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Literature summary extracted from

  • Ragg, R.; Natalio, F.; Tahir, M.N.; Janssen, H.; Kashyap, A.; Strand, D.; Strand, S.; Tremel, W.
    Molybdenum trioxide nanoparticles with intrinsic sulfite oxidase activity (2014), ACS nano, 8, 5182-5189 .
    View publication on PubMed

Application

EC Number Application Comment Organism
1.8.3.1 medicine 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 Homo sapiens
1.8.3.1 molecular biology 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 Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.8.3.1 additional information 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 Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.8.3.1 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 Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.8.3.1 additional information
-
 additional information Michaelis-Menten model Homo sapiens

Localization

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.3.1 Molybdenum in the molybdenum cofactor 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 the enzyme catalyzes the oxidation of sulfite to sulfate using ferricytochrome c as the physiological electron acceptor sulfate + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.8.3.1 Homo sapiens
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.8.3.1 Hep-G2 cell
-
 Homo sapiens
-
1.8.3.1 kidney
-
 Homo sapiens
-
1.8.3.1 liver
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.3.1 sulfite + O2 + H2O the enzyme catalyzes the oxidation of sulfite to sulfate using ferricytochrome c as the physiological electron acceptor Homo sapiens sulfate + H2O2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.8.3.1 SUOX
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.3.1 25
-
 assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.3.1 cytochrome c
-
 Homo sapiens
1.8.3.1 molybdenum cofactor
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
1.8.3.1 malfunction defects in the enzyme cause a severe infant disease leading to early death with no efficient or costeffective therapy in sight Homo sapiens
1.8.3.1 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) Homo sapiens