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SUOX is negatively associated with the progression and proliferation of oral squamous cell carcinoma.
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This is the first description of the prenatal neurodevelopment of brain disruption in isolated sulfite oxidase deficiency.
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Novel SUOX mutations were detected in 3 Sulfite oxidase deficiency cases
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Nitrite binds and reduces at the molybdenum site of mammalian sulfite oxidase, which may be allosterically regulated by heme and molybdenum domain interactions, and contributes to the mammalian nitrate-nitrite-NO signaling pathway in human fibroblasts.
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This finding suggests the possibility to use oxygen-reactive SO variants in sulfite detoxification, as the loss of SO activity is causing severe neurodegeneration
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Several mutants of H304 and R309 of SUOX were investigated by steady-state kinetics, laser flash photolysis studies of intramolecular electron transfer (IET), and spectroelectrochemistry.
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SUOX was decreased and AKR1B10 and CD34 were increased with the stepwise progression of hepatocarcinogenesis.
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combined genetic association studies in women from China/Netherlands/United States: Data suggest that an SNP in SUOX locus (rs705702) and SNPs in other proteins are associated with polycystic ovary syndrome across ethnic differences. [META-ANALYSIS]
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effect of mutation of surface residues on the heme domain on intramolecular electron transfer, and steady-state kinetics
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In this study a human sulfite oxidase variant, in which the active site has been modified to alter substrate specificity and activity from sulfite oxidation to nitrate reduction, is compared to chicken sulfite oxidase.
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prepared and purified samples of the wild type and various mutants of human SO that are depleted of chloride. These samples do not exhibit the typical lpH EPR spectrum at low pH but rather exhibit spectra that are characteristic of the blocked species
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Experimental deletions of nonconserved amino acids in the 14-residue interdomain polypeptide tether of sulfite oxidase shorten its length and result in more drastically reduced intramolecular electron transfer rate constants.
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role of conserved tyrosine 343 in intramolecular electron transfer in this enzyme
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Sulfite oxidase gene expression in brain and in other tissues.
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comparison of this structure with other b(5)-type cytochromes reveals distinct structural features present in the sulfite oxidase b(5) domain which promote optimal electron transport between the Moco of sulfite oxidase and the heme of cytochrome c
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To further assess the role of Arg 160 in human SO, intramolecular electron transfer rates between the reduced heme and oxidized molybdenum centers in the wild type, R160Q, and R160K human SO forms were investigated by laser flash photolysis
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the Tyr(343) residue is important for both substrate binding and oxidation of sulfite by sulfite oxidase
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mutation in SUOX gene in sulfite oxidase deficiency
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mutations to charged residues at the equivalent sites most likely cause crucial global or localized structural changes, and expose an alternative docking site that may compete with the Mo domain for docking of the heme
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Analysis of recombinant G473D sulfite oxidase indicated that it is severely impaired both in the ability to bind sulfite and in catalysis, with a second-order rate constant 5 orders of magnitude lower than that of the wild type.
