1.8.3.1: sulfite oxidase
This is an abbreviated version!
For detailed information about sulfite oxidase, go to the full flat file.
Word Map on EC 1.8.3.1
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1.8.3.1
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molybdenum
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sulfur
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xanthine
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heme
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thiosulfate
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moco
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epr
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seizures
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molybdopterin
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molybdoenzymes
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sulfur-containing
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tungsten
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molybdenum-containing
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pterin
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s-sulfocysteine
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soxs
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sulfurtransferase
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ectopia
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low-ph
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pyranopterins
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lentis
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dithiolene
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amidoxime
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eseem
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hyperfine
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food industry
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agriculture
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high-ph
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analysis
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oxidase-deficient
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medicine
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xanthinuria
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marc
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molecular biology
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encephalomalacia
- 1.8.3.1
- molybdenum
- sulfur
- xanthine
- heme
- thiosulfate
- moco
- epr
- seizures
- molybdopterin
-
molybdoenzymes
-
sulfur-containing
- tungsten
-
molybdenum-containing
- pterin
- s-sulfocysteine
- soxs
- sulfurtransferase
-
ectopia
-
low-ph
-
pyranopterins
- lentis
-
dithiolene
-
amidoxime
-
eseem
-
hyperfine
- food industry
- agriculture
-
high-ph
- analysis
-
oxidase-deficient
- medicine
-
xanthinuria
-
marc
- molecular biology
- encephalomalacia
Reaction
Synonyms
At-SO, AtSOX, CG7280, HSO, NIA, oxidase, sulfite, PSO, Shopper, SO, SorT, SOX, sulfite oxidase, sulfite oxidase homologue, sulfite: acceptor oxidoreductase, sulfite:acceptor oxidoreductase, sulfite:oxygen oxidoreductase, sulphite oxidase cytochrome b9, SUOX, YedY, YedYZ, ZmSO
ECTree
Advanced search results
Metals Ions
Metals Ions on EC 1.8.3.1 - sulfite oxidase
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Cl-
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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
Fe3+
Iron
Mo
Mo6+
Molybdenum
Sodium arsenate
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up to a concentration of 5 mM, up to 2fold activation
additional information
Mo
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coordination of sulfate to the Mo(V) center in the blocked form of sulfite oxidase
Mo
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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
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the wild-type enzyme is five-coordinate with approximately square-based pyramidal geometry
Mo
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the oxygen-atom transfer reactions involve the formation of the stable intermediate (MoO2HSO3)- through oxoanionic binding of HSO3- at the Mo center
Mo
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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
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molybdenum covalently bound to two sulfur atoms of a unique tricyclic pterin moiety referred to as molybdopterin, essential for dimerization of the enzyme
Molybdenum
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consists of a single molybdenum atom coordinated through the dithiolene group of a single molybdopterin molecule
Molybdenum
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sulfite oxidation occurs at the dioxomolybdenum center of the enzyme
Molybdenum
active site 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
Molybdenum
in the catalytic reaction, SO is active in its fully oxidized state (MoVI) in which molybdenum is coordinated by a cysteine thiolate, the dithiolene group of molybdopterin, and two terminal oxygen atoms
Molybdenum
recombinant enzyme contains 0.69 molecules of Mo per protein subunit
Molybdenum
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the addition of molybdenum to culture media at a concentration of 2.07 mM molybdate leads to a 4fold increase in activity
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
additional information
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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