
-
-
?
additional information
?
-
-
sulfite ligand docking study
-
-
?
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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1-Ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride
-
EDC
2,6-dichloroindophenol
-
inhibition of O2 consumption
arsenate
-
100 mM, EPR spectra
cytochrome c
-
inhibition of O2 consumption
diethylpyrocarbonate
-
modifies ten His per enzyme molecule
EDTA
-
20 mM, 50% inhibition
imidazole
-
0.1 mM, complete inhibition
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
mannitol
-
only with O2 as electron acceptor
N-cyclohexyl-N'-[2-(N-methylmorpholino)-ethyl]carbodiimide p-toluene sulfonate
-
CMC
N-ethyl-5-phenylisoxazolium-3'-sulfonate
-
Woodward's reagent K
Ni2+
-
stronger inhibition at pH 7.0 than at pH 3.0
NiCl2
-
0.1 mM, complete inhibition
nitrite
nitrite inhibits sulfite-dependent cytochrome c reduction at sulfite concentrations ranging from 0.01 to 0.1 mM
phosphate
-
100 mM, EPR spectra
potassium nitrate
50% inhibition at 1 mM, in Tris/HCl 20 mM, pH 8.5
Sodium arsenate
-
7 mM, 50% inhibition
Sodium sulfate
-
20 mM, 50% inhibition
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
sulfite
-
competitive inhibitor of nitric oxide production above 0.037 mM
Tris-acetate
-
80 mM, pH 8.0, 50% inhibition
Tris-HCl
-
100 mM, pH 8.0, 50% inhibition
Tris/HCl
50% inhibition at 90 mM, pH 8.5
Ag+
-
-
arsenite
-
-
arsenite
-
7.4 mM, 50% inhibition
CN-
-
-
CN-
-
profound at low O2 concentration, not at high O2 concentration
CN-
-
profound at low O2 concentration, not at high O2 concentration
CN-
-
mechanism of inactivation
ferricyanide
-
inhibition of O2 consumption
ferricyanide
-
irreversible inactivation of molybdenum center
heavy metal ions
-
-
-
Hg2+
-
-
KCl
-
30 mM, 50% inhibition
KCl
-
at 95 mM 50% inhibition if cytochrome c or ferricyanide is electron acceptor
KNO3
-
3 mM, 50% inhibition
KNO3
-
at 78 mM 50% inhibition if cytochrome c or ferricyanide is electron acceptor
methylene blue
-
70% inhibition at 0.4 mM
methylene blue
-
70% inhibition at 0.4 mM
N-bromosuccinimide
-
94% inhibition at 0.1 mM
N-bromosuccinimide
-
94% inhibition at 0.1 mM
NaCl
50% inhibition at 70 mM, in Tris/HCl 20 mM, pH 8.5
NaCl
-
150 mM, 50% inhibition
NaCl
-
at 100 mM 50% inhibition if cytochrome c or ferricyanide is electron acceptor
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
potassium phosphate
50% inhibition at 30 mM, pH 8.5
potassium phosphate
-
20 mM, pH 8.0, 50% inhibition
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
-
tungstate
-
complete inhibition at 1 mM
tungstate
-
treatment with sodium tungstate, leading to a catalytically inactive analogue by replacing molybdenum with tungsten in molybdenum cofactor because of its higher affinity constant. Determination of tolerance and impact of different concentrations of tungstate on the viability of HepG2 cells using a luciferase-based cytotoxicity assay, sodium tungstate is nontoxic up to 1000 ppm
additional information
-
not inhibitory: CN-
-
additional information
-
not inhibitory: CN-
-
additional information
-
not inhibitory: NaN3 at 0.5 mM, NaCN at 0.5 mM
-
additional information
-
not inhibitory: CN-
-
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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0.00043 - 0.107
cytochrome c
additional information
additional information
-
0.00043
cytochrome c
-
mutant enzyme G473A, pH 8.5
0.00082
cytochrome c
-
mutant enzyme G473A, pH 7.0
0.00123
cytochrome c
-
mutant enzyme G473A, pH 6.0
0.00141
cytochrome c
-
wild type enzyme, pH 7.0
0.00173
cytochrome c
-
wild type enzyme, pH 6.0
0.00371
cytochrome c
-
mutant enzyme G473D, pH 8.6
0.0044
cytochrome c
-
wild type enzyme, pH 8.5
0.00474
cytochrome c
-
mutant enzyme G473D, pH 8.0
0.00536
cytochrome c
-
mutant enzyme G473W, pH 8.5
0.014
cytochrome c
-
mutant enzyme G473D, pH 7.5
0.0357
cytochrome c
-
mutant enzyme G473W, pH 7.0
0.0362
cytochrome c
-
mutant enzyme G473D, pH 7.0
0.0635
cytochrome c
-
mutant enzyme G473D, pH 6.5
0.0905
cytochrome c
-
mutant enzyme G473W, pH 6.0
0.107
cytochrome c
-
mutant enzyme G473D, pH 6.0
0.015
O2
-
-
0.00046
sulfite
-
mutant V474M, 25°C, pH 6.0
0.00129
sulfite
-
25°C, pH 6.0, 20 mM buffer, wild-type enzyme
0.00129
sulfite
-
wild type enzyme in 20 mM Tris at pH 6.0
0.00129
sulfite
-
wild type enzyme, pH 6.0
0.0013
sulfite
-
wild-type, 25°C, pH 6.0
0.00133
sulfite
wild-type, 25°C, pH 7.0
0.00134
sulfite
-
mutant V474M, 25°C, pH 7.0
0.00162
sulfite
-
25°C, pH 6.5, 20 mM buffer, wild-type enzyme
0.00162
sulfite
-
wild type enzyme, pH 6.5
0.0017
sulfite
-
mutant Y83A, pH 8.0, 25°C
0.0019
sulfite
-
mutant R472M, 25°C, pH 6.0
0.0023
sulfite
-
mutant R472Q, 25°C, pH 6.0
0.0025
sulfite
-
mutant R472M, 25°C, pH 7.0
0.0027
sulfite
-
wild-type, 25°C, pH 7.0
0.00272
sulfite
-
25°C, pH 7.0, 20 mM buffer, wild-type enzyme
0.00272
sulfite
-
wild type enzyme, pH 7.0
0.0028
sulfite
-
mutant H90F, pH 8.0, 25°C
0.00311
sulfite
-
25°C, pH 6.0, 20 mM buffer, mutant enzyme Y343F
0.0032
sulfite
-
mutant R472K, pH 7.6, 25°C
0.0032
sulfite
-
mutant V474M, 25°C, pH 8.0
0.00339
sulfite
-
wild type enzyme, pH 7.5
0.00339
sulfite
-
25°C, pH 7.5, 20 mM buffer, wild-type enzyme
0.0035
sulfite
-
mutant R472Q, 25°C, pH 7.0
0.00352
sulfite
-
25°C, pH 7.0, 100 mM buffer, mutant enzyme Y343F
0.00362
sulfite
-
25°C, pH 7.0, 100 mM buffer, wild-type enzyme
0.00367
sulfite
-
25°C, pH 7.5, 100 mM buffer, wild-type enzyme
0.0038
sulfite
-
mutant F79A, pH 8.0, 25°C
0.0039
sulfite
-
mutant H90Y, pH 8.0, 25°C
0.004
sulfite
with ferricanide, pH 7.1, 25°C, recombinant wild-type enzyme
0.00414
sulfite
-
25°C, pH 6.5, 20 mM buffer, mutant enzyme Y343F
0.0042
sulfite
with ferricanide, pH 7.1, 25°C, recombinant wild-type enzyme
0.00423
sulfite
-
25°C, pH 7.5, 100 mM buffer, mutant enzyme Y343F
0.0043
sulfite
-
wild-type, 25°C, pH 8.0
0.00435
sulfite
-
25°C, pH 8.0, 20 mM buffer, wild-type enzyme
0.00435
sulfite
-
wild type enzyme, pH 8.0
0.00453
sulfite
-
mutant enzyme G473A in 20 mM Tris at pH 6.0
0.00453
sulfite
-
mutant enzyme G473A, pH 6.0
0.00459
sulfite
-
25°C, pH 7.0, 20 mM buffer, mutant enzyme Y343F
0.0047
sulfite
-
mutant R472M, 25°C, pH 8.0
0.0048
sulfite
with ferricanide, pH 7.1, 25°C, recombinant mutant C242S/C253S/C260S/C451S
0.00503
sulfite
-
25°C, pH 8.25, 20 mM buffer, wild-type enzyme
0.00536
sulfite
-
mutant enzyme G473A, pH 7.0
0.00612
sulfite
-
25°C, pH 8.0, 100 mM buffer, wild-type enzyme
0.0062
sulfite
with ferricanide, pH 7.1, 25°C, recombinant mutant C242S/C253S/C260S/C451S
0.00635
sulfite
-
25°C, pH 7.5, 20 mM buffer, mutant enzyme Y343F
0.00728
sulfite
-
25°C, pH 8.25, 100 mM buffer, wild-type enzyme
0.0079
sulfite
with ferricanide, pH 7.1, 25°C, recombinant selenomethionine-labeled mutant C242S/C253S/C260S/C451S
0.008
sulfite
-
mutant F57Y, pH 8.0, 25°C
0.008
sulfite
wild-type, 25°C, pH 8.5
0.0082
sulfite
with ferricanide, pH 7.1, 25°C, recombinant selenomethionine-labeled mutant C242S/C253S/C260S/C451S
0.00825
sulfite
-
wild type enzyme, pH 8.5
0.00825
sulfite
-
25°C, pH 8.5, 20 mM buffer, wild-type enzyme
0.00825
sulfite
-
wild type enzyme in 20 mM Tris at pH 8.5
0.0083
sulfite
-
wild-type, 25°C, pH 8.5
0.00851
sulfite
-
25°C, pH 10.0, 20 mM buffer, mutant enzyme Y343F
0.00859
sulfite
-
25°C, pH 8.0, 20 mM buffer, mutant enzyme Y343F
0.00908
sulfite
-
25°C, pH 8.25, 20 mM buffer, mutant enzyme Y343F
0.00924
sulfite
-
25°C, pH 8.5, 20 mM buffer, mutant enzyme Y343F
0.00947
sulfite
-
25°C, pH 9.0, 20 mM buffer, mutant enzyme Y343F
0.00959
sulfite
-
25°C, pH 8.75, 20 mM buffer, wild-type enzyme
0.0096
sulfite
with ferricanide, pH 6.0, 25°C, recombinant mutant C242S/C253S/C260S/C451S
0.00963
sulfite
-
25°C, pH 9.5, 20 mM buffer, mutant enzyme Y343F
0.00992
sulfite
-
25°C, pH 9.75, 20 mM buffer, mutant enzyme Y343F
0.0107
sulfite
with ferricanide, pH 8.4, 25°C, recombinant mutant C242S/C253S/C260S/C451S
0.011
sulfite
-
wild-type, pH 8.0, 25°C
0.011
sulfite
-
25°C, pH 8.5, 100 mM buffer, wild-type enzyme
0.012
sulfite
-
mutant D342K, pH 7.6, 25°C
0.012
sulfite
-
mutant Y83F, pH 8.0, 25°C
0.0121
sulfite
with ferricanide, pH 6.0, 25°C, recombinant wild-type enzyme
0.013
sulfite
-
mutant F57A, pH 8.0, 25°C
0.013
sulfite
-
mutant R472Q, 25°C, pH 8.0
0.0144
sulfite
-
mutant V474M, 25°C, pH 9.0
0.0146
sulfite
with ferricanide, pH 8.4, 25°C, recombinant selenomethionine-labeled mutant C242S/C253S/C260S/C451S
0.0158
sulfite
-
25°C, pH 8.0, 100 mM buffer, mutant enzyme Y343F
0.016
sulfite
-
mutant R472Q, 25°C, pH 8.5
0.0166
sulfite
with ferricanide, pH 8.4, 25°C, recombinant wild-type enzyme
0.0172
sulfite
-
mutant enzyme G473A, pH 7.4
0.0174
sulfite
with ferricanide, pH 8.9, 25°C, recombinant selenomethionine-labeled mutant C242S/C253S/C260S/C451S
0.019
sulfite
with ferricanide, pH 6.0, 25°C, recombinant selenomethionine-labeled mutant C242S/C253S/C260S/C451S
0.0196
sulfite
with ferricanide, pH 8.9, 25°C, recombinant wild-type enzyme
0.021
sulfite
-
mutant R472M, 25°C, pH 9.0
0.0214
sulfite
pH not specified in the publication, temperature not specified in the publication
0.022
sulfite
-
mutant R472Q, pH 7.6, 25°C
0.022
sulfite
-
wild-type, 25°C, pH 9.0
0.0221
sulfite
-
25°C, pH 9.0, 20 mM buffer, wild-type enzyme
0.0221
sulfite
-
wild type enzyme, pH 9.0
0.0226
sulfite
-
using ferricyanide as electron acceptor
0.023
sulfite
-
mutant R472D, pH 7.6, 25°C
0.023
sulfite
-
mutant R472D/D342K, pH 7.6, 25°C
0.026
sulfite
-
25°C, pH 9.0, 100 mM buffer, wild-type enzyme
0.0288
sulfite
with ferricanide, pH 8.9, 25°C, recombinant mutant C242S/C253S/C260S/C451S
0.0319
sulfite
-
25°C, pH 8.25, 100 mM buffer, mutant enzyme Y343F
0.0319
sulfite
-
mutant V474M, 25°C, pH 9.5
0.0338
sulfite
-
using ferricyanide as electron acceptor
0.0354
sulfite
-
mutant V474M, 25°C, pH 8.5
0.04
sulfite
-
mutant V474M, 25°C, pH 10.0
0.042
sulfite
-
mutant R472M, pH 7.6, 25°C
0.045
sulfite
-
mutant R472Q, 25°C, pH 9.0
0.0487
sulfite
-
mutant enzyme G473A, pH 8.0
0.051
sulfite
-
mutant R472D, pH 6.5, 25°C
0.0529
sulfite
-
wild-type, 25°C, pH 10.0
0.0536
sulfite
-
25°C, pH 9.5, 100 mM buffer, wild-type enzyme
0.0537
sulfite
-
mutant R472M, 25°C, pH 9.5
0.0557
sulfite
-
25°C, pH 8.5, 100 mM buffer, mutant enzyme Y343F
0.0614
sulfite
-
mutant Y343F/R472Q, 25°C, pH 6.0
0.067
sulfite
-
wild-type, 25°C, pH 9.5
0.0671
sulfite
-
25°C, pH 9.5, 20 mM buffer, wild-type enzyme
0.0671
sulfite
-
wild type enzyme, pH 9.5
0.0692
sulfite
-
mutant enzyme A208D in 20 mM Tris at pH 6.0
0.0877
sulfite
-
mutant Y343F/R472Q, 25°C, pH 7.0
0.094
sulfite
-
mutant R472M, 25°C, pH 8.5
0.0947
sulfite
-
mutant Y343N, 25°C, pH 7.0
0.0953
sulfite
-
mutant Y343N, 25°C, pH 6.0
0.0967
sulfite
-
mutant R472Q, 25°C, pH 9.5
0.0969
sulfite
-
mutant R472M, 25°C, pH 10.0
0.107
sulfite
-
mutant enzyme G473A in 20 mM Tris at pH 8.5
0.107
sulfite
-
mutant enzyme G473A, pH 8.5
0.147
sulfite
-
25°C, pH 9.0, 100 mM buffer, mutant enzyme Y343F
0.181
sulfite
-
mutant R472Q, 25°C, pH 10.0
0.2827
sulfite
-
mutant Y343F/R472Q, 25°C, pH 8.0
0.297
sulfite
-
mutant Y343N, 25°C, pH 8.0
0.33
sulfite
-
mutant enzyme G473W, pH 7.0
0.59 - 1
sulfite
-
25°C, pH 9.5, 100 mM buffer, mutant enzyme Y343F
0.623
sulfite
-
mutant enzyme G473D, pH 7.0
0.712
sulfite
-
mutant Y343F/R472Q, 25°C, pH 8.5
0.774
sulfite
-
mutant enzyme G473A, pH 9.1
0.85
sulfite
-
mutant Y343N, 25°C, pH 8.5
0.99
sulfite
-
mutant enzyme G473D, pH 6.5
1.063
sulfite
-
mutant enzyme G473D, pH 7.5
1.1
sulfite
-
mutant Y343N/R472M/V474M, 25°C, pH 6.0
1.223
sulfite
-
mutant enzyme G473D, pH 8.0
1.39
sulfite
-
mutant enzyme A208D in 20 mM Tris at pH 8.5
1.42
sulfite
-
mutant Y343N/R472M/V474M, 25°C, pH 7.0
1.54
sulfite
-
25°C, pH 10.0, 100 mM buffer, mutant enzyme Y343F
1.66
sulfite
-
mutant enzyme G473D in 20 mM Tris at pH 6.0
1.66
sulfite
-
mutant enzyme G473D, pH 6.0
1.91
sulfite
-
mutant enzyme G473W in 20 mM Tris at pH 6.0
1.91
sulfite
-
mutant enzyme G473W, pH 6.0
2.03
sulfite
-
mutant enzyme G473W in 20 mM Tris at pH 8.5
2.034
sulfite
-
mutant enzyme G473W, pH 8.5
2.04
sulfite
-
mutant enzyme G473D in 20 mM Tris at pH 8.5
2.04
sulfite
-
mutant enzyme G473D, pH 8.5
2.14
sulfite
-
mutant Y343N/R472M/V474M, 25°C, pH 8.0
2.46
sulfite
-
mutant Y343N, 25°C, pH 9.0
3.34
sulfite
-
mutant Y343F/R472Q, 25°C, pH 9.0
3.684
sulfite
-
mutant enzyme G473A, pH 10.0
4.64
sulfite
-
mutant Y343N/R472M, 25°C, pH 7.0
8.6
sulfite
mutant Y322N/R450M, 25°C, pH 7.0
9.37
sulfite
-
mutant Y343N, 25°C, pH 9.5
10.41
sulfite
-
mutant enzyme G473W, pH 9.0
11.73
sulfite
mutant Y322N/R450M, 25°C, pH 8.5
12
sulfite
-
mutant Y343N, 25°C, pH 10.0
14
sulfite
-
mutant Y343N/R472M/V474M, 25°C, pH 8.5
16.8
sulfite
-
mutant Y343N/R472M, 25°C, pH 6.0
19.28
sulfite
-
mutant Y343N/R472M, 25°C, pH 8.0
25.88
sulfite
-
mutant enzyme G473D, pH 9.1
39.9
sulfite
-
mutant Y343F/R472Q, 25°C, pH 9.5
42.99
sulfite
-
mutant Y343N/R472M, 25°C, pH 8.5
55.5
sulfite
-
mutant Y343N/R472M/V474M, 25°C, pH 9.0
59.6
sulfite
-
mutant Y343F/R472Q, 25°C, pH 10.0
85.64
sulfite
-
mutant Y343N/R472M, 25°C, pH 9.0
111
sulfite
-
mutant Y343N/R472M/V474M, 25°C, pH 9.5
208
sulfite
-
mutant Y343N/R472m, 25°C, pH 9.5
418
sulfite
-
mutant Y343N/R472M/V474M, 25°C, pH 10.0
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
kinetic studies
-
additional information
additional information
-
variation of KM with pH
-
additional information
additional information
steady-state kinetics
-
additional information
additional information
-
steady-state kinetics
-
additional information
additional information
kinetics of sulfite oxidase-dependent nitrite reduction, the catalyzes single-electron transfer is similar to Michaelis-Menten kinetics
-
additional information
additional information
-
kinetics of sulfite oxidase-dependent nitrite reduction, the catalyzes single-electron transfer is similar to Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten model
-
additional information
additional information
Michaelis-Menten steady-state kinetics of wild-type and mutant enzymes. All of the mutants show decreased rates of intramolecular electron transfer (IET) but increased steady-state rates of catalysis
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics of wild-type and mutant enzymes. All of the mutants show decreased rates of intramolecular electron transfer (IET) but increased steady-state rates of catalysis
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.34
cytochrome c
-
mutant enzyme G473D, pH 6.0
0.48
cytochrome c
-
mutant enzyme G473D, pH 8.6
0.53
cytochrome c
-
mutant enzyme G473D, pH 6.5
0.59
cytochrome c
-
mutant enzyme G473D, pH 8.0
0.62
cytochrome c
-
mutant enzyme G473D, pH 7.5
0.78
cytochrome c
-
mutant enzyme G473D, pH 7.0
1.67
cytochrome c
-
mutant enzyme G473W, pH 6.0
1.95
cytochrome c
-
mutant enzyme G473W, pH 8.5
2.94
cytochrome c
-
mutant enzyme G473W, pH 7.0
3.83
cytochrome c
-
mutant enzyme G473A, pH 6.0
12.4
cytochrome c
-
wild type enzyme, pH 6.0
12.8
cytochrome c
-
mutant enzyme G473A, pH 7.0
18.1
cytochrome c
-
wild type enzyme, pH 7.0
25.4
cytochrome c
-
mutant enzyme G473A, pH 8.5
26.9
cytochrome c
-
wild type enzyme, pH 8.5
0.14
sulfite
-
mutant enzyme G473D in 20 mM Tris at pH 6.0
0.14
sulfite
-
mutant enzyme G473D, pH 6.0
0.15
sulfite
-
mutant enzyme A208D in 20 mM Tris at pH 6.0
0.28
sulfite
-
mutant enzyme G473D, pH 6.5
0.42
sulfite
-
mutant enzyme G473D, pH 9.1
0.46
sulfite
-
mutant R472M, 25°C, pH 10.0
0.5
sulfite
-
mutant enzyme G473D, pH 7.0
0.52
sulfite
-
mutant R472Q, 25°C, pH 10.0
0.54
sulfite
-
mutant enzyme G473D in 20 mM Tris at pH 8.5
0.54
sulfite
-
mutant enzyme G473D, pH 8.5
0.57
sulfite
-
mutant enzyme G473D, pH 7.5
0.58
sulfite
-
mutant enzyme G473D, pH 8.0
0.6
sulfite
-
mutant enzyme G473W in 20 mM Tris at pH 6.0
0.6
sulfite
-
mutant enzyme G473W, pH 6.0
0.75
sulfite
-
mutant enzyme A208D in 20 mM Tris at pH 8.5
0.97
sulfite
-
mutant Y343N/R472Q, 25°C, pH 9.5
1.13
sulfite
-
mutant Y343N/R472Q, 25°C, pH 7.0
1.13
sulfite
-
mutant Y343N/R472Q, 25°C, pH 9.0
1.33
sulfite
-
mutant Y343N/R472Q, 25°C, pH 8.0
1.35
sulfite
-
mutant enzyme G473W, pH 9.0
1.35
sulfite
-
mutant Y343N/R472Q, 25°C, pH 6.0
1.42
sulfite
-
mutant Y343N/R472Q, 25°C, pH 8.5
1.44
sulfite
-
mutant Y343F/R472Q, 25°C, pH 6.0
1.7
sulfite
-
mutant R472Q, 25°C, pH 9.5
1.73
sulfite
-
mutant Y343F/R472Q, 25°C, pH 7.0
1.8
sulfite
-
mutant enzyme G473W, pH 7.0
1.8
sulfite
-
mutant R472M, 25°C, pH 9.5
1.9
sulfite
-
mutant Y343N/R472M/V474M, 25°C, pH 6.0
2.05
sulfite
-
mutant Y343F/R472Q, 25°C, pH 8.0
2.06
sulfite
-
25°C, pH 7.0, 100 mM buffer, mutant enzyme Y343F
2.25
sulfite
-
mutant Y343F/R472Q, 25°C, pH 8.5
2.3
sulfite
-
mutant Y343F/R472Q, 25°C, pH 9.0
2.48
sulfite
-
mutant enzyme G473W in 20 mM Tris at pH 8.5
2.48
sulfite
-
mutant enzyme G473W, pH 8.5
2.52
sulfite
mutant Y322N/R450M, 25°C, pH 8.5
2.8
sulfite
-
mutant Y343N/R472M/V474M, 25°C, pH 10.0
2.96
sulfite
-
mutant Y343F/R472Q, 25°C, pH 10.0
3 - 6
sulfite
-
mutant Y83F, pH 8.0, 25°C
3.11
sulfite
-
25°C, pH 6.0, 20 mM buffer, mutant enzyme Y343F
3.17
sulfite
-
mutant Y343N, 25°C, pH 6.0
3.26
sulfite
-
25°C, pH 7.5, 100 mM buffer, mutant enzyme Y343F
3.4
sulfite
-
mutant Y343N/R472M/V474M, 25°C, pH 7.0
3.45
sulfite
-
mutant R472M, 25°C, pH 9.0
3.5
sulfite
-
mutant R472M, 25°C, pH 8.0
3.58
sulfite
-
mutant Y343N/R472M/V474M, 25°C, pH 8.0
3.6
sulfite
-
mutant R472M, 25°C, pH 7.0
3.8
sulfite
-
mutant R472M, 25°C, pH 8.5
3.9
sulfite
-
mutant Y343N/R472M/V474M, 25°C, pH 8.5
4.14
sulfite
-
25°C, pH 6.5, 20 mM buffer, mutant enzyme Y343F
4.15
sulfite
-
mutant enzyme G473A in 20 mM Tris at pH 6.0
4.15
sulfite
-
mutant enzyme G473A, pH 6.0
4.24
sulfite
-
mutant R472Q, 25°C, pH 9.0
4.38
sulfite
-
mutant Y343N, 25°C, pH 10.0
4.59
sulfite
-
25°C, pH 7.0, 20 mM buffer, mutant enzyme Y343F
4.6
sulfite
-
mutant R472Q, 25°C, pH 8.5
4.83
sulfite
mutant Y322N/R450M, 25°C, pH 7.0
4.9
sulfite
-
mutant Y343F/R472Q, 25°C, pH 9.5
5
sulfite
-
mutant R472M, 25°C, pH 6.0
5.23
sulfite
-
mutant Y343N/R472M/V474M, 25°C, pH 9.5
5.6
sulfite
-
mutant Y343N/R472M/V474M, 25°C, pH 9.0
5.7
sulfite
-
mutant R472D, pH 6.5, 25°C
5.8
sulfite
-
mutant R472Q, 25°C, pH 7.0
5.96
sulfite
-
mutant V474M, 25°C, pH 6.0
6.35
sulfite
-
25°C, pH 7.5, 20 mM buffer, mutant enzyme Y343F
7
sulfite
-
mutant Y83A, pH 8.0, 25°C
7.17
sulfite
-
25°C, pH 8.0, 100 mM buffer, mutant enzyme Y343F
8.1
sulfite
-
mutant Y343N, 25°C, pH 9.5
8.2
sulfite
-
mutant R472Q, 25°C, pH 6.0
8.21
sulfite
-
25°C, pH 10.0, 100 mM buffer, mutant enzyme Y343F
8.51
sulfite
-
25°C, pH 10.0, 20 mM buffer, mutant enzyme Y343F
8.59
sulfite
-
25°C, pH 8.0, 20 mM buffer, mutant enzyme Y343F
8.72
sulfite
-
25°C, pH 8.25, 100 mM buffer, mutant enzyme Y343F
9.08
sulfite
-
25°C, pH 8.25, 20 mM buffer, mutant enzyme Y343F
9.2
sulfite
-
25°C, pH 8.5, 100 mM buffer, mutant enzyme Y343F
9.24
sulfite
-
25°C, pH 8.5, 20 mM buffer, mutant enzyme Y343F
9.3
sulfite
-
mutant R472Q, 25°C, pH 8.0
9.4
sulfite
with ferricanide, pH 6.0, 25°C, recombinant mutant C242S/C253S/C260S/C451S
9.47
sulfite
-
25°C, pH 9.0, 20 mM buffer, mutant enzyme Y343F
9.63
sulfite
-
25°C, pH 9.5, 20 mM buffer, mutant enzyme Y343F
9.92
sulfite
-
25°C, pH 9.75, 20 mM buffer, mutant enzyme Y343F
9.99
sulfite
-
25°C, pH 9.0, 100 mM buffer, mutant enzyme Y343F
10.5
sulfite
-
25°C, pH 9.5, 100 mM buffer, mutant enzyme Y343F
11.4
sulfite
-
mutant V474M, 25°C, pH 7.0
12.1
sulfite
-
25°C, pH 7.0, 100 mM buffer, wild-type enzyme
12.4
sulfite
-
mutant V474M, 25°C, pH 10.0
12.8
sulfite
-
mutant Y343N, 25°C, pH 7.0
13
sulfite
-
mutant F79A, pH 8.0, 25°C
13
sulfite
-
wild-type, 25°C, pH 10.0
13.2
sulfite
-
25°C, pH 6.0, 20 mM buffer, wild-type enzyme
13.2
sulfite
-
wild type enzyme in 20 mM Tris at pH 6.0
13.2
sulfite
-
wild type enzyme, pH 6.0
13.2
sulfite
-
wild-type, 25°C, pH 6.0
13.75
sulfite
-
mutant Y343N, 25°C, pH 8.0
13.9
sulfite
with ferricanide, pH 6.0, 25°C, recombinant wild-type enzyme
14.1
sulfite
-
mutant R472D, pH 7.6, 25°C
15.1
sulfite
-
mutant enzyme G473A, pH 10.0
15.5
sulfite
-
mutant Y343N, 25°C, pH 9.0
15.8
sulfite
-
mutant V474M, 25°C, pH 8.5
15.9
sulfite
-
mutant enzyme G473A, pH 7.0
16
sulfite
-
mutant F57A, pH 8.0, 25°C
16.2
sulfite
with ferricanide, pH 7.1, 25°C, recombinant wild-type enzyme
16.9
sulfite
-
mutant Y343N, 25°C, pH 8.5
17.1
sulfite
-
mutant V474M, 25°C, pH 9.5
17.2
sulfite
-
25°C, pH 7.5, 100 mM buffer, wild-type enzyme
17.7
sulfite
-
25°C, pH 6.5, 20 mM buffer, wild-type enzyme
17.7
sulfite
-
wild type enzyme, pH 6.5
17.8
sulfite
-
mutant V474M, 25°C, pH 8.0
18.5
sulfite
-
mutant R472K, pH 7.6, 25°C
19
sulfite
-
mutant F57Y, pH 8.0, 25°C
19
sulfite
-
mutant H90F, pH 8.0, 25°C
19.6
sulfite
-
mutant V474M, 25°C, pH 9.0
19.8
sulfite
with ferricanide, pH 7.1, 25°C, recombinant mutant C242S/C253S/C260S/C451S
20.8
sulfite
with ferricanide, pH 7.1, 25°C, recombinant wild-type enzyme
21.6
sulfite
-
mutant enzyme G473A, pH 7.4
23
sulfite
-
mutant D342K, pH 7.6, 25°C
23.6
sulfite
-
25°C, pH 8.75, 20 mM buffer, wild-type enzyme
24.2
sulfite
-
25°C, pH 7.0, 20 mM buffer, wild-type enzyme
24.2
sulfite
-
wild-type, 25°C, pH 7.0
24.2
sulfite
-
wild type enzyme, pH 7.0
24.6
sulfite
-
25°C, pH 9.5, 100 mM buffer, wild-type enzyme
24.7
sulfite
-
wild type enzyme, pH 7.5
24.7
sulfite
-
25°C, pH 7.5, 20 mM buffer, wild-type enzyme
24.8
sulfite
-
25°C, pH 8.25, 20 mM buffer, wild-type enzyme
25
sulfite
-
25°C, pH 8.0, 100 mM buffer, wild-type enzyme
25.7
sulfite
-
25°C, pH 9.0, 20 mM buffer, wild-type enzyme
25.7
sulfite
-
wild type enzyme, pH 9.0
25.7
sulfite
-
wild-type, 25°C, pH 9.0
25.8
sulfite
with ferricanide, pH 8.4, 25°C, recombinant mutant C242S/C253S/C260S/C451S
25.9
sulfite
-
25°C, pH 8.0, 20 mM buffer, wild-type enzyme
25.9
sulfite
-
wild type enzyme, pH 8.0
25.9
sulfite
-
wild-type, 25°C, pH 8.0
26.1
sulfite
with ferricanide, pH 6.0, 25°C, recombinant selenomethionine-labeled mutant C242S/C253S/C260S/C451S
26.2
sulfite
-
mutant enzyme G473A, pH 8.0
26.3
sulfite
-
25°C, pH 9.5, 20 mM buffer, wild-type enzyme
26.3
sulfite
-
wild type enzyme, pH 9.5
26.3
sulfite
-
wild-type, 25°C, pH 9.5
26.6
sulfite
-
mutant R472Q, pH 7.6, 25°C
26.9
sulfite
-
wild type enzyme, pH 8.5
26.9
sulfite
-
wild-type, pH 8.0, 25°C
26.9
sulfite
-
25°C, pH 8.5, 100 mM buffer, wild-type enzyme
26.9
sulfite
-
25°C, pH 8.5, 20 mM buffer, wild-type enzyme
26.9
sulfite
-
wild type enzyme in 20 mM Tris at pH 8.5
26.9
sulfite
-
wild-type, 25°C, pH 8.5
27
sulfite
-
wild-type, pH 8.0, 25°C
27
sulfite
-
25°C, pH 8.25, 100 mM buffer, wild-type enzyme
27
sulfite
-
mutant R472M, pH 7.6, 25°C
27.3
sulfite
with ferricanide, pH 8.9, 25°C, recombinant wild-type enzyme
28.1
sulfite
-
25°C, pH 9.0, 100 mM buffer, wild-type enzyme
28.4
sulfite
-
mutant enzyme G473A in 20 mM Tris at pH 8.5
28.4
sulfite
-
mutant enzyme G473A, pH 8.5
31.8
sulfite
with ferricanide, pH 8.9, 25°C, recombinant selenomethionine-labeled mutant C242S/C253S/C260S/C451S
31.9
sulfite
-
mutant enzyme G473A, pH 9.1
32.4
sulfite
with ferricanide, pH 8.4, 25°C, recombinant wild-type enzyme
36.1
sulfite
wild-type, 25°C, pH 7.0
36.2
sulfite
with ferricanide, pH 8.9, 25°C, recombinant mutant C242S/C253S/C260S/C451S
37.7
sulfite
with ferricanide, pH 7.1, 25°C, recombinant selenomethionine-labeled mutant C242S/C253S/C260S/C451S
41.2
sulfite
with ferricanide, pH 8.4, 25°C, recombinant selenomethionine-labeled mutant C242S/C253S/C260S/C451S
42
sulfite
-
mutant H90Y, pH 8.0, 25°C
46.6
sulfite
with ferricanide, pH 7.1, 25°C, recombinant selenomethionine-labeled mutant C242S/C253S/C260S/C451S
47
sulfite
-
mutant R472D/D342K, pH 7.6, 25°C
73
sulfite
wild-type, 25°C, pH 8.5
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0.00047
sulfite
-
mutant Y343N/R472M, 25°C, pH 9.5
0.00067
sulfite
-
mutant Y343N/R472M/V474M, 25°C, pH 10.0
0.0013
sulfite
-
mutant Y343N/R472M, 25°C, pH 9.0
0.0033
sulfite
-
mutant Y343N/R472m, 25°C, pH 8.5
0.0047
sulfite
-
mutant Y343N/R472M/V474M, 25°C, pH 9.5
0.0049
sulfite
-
mutant Y343F/R472Q, 25°C, pH 10.0
0.0069
sulfite
-
mutant Y343N/R472m, 25°C, pH 8.0
0.008
sulfite
-
mutant Y343N/R472M, 25°C, pH 6.0
0.01
sulfite
-
mutant Y343N/R472M/V474M, 25°C, pH 9.0
0.0124
sulfite
-
mutant Y343F/R472Q, 25°C, pH 9.5
0.0244
sulfite
-
mutant Y343N/R472M, 25°C, pH 7.0
0.0279
sulfite
-
mutant Y343N/R472M/V474M, 25°C, pH 8.5
0.036
sulfite
-
mutant Y343N, 25°C, pH 10.0
0.069
sulfite
-
mutant Y343F/R472Q, 25°C, pH 9.0
0.0866
sulfite
-
mutant Y343N, 25°C, pH 9.5
0.167
sulfite
-
mutant Y343N/R472M/V474M, 25°C, pH 8.0
0.173
sulfite
-
mutant Y343N/R472M/V474M, 25°C, pH 6.0
0.214
sulfite
mutant Y322N/R450M, 25°C, pH 8.5
0.237
sulfite
-
mutant Y343N/R472M/V474M, 25°C, pH 7.0
0.316
sulfite
-
mutant Y343F/R472Q, 25°C, pH 8.5
0.632
sulfite
-
mutant Y343N, 25°C, pH 9.0
0.725
sulfite
-
mutant Y343F/R472Q, 25°C, pH 8.0
1.97
sulfite
-
mutant Y343F/R472Q, 25°C, pH 7.0
1.99
sulfite
-
mutant Y343N, 25°C, pH 8.5
2.35
sulfite
-
mutant Y343F/R472Q, 25°C, pH 6.0
3.33
sulfite
-
mutant Y343N, 25°C, pH 6.0
4.63
sulfite
-
mutant Y343N, 25°C, pH 8.0
8.6
sulfite
wild-type, 25°C, pH 7.0
11
sulfite
-
mutant R472D, pH 6.5, 25°C
13.5
sulfite
-
mutant Y343N, 25°C, pH 7.0
30.8
sulfite
-
mutant V474M, 25°C, pH 10.0
53.6
sulfite
-
mutant V474M, 25°C, pH 9.5
136
sulfite
-
mutant V474M, 25°C, pH 9.0
246
sulfite
-
wild-type, 25°C, pH 10.0
392
sulfite
-
wild-type, 25°C, pH 9.5
446
sulfite
-
mutant V474M, 25°C, pH 8.5
558
sulfite
-
mutant V474M, 25°C, pH 8.0
610
sulfite
-
mutant R472D, pH 7.6, 25°C
640
sulfite
-
mutant R472M, pH 7.6, 25°C
851
sulfite
-
mutant V474M, 25°C, pH 7.0
979
sulfite
with ferricanide, pH 6.0, 25°C, recombinant mutant C242S/C253S/C260S/C451S
1139
sulfite
with ferricanide, pH 6.0, 25°C, recombinant wild-type enzyme
1160
sulfite
-
wild-type, 25°C, pH 9.0
1200
sulfite
-
mutant R472Q, pH 7.6, 25°C
1257
sulfite
with ferricanide, pH 8.9, 25°C, recombinant mutant C242S/C253S/C260S/C451S
1300
sulfite
-
mutant V474M, 25°C, pH 6.0
1374
sulfite
with ferricanide, pH 6.0, 25°C, recombinant selenomethionine-labeled mutant C242S/C253S/C260S/C451S
1615
sulfite
with ferricanide, pH 8.9, 25°C, recombinant wild-type enzyme
1828
sulfite
with ferricanide, pH 8.9, 25°C, recombinant selenomethionine-labeled mutant C242S/C253S/C260S/C451S
1900
sulfite
-
mutant D342K, pH 7.6, 25°C
1952
sulfite
with ferricanide, pH 8.4, 25°C, recombinant wild-type enzyme
2000
sulfite
-
mutant R472D/D342K, pH 7.6, 25°C
2400
sulfite
-
wild-type, pH 8.0, 25°C
2411
sulfite
with ferricanide, pH 8.4, 25°C, recombinant mutant C242S/C253S/C260S/C451S
2822
sulfite
with ferricanide, pH 8.4, 25°C, recombinant selenomethionine-labeled mutant C242S/C253S/C260S/C451S
3194
sulfite
with ferricanide, pH 7.1, 25°C, recombinant mutant C242S/C253S/C260S/C451S
3260
sulfite
-
wild-type, 25°C, pH 8.5
4050
sulfite
with ferricanide, pH 7.1, 25°C, recombinant wild-type enzyme
4125
sulfite
with ferricanide, pH 7.1, 25°C, recombinant mutant C242S/C253S/C260S/C451S
4598
sulfite
with ferricanide, pH 7.1, 25°C, recombinant selenomethionine-labeled mutant C242S/C253S/C260S/C451S
4952
sulfite
with ferricanide, pH 7.1, 25°C, recombinant wild-type enzyme
5800
sulfite
-
mutant R472K, pH 7.6, 25°C
5899
sulfite
with ferricanide, pH 7.1, 25°C, recombinant selenomethionine-labeled mutant C242S/C253S/C260S/C451S
5950
sulfite
-
wild-type, 25°C, pH 8.0
8690
sulfite
wild-type, 25°C, pH 8.5
8900
sulfite
-
wild-type, 25°C, pH 7.0
10000
sulfite
-
wild-type, 25°C, pH 6.0
27000
sulfite
mutant Y322N/R450M, 25°C, pH 7.0
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malfunction
-
defects in the enzyme cause a severe infant disease leading to early death with no efficient or costeffective therapy in sight
malfunction
in humans, sulfite oxidase deficiency is one of the most accepted causes of sulfite hypersensitivity and toxicity. A congenital deficiency of sulfite oxidase can cause an excessive accumulation of sulfite and lead to early death in infancy (usually between 2 and 6 years of age), or in neonatal cases, neurological abnormalities, mental retardation, intractable seizures, and ocular lens dislocation. Molybdenum cofactor deficiency, which compromises sulfite oxidase activity, results in profound mental retardation, brain damage, microcephaly, and spasticity. It has also been suggested that hypoxic-ischemic encephalopathy is due to molybdenum cofactor deficiency
malfunction
R309H and K322R mutations are responsible for isolated sulfite oxidase deficiency
malfunction
silencing of ZmSO could lead to seed germination delay upon sulfite exposure, but not under normal conditions
malfunction
-
the imbalanced sulfite level resulting from sulfite oxidase impairment confers a metabolic shift towards elevated reduced S-compounds, namely sulfide, S-amino acids (S-AA), Co-A and acetyl-CoA, followed by non-S-AA, nitrogen and carbon metabolite enhancement, including polar lipids. Exposing mutant plants to dark-induced carbon starvation result in a higher degradation of S-compounds, total AA, carbohydrates, polar lipids and total RNA in the mutant plants. Significantly, a failure to balance the carbon backbones is evident in the mutants, indicated by an increase in tricarboxylic acid cycle (TCA) cycle intermediates, whereas a decrease is shown in stressed wild-type plants. Sulfite oxidase deficiency is not necessarily lethal, unless other sulfite network enzymes are down-regulated or the capacity of the sulfite network enzymes in sulfite detoxification is exceeded. Sulfite oxidase mutation affects carbon metabolism in normal and dark-stressed plants. Extended dark stress leads to enhanced degradation of organic nitrogen, elevated ammonium and preference for lower C/N ratio metabolites in the sulfite oxidase mutants as compared with the wild-type plants. Phenotype, detailed overview
malfunction
-
enzyme absence confers reduced biomass accumulation in Arabidopsis plants exposed to carbon starvation. Enzyme impairment leads to a reduced sulfur reduction pathway under sucrose depletion and reduced biomass accumulation in plants grown on excess carbon supply
malfunction
-
enzyme knockdown animals move less resulting from a reduced peristalsis efficacy
malfunction
-
impairment in enzyme activity results in enhanced water consumption
malfunction
-
impairment in enzyme activity results in enhanced water consumption
-
metabolism
the enzyme is involved in the sulfite pathway in plants, overview
metabolism
the enzyme is involved in the sulfite pathway in plants, overview
metabolism
the enzyme is involved in the sulfite pathway in plants, overview
metabolism
the enzyme is involved in the sulfite pathway in plants, overview
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
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
sulfite is detoxified in the liver and lung to sulfate by sulfite oxidase (SO), a molybdenum dependent mitochondrial enzyme. The enzyme ensures that intracellular levels of the sulfite ion remain at acceptably low levels. Sulfite oxidation is the final step in the metabolism of sulfur derived from sulfur containing amino acids. SO catalyzes the oxidation of endogenous or exogenous sulfite to sulfate, which is excreted in to the urine
physiological function
sulfite oxidase (SO) is an essential molybdoenzyme for humans, catalyzing the final step in the degradation of sulfur-containing amino acids and lipids, which is the oxidation of sulfite to sulfate
physiological function
-
sulfite oxidase activity is essential for normal sulfur, nitrogen and carbon metabolism in tomato leaves. The enzyme is a key player in protecting plants against exogenous toxic sulfite. And the enzyme activity is essential to cope with rising dark-induced endogenous sulfite levels in tomato plants. The role of sulfite oxidase is not limited to a rescue reaction under elevated sulfite, but sulfite oxidase is a key player in maintaining optimal carbon, nitrogen and sulfur metabolism in tomato plants
physiological function
sulfite oxidase detoxifies sulfite by oxidizing it to sulfate, which detoxifies sulfite by oxidizing it to sulfate. This reaction is the terminal step in the biological sulfur cycle in many organisms, including humans
physiological function
sulfite oxidase is a crucial molybdenum cofactor-containing enzyme in plants that re-oxidizes the sulfite back to sulfate in sulfite assimilation pathway
physiological function
sulfite oxidase is a crucial molybdenum cofactor-containing enzyme in plants that re-oxidizes the sulfite back to sulfate in sulfite assimilation pathway
physiological function
sulfite oxidase is a crucial molybdenum cofactor-containing enzyme in plants that re-oxidizes the sulfite back to sulfate in sulfite assimilation pathway
physiological function
sulfite oxidase is a crucial molybdenum cofactor-containing enzyme in plants that re-oxidizes the sulfite back to sulfate in sulfite assimilation pathway
physiological function
-
sulfite oxidase is a mitochondria-located molybdenum-containing enzyme catalyzing the oxidation of sulfite to sulfate in the amino acid and lipid metabolism. It plays a major role in detoxification processes. It catalyzes the oxidation of sulfite to sulfate using ferricytochrome c as the physiological electron acceptor. This reaction is biologically essential as the final step in the catabolism of sulfur-containing amino acids cysteine and methionine. SuOx functions in detoxifying exogenously supplied sulfite and sulfur dioxide (e.g., pollution, preservatives)
physiological function
sulfite oxidase plays an important role in sulfite metabolism by catalyzing the physiologically vital oxidation of sulfite to sulfate in plants. Sulfite oxidase is essential for timely germination of maize seeds upon sulfite exposure, seed germination is inhibited by sulfite. Embryonic sulfite oxidase might be essential for timely seed germination upon sulfite exposure in maize
physiological function
sulfite oxidase significantly contributes to hypoxic nitrite signaling as demonstrated by activation of the canonical NO-sGCcGMP pathway
physiological function
enzyme overexpression improves drought tolerance in tobacco. Enzyme-overexpressing transgenic plants show higher sulfate and glutathione (GSH) levels but lower hydrogen peroxide and malondialdehyde contents under drought stress, indicating that the enzyme confers drought tolerance by enhancing GSH-dependent antioxidant system that scavenges reactive oxygen species and reduces membrane injury. In addition, the transgenic plants exhibit more increased stomatal response than the wild type to water deficit
physiological function
-
the enzyme is specifically required for larval locomotion control in ensheathing glia to regulate head bending and peristalsis
physiological function
-
the enzyme plays an important role in sulfite homeostasis and stomatal closure
physiological function
the enzyme serves as an anti-viral factor through sequestering Turnip crinkle virus coat protein for binding with Argonaute 1 and confers virus resistance
physiological function
-
the role of the enzyme is not limited to protection against elevated sulfite toxicity but to maintaining optimal carbon and sulfur metabolism in Arabidopsis plants
physiological function
-
the enzyme plays an important role in sulfite homeostasis and stomatal closure
-
additional information
the catalytic site of SO consists of a molybdenum ion bound to the dithiolene sulfurs of one molybdopterin (MPT) molecule, carrying two oxygen ligands, and is further coordinated by the thiol sulfur of a conserved cysteine residue
additional information
-
the catalytic site of SO consists of a molybdenum ion bound to the dithiolene sulfurs of one molybdopterin (MPT) molecule, carrying two oxygen ligands, and is further coordinated by the thiol sulfur of a conserved cysteine residue
additional information
three-dimensional modeling and structure-based phylogeny
additional information
-
three-dimensional modeling and structure-based phylogeny
additional information
three-dimensional modeling and structure-based phylogeny
additional information
-
three-dimensional modeling and structure-based phylogeny
additional information
three-dimensional modeling and structure-based phylogeny
additional information
-
three-dimensional modeling and structure-based phylogeny
additional information
three-dimensional modeling and structure-based phylogeny. Analysis of the protein-protein interaction (PPI) network of AtSOX, overview
additional information
-
three-dimensional modeling and structure-based phylogeny. Analysis of the protein-protein interaction (PPI) network of AtSOX, overview
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D223A
the mutation abolishes infectivity of Turnip crinkle virus
C102S
-
different location compared to the wild type enzyme
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
C207S
-
C207 essential for enzyme activity, probably as ligand of Mo
C242S/C253S/C260S/C451S
site-directed mutagenesis, mutation of the four active site Cys residues
D342K
-
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
-
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
-
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
-
the size and hydrophobicity of F57 play an important role in modulating the heme potential, residue F57 also affects the intramolecular electron transfer rate
G473D/R212A
-
shows no intramolecular electron transfer rate
H304A R309H
site-directed mutagenesis, a mutation that removes the charge, hydrogen bonding, and is of smaller size, shows a decrease in Ksulfite m , thus binding sulfite more efficiently than the wild-type, kcat is increased compared to wild-type
H304R/R309H
site-directed mutagenesis, the mutant shows altered kinetics and reaction rates compared to the wild-type enzyme
H61Y/R160G
the mutations are associated with isolated sulfite oxidase deficiency
H90F
-
interactions of H90 with a heme propionate group destabilize the Fe(III) state of the heme
H90Y
-
interactions of H90 with a heme propionate group destabilize the Fe(III) state of the heme
K322R
site-directed mutagenesis, the mutant shows altered kinetics and reaction rates compared to the wild-type enzyme
R160K
-
the intramolecular electron transfer rate constant for the mutant enzyme is about one-fourth that of the wild-type enzyme
R212A/G473D
-
mutant is able to oligomerize but has undetectable activity, significant random-coil formation
R309E
site-directed mutagenesis, the mutant shows altered kinetics and reaction rates compared to the wild-type enzyme, mutant R309E, which shows the greatest increase in activity, also shows the greatest increase in Km
R309H
site-directed mutagenesis, the mutant shows altered kinetics and reaction rates compared to the wild-type enzyme, purified R309H mutant enzyme has substantially increased catalytic activity and a slightly less efficient Km sulfite compared to the wild-type enzyme
R472D
-
significant decrease in the intramolecular electron transfer rate constant, and the redox potentials of both metal centers are affected
R472D/D342K
-
mutation reverses the charges of the salt bridge components, large decrease in intramolecular electron transfer rate constant
R472K
-
40% increase in catalytic efficiency
V474M
-
active site mutant, kinetic analysis
Y343F/R472Q
-
active site mutant, kinetic analysis
Y343N
-
active site mutant, kinetic analysis
Y343N/R472M
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active site mutant, kinetic analysis
Y343N/R472M/V474M
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active site mutant, kinetic analysis
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
C207S
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C207 essential for enzyme activity
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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dimer
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
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
G473W
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monomer
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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sulfite-oxidase deficient patient
R160Q
site-directed mutagenesis, inactive mutant
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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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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clinical mutant, has a six-coordinate pseudooctahedral active site with coordination of glutamine Oepsilon to molybdenum
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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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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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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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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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
all of the mutants show decreased rates of intramolecular electron transfer (IET) but increased steady-state rates of catalysis, IET is not the rate determining step for any of the mutations. Redox potentials of wild-tyype and mutant enzymes, overview
additional information
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all of the mutants show decreased rates of intramolecular electron transfer (IET) but increased steady-state rates of catalysis, IET is not the rate determining step for any of the mutations. Redox potentials of wild-tyype and mutant enzymes, overview
additional information
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construction of surface functionalized MoO3 nanoparticles that exhibit an intrinsic biomimetic SuOx activity that allows intracellular oxidation of sulfite to sulfate. Functionalized with a customized bifunctional ligand containing dopamine as anchor group and triphenylphosphonium ion as targeting agent, they selectively target the mitochondria while being highly dispersible in aqueous solutions. Chemically induced sulfite oxidase knockdown cells treated with MoO3 nanoparticles recover their sulfite oxidase activity in vitro, which makes MoO3 nanoparticles a potential therapeutic for sulfite oxidase deficiency and opens new avenues for cost-effective therapies for gene-induced deficiencies. Molybdenum trioxide (MoO3) is a well-known model compound for selective oxidation catalysis. Given their small size and surface-targeting moiety triphenylphosphonium ion (TPP), functionalized MoO3-TPP nanoparticles can cross the cellular membrane and accumulate specifically at the mitochondria, allowing recovery of the SuOx activity of tungstate knockdown human HepG2 hepatoblastoma cells. Steady-state kinetics of MoO3-TPP nanoparticles, a 4fold activity difference between nanoscale and bulkMoO3 indicates the importance of a higher surface area for attaining higher catalytic efficiencies
additional information
mediated electrocatalytic voltammetry of human sulfite oxidase (HSO) is demonstrated with synthetic one electron transfer iron complexes bis(1,4,7-triazacyclononane)iron(III) ([Fe(tacn)2]3+) and 1,2-bis(1,4,7-triaza-1-cyclononyl)ethane iron(III) ([Fe(dtne)]3+) at a glassy carbon working electrode, enzyme-dependent kinetics, overview. The HSO coupled electrode is successfully used for the determination of sulfite concentration in white wine and beer samples, and the results validate with a standard spectrophotometric method
additional information
the specific replacement of the active site Cys207 with selenocysteine during protein expression in Escherichia coli. The sulfite oxidizing activity (kcat/KM) of SeSOMD4Ser is increased at least 1.5fold, and the pH optimum is shifted to a more acidic value compared to those of SOMD4Ser and SOMD4Cys(wt)
additional information
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the specific replacement of the active site Cys207 with selenocysteine during protein expression in Escherichia coli. The sulfite oxidizing activity (kcat/KM) of SeSOMD4Ser is increased at least 1.5fold, and the pH optimum is shifted to a more acidic value compared to those of SOMD4Ser and SOMD4Cys(wt)
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 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 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-deficient rats, exposure to sulfite has no effect on hippocampus antioxidant enzymes superoxidase dismutase, catalase, and glutathione peroxidase
additional information
unlike the null mutant atso-1, ZmSO-overexpressing transgenic Arabidopsis plants are tolerant to SO2 stress and can effectively rescue the susceptible phenotype of atso-1
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molecular biology
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molybdenum trioxide (MoO3) nanoparticles display an intrinsic biomimetic sulfite oxidase activity under physiological conditions, and, functionalized with a customized bifunctional ligand containing dopamine as anchor group and triphenylphosphonium ion as targeting agent, they selectively target the mitochondria while being highly dispersible in aqueous solutions. Chemically induced sulfite oxidase knockdown cells treated with MoO3 nanoparticles recover their sulfite oxidase activity in vitro, which makes MoO3 nanoparticles a potential therapeutic for sulfite oxidase deficiency and opens new avenues for cost-effective therapies for gene-induced deficiencies. Molybdenum trioxide (MoO3) is a well-known model compound for selective oxidation catalysis
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
agriculture
ZmSO might be a promising target for genetic improvement of crops tolerant to acid rain in molecular breeding programs. Sulfite oxidase is essential for timely germination of maize seeds upon sulfite exposure
analysis
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electroimmobilisation into polypyrrole film, use for amperometric detection of sulfite
analysis
an enzyme-coupled electrode is successfully used for the determination of sulfite concentration in white wine and beer samples, enzyme electrode preparation and method evaluation
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
food industry
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biosensor for detection of sulfite in food and beverages
food industry
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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
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
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
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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molybdenum trioxide (MoO3) nanoparticles display an intrinsic biomimetic sulfite oxidase activity under physiological conditions, and, functionalized with a customized bifunctional ligand containing dopamine as anchor group and triphenylphosphonium ion as targeting agent, they selectively target the mitochondria while being highly dispersible in aqueous solutions. Chemically induced sulfite oxidase knockdown cells treated with MoO3 nanoparticles recover their sulfite oxidase activity in vitro, which makes MoO3 nanoparticles a potential therapeutic for sulfite oxidase deficiency and opens new avenues for cost-effective therapies for gene-induced deficiencies. Molybdenum trioxide (MoO3) is a well-known model compound for selective oxidation catalysis
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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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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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
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
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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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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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