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
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Reaction
Reaction on EC 1.8.3.1 - sulfite oxidase
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sulfite + O2 + H2O = sulfate + H2O2
this direct reduction of O2 is prevented completely in presence of cytochrome c
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sulfite + O2 + H2O = sulfate + H2O2
x-ray absorption spectroscopy of oxidation states
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sulfite + O2 + H2O = sulfate + H2O2
intramolecular electron transfer and effect of solution viscosity
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sulfite + O2 + H2O = sulfate + H2O2
mechanism and kinetics of electron transfer
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sulfite + O2 + H2O = sulfate + H2O2
mechanism and kinetics of electron transfer
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sulfite + O2 + H2O = sulfate + H2O2
catalytic cycle and electron transfer steps, and proposed oxidation state changes occurring at the Mo and Fe centers of one subunit of human sulfite oxidase during the catalytic oxidation of sulfite and the concomitant reduction of (cyt c)ox, overview
sulfite + O2 + H2O = sulfate + H2O2
electrocatalytic mechanism of HSO, overview
sulfite + O2 + H2O = sulfate + H2O2
quantum-mechanical study/quantum-mechanical cluster calculations of the reaction mechanism of sulfite oxidase using protonated and deprotonated substrates. The lowest barriers are obtained for a mechanism where the substrate attacks a Mo-bound oxo ligand, directly forming a Mo-bound sulfate complex, which then dissociates into the products. The activation energy is dominated by the Coulomb repulsion between the Mo complex and the substrate. The general catalytic cycle for sulfite oxidase includes the molybdenum ion refering to the molybdenum cofactor, and the iron ion refering to the heme, at the start of the catalytic cycle, Mo is in the oxidized +VI state and the heme group is in the Fe(III) state. Then SO3- binds and is oxidized to SO42-, while the Mo ion is reduced to the +IV state. To complete the catalytic cycle, the reduced Mo ion binds water and is reoxidized to the +VI state in two coupled one-electron/proton-transfer steps, proceeding via a transient Mo(V)-OH-state to form the active Mo(VI)=O form of the cofactor. The electrons are transferred via reduction of the heme, which subsequently is reoxidized by cytochrome c. Molecular mechanism of the oxo-atom transfer, modeling, detailed overview