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Sulfite oxidase

sulfite oxidase, SUOX
Sulfite oxidase is a homodimeric protein localized to the intermembrane space of mitochondria. Each subunit contains a heme domain and a molybdopterin-binding domain. The enzyme catalyzes the oxidation of sulfite to sulfate, the final reaction in the oxidative degradation of the sulfur amino acids cysteine and methionine. Sulfite oxidase deficiency results in neurological abnormalities which are often fatal at an early age. Alternative splicing results in multiple transcript variants encoding identical proteins. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, CAN, HAD, STEP, oxidoreductase
Papers on sulfite oxidase
Sulfite Oxidase Activity of Cytochrome c: Role of Hydrogen Peroxide.
Zweier et al., Pittsburgh, United States. In Biochem Biophys Rep, Apr 2016
It also shows that the increased production of sulfite radical may be responsible for neurotoxicity and some of the injuries which occur to humans born with molybdenum cofactor and sulfite oxidase deficiencies.
[Sulfite oxidase activity deficiency caused by cofactor molybdenum deficiency: A case of early severe encephalopathy].
Patural et al., Saint-Étienne, France. In Arch Pediatr, Feb 2016
Among them, the catabolism anomaly of sulfite to sulfate caused by sulfite oxidase or cofactor molybdenum deficiency (MoCD) is a rare metabolic disorder in which neurological damage is similar to that found in neonatal asphyxia.
Molybdenum cofactor deficiency.
Scaglia et al., Houston, United States. In Mol Genet Metab, Jan 2016
MoCD results in deficiency of the molybdenum cofactor dependent enzymes sulfite oxidase, xanthine dehydrogenase, aldehyde oxidase and mitochondrial amidoxime reducing component.
Clinical and neuroimaging features as diagnostic guides in neonatal neurology diseases with cerebellar involvement.
Poretti et al., Baltimore, United States. In Cerebellum Ataxias, Dec 2015
In other disorders such as Krabbe disease or sulfite oxidase deficiency, the main abnormalities are found within the supratentorial brain, but the cerebellar involvement may be helpful for diagnostic purposes.
Globins Scavenge Sulfur Trioxide Anion Radical.
Gardner et al., Dayton, United States. In J Biol Chem, Dec 2015
Saccharomyces cerevisiae lacking sulfite oxidase and deleted of flavohemoglobin showed an O2-dependent growth impairment with nonfermentable substrates that was exacerbated by sulfide, a precursor to mitochondrial sulfite formation.
Effective Electrochemistry of Human Sulfite Oxidase Immobilized on Quantum-Dots-Modified Indium Tin Oxide Electrode.
Wollenberger et al., Potsdam, Germany. In Acs Appl Mater Interfaces, Oct 2015
The bioelectrocatalytic sulfite oxidation by human sulfite oxidase (hSO) on indium tin oxide (ITO) is reported, which is facilitated by functionalizing of the electrode surface with polyethylenimine (PEI)-entrapped CdS nanoparticles and enzyme.
Structural Insights into the Incorporation of the Mo Cofactor into Sulfite Oxidase from Site-Directed Spin Labeling.
Risse et al., Berlin, Germany. In Angew Chem Int Ed Engl, Oct 2015
This study addresses the question of how the Mo cofactor (Moco) is incorporated into the apo form of human sulfite oxidase (hSO) by using site-directed spin labeling to determine intramolecular distances in the nanometer range.
Hydrogen sulfide in pharmacology and medicine--An update.
Bełtowski, Lublin, Poland. In Pharmacol Rep, Jun 2015
H2S is enzymatically oxidized in mitochondria to thiosulfate and sulfate by specific enzymes, sulfide:quinone oxidoreductase, persulfide dioxygenase, rhodanese and sulfite oxidase.
Shifting the metallocentric molybdoenzyme paradigm: the importance of pyranopterin coordination.
Weiner et al., Edmonton, Canada. In J Biol Inorg Chem, Mar 2015
Enzyme families containing a single pyranopterin dithiolene chelate have been demonstrated to have reactivity towards two (sulfite oxidase, SUOX-fold) and five (xanthine dehydrogenase, XDH-fold) types of substrate, whereas the major family of enzymes containing a bis-pyranopterin dithiolene chelate (dimethylsulfoxide reductase, DMSOR-fold) is reactive towards eight types of substrate.
Local Hybrid QM/QM Calculations of Reaction Pathways in Metallobiosites.
Mata et al., Göttingen, Germany. In J Chem Theory Comput, 2015
We present calculations on two selected molybdenum complexes modeling the active sites of sulfite oxidase and dimethyl sulfoxide reductase.
Genetics of polycystic ovary syndrome.
Duran et al., Boston, United States. In Semin Reprod Med, 2014
The strongest loci in Europeans contain genes for DENND1A and THADA, with additional associations in loci containing the LHCGR and FSHR, YAP1 and RAB5/SUOX.
Structure-based alteration of substrate specificity and catalytic activity of sulfite oxidase from sulfite oxidation to nitrate reduction.
Rajagopalan et al., Durham, United States. In Biochemistry, 2012
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.
Characterization of chloride-depleted human sulfite oxidase by electron paramagnetic resonance spectroscopy: experimental evidence for the role of anions in product release.
Enemark et al., Tucson, United States. In Biochemistry, 2010
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
Effects of interdomain tether length and flexibility on the kinetics of intramolecular electron transfer in human sulfite oxidase.
Enemark et al., Tucson, United States. In Biochemistry, 2010
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.
Heavy metal ions inhibit molybdoenzyme activity by binding to the dithiolene moiety of molybdopterin in Escherichia coli.
Leimkühler et al., Potsdam, Germany. In Febs J, 2008
the activity of molybdoenzymes, such as sulfite oxidase, is inhibited by high concentrations of heavy metals in the cell
Structural studies of the molybdenum center of the pathogenic R160Q mutant of human sulfite oxidase by pulsed EPR spectroscopy and 17O and 33S labeling.
Enemark et al., Tucson, United States. In J Am Chem Soc, 2008
EPR study of the Mo(V) center of the pathogenic R160Q mutant confirms the presence of three distinct species whose relative abundances depend upon pH.
Molybdenum cofactor biosynthesis and molybdenum enzymes.
Mendel et al., Braunschweig, Germany. In Annu Rev Plant Biol, 2005
There are four Mo enzymes in plants: (1) nitrate reductase catalyzes the first and rate-limiting step in nitrate assimilation and is structurally similar to the recently identified, (2) peroxisomal sulfite oxidase that detoxifies excessive sulfite.
With the help of giants.
Fridovich, Durham, United States. In Annu Rev Biochem, 2002
The premier discoveries to emanate from my laboratory have been the sulfite oxidase, the several superoxide dismutases, the manganese catalase, and the catalase/peroxidase.
Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase.
Rees et al., Pasadena, United States. In Cell, 1998
The molybdenum-containing enzyme sulfite oxidase catalyzes the conversion of sulfite to sulfate, the terminal step in the oxidative degradation of cysteine and methionine.
Sulfite oxidase deficiency in man: demonstration of the enzymatic defect.
Laster et al., In Science, 1967
His liver, brain, and kidney specifically lacked sulfite oxidase activity.
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