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Literature summary extracted from

  • Velayutham, M.; Hemann, C.F.; Cardounel, A.J.; Zweier, J.L.
    Sulfite oxidase activity of cytochrome c role of hydrogen peroxide (2016), Biochem. Biophys. Rep., 5, 96-104 .
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.3.1 mitochondrial intermembrane space
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 Homo sapiens 5758
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Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.3.1 Fe3+ ferric cytochrome c, Fe3+ cyt c Homo sapiens
1.8.3.1 Molybdenum
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 Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.3.1 sulfite + O2 + H2O Homo sapiens under normal physiological conditions, SO catalyzes the oxidation of sulfite to sulfate with cytochrome c (cyt c) as oxidizing substrate sulfate + H2O2
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Organism

EC Number Organism UniProt Comment Textmining
1.8.3.1 Homo sapiens P51687
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Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.8.3.1 liver
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 Homo sapiens
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1.8.3.1 lung
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 Homo sapiens
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.3.1 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 Homo sapiens ?
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 ?
1.8.3.1 sulfite + O2 + H2O under normal physiological conditions, SO catalyzes the oxidation of sulfite to sulfate with cytochrome c (cyt c) as oxidizing substrate Homo sapiens sulfate + H2O2
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 ?
1.8.3.1 sulfite + O2 + H2O usage of Fe3+ oxidized cytochrome c from horse heart Homo sapiens sulfate + H2O2
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 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.3.1 cytochrome c ferric cytochrome c, Fe3+ cyt c, cytochrome c is known to participate in mitochondrial respiration and has antioxidant and peroxidase activities. Fe3+ cyt c might have a role in the deleterious effects of sulfite in biological systems due to increased production of sulfite radical. Mammalian cytochrome c (cyt c) is a small, globular protein that exists in high concentrations in the inner membrane of mitochondria Homo sapiens
1.8.3.1 molybdenum cofactor
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 Homo sapiens

General Information

EC Number General Information Comment Organism
1.8.3.1 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 Homo sapiens
1.8.3.1 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 Homo sapiens