EC Number   |
Reaction |
Reference |
|---|
    1.8.3.1 | 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 |
743226 |
| 1.8.3.1 | sulfite + O2 + H2O = sulfate + H2O2 |
electrocatalytic mechanism of HSO, overview |
742364 |
| 1.8.3.1 | sulfite + O2 + H2O = sulfate + H2O2 |
intramolecular electron transfer and effect of solution viscosity |
393033 |
| 1.8.3.1 | sulfite + O2 + H2O = sulfate + H2O2 |
kinetics and proposed mechanism |
393018, 393034 |
| 1.8.3.1 | sulfite + O2 + H2O = sulfate + H2O2 |
mechanism and kinetics of electron transfer |
393023, 393027, 393036 |
| 1.8.3.1 | sulfite + O2 + H2O = sulfate + H2O2 |
ping-pong mechanism |
393013, 393014 |
| 1.8.3.1 | 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 |
742912 |
| 1.8.3.1 | sulfite + O2 + H2O = sulfate + H2O2 |
this direct reduction of O2 is prevented completely in presence of cytochrome c |
393007 |
| 1.8.3.1 | sulfite + O2 + H2O = sulfate + H2O2 |
x-ray absorption spectroscopy of oxidation states |
393017 |
