1. The activity of rat liver microsomal sulphite oxidase (EC 1.8.3.1) was increased several-fold on aging of microsomes, on delipidation by extraction with acetone or on solubilization with deoxycholate, suggesting its existence in a cryptic state. 2. In rat liver most of the sulphite oxidase was present in the nuclear fraction and only a small portion in the microsomes. 3. Microsomal sulphite oxidase activity was low in the developing embryo and increased rapidly after birth.. ...
Five patients with a combined deficiency of xanthine dehydrogenase, sulphite oxidase and, possibly, also of aldehyde oxidase are described. This remarkable coincidence of three inborn errors of metabolism in a single individual was demonstrated to re
Essential protein with sulfite reductase activity required in assimilatory sulfate reduction pathway during both primary and secondary metabolism and thus involved in development and growth.
In this study, we provide, for the first time, an insight into the QSOX1 expression level in breast tumors and into its role in breast cancer cells and tumor development.. Even if the enzymatic function of QSOX1 is well described in the literature, its biological function is not clearly established. In fact, QSOX1 expression is differentially modulated in some cancers. It turns out that QSOX1 is overexpressed during the early stages of prostate cancer, and in pancreatic tumor cells [15-17]. However, it has also been shown that QSOX1 is down-regulated in an endothelial cancer cell model [18]. As such, we decided to investigate the QSOX1 expression in normal and cancerous human breast tissues.. Prior to our study, it was not previously reported where QSOX1 was expressed in breast tissues. IHC results showed that the protein was expressed in the endomembranous system in epithelial cells, but not in stroma cells and in adipocytes. Results were consistent with the fact that QSOX1 is a protein ...
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Flavin-linked sulfhydryl oxidase of the mitochondrial intermembrane space (IMS), oxidizes Mia40p as part of a disulfide relay system that promotes IMS retention of imported ...
QSOX1 antibody [N2C2], Internal (quiescin Q6 sulfhydryl oxidase 1) for WB. Anti-QSOX1 pAb (GTX104581) is tested in Human samples. 100% Ab-Assurance.
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Sulfite reductases, which belong to the oxidoreductase family, are found in archaea, bacteria, fungi, and plants.[5] They are grouped as either assimilatory or dissimilatory sulfite reductases depending on their function, their spectroscopic properties, and their catalytic properties. This enzyme participates in selenoamino acid metabolism and sulfur assimilation. It employs two covalently coupled cofactors - an iron sulfur cluster and a siroheme - which deliver electrons to the substrate via this coupling.[6]. The systematic name of this enzyme class is hydrogen-sulfide:acceptor oxidoreductase. Other names in common use include assimilatory sulfite reductase, assimilatory-type sulfite reductase, and hydrogen-sulfide:(acceptor) oxidoreductase.. ...
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A critical step in the biogeochemical cycle of sulfur on Earth is microbial sulfate reduction, yet organisms from relatively few lineages have been implicated in this process. Previous studies using functional marker genes have detected abundant, novel dissimilatory sulfite reductases (DsrAB) that could confer the capacity for microbial sulfite/sulfate reduction but were not affiliated with known organisms. Thus, the identity of a significant fraction of sulfate/sulfite-reducing microbes has remained elusive. Here we report the discovery of the capacity for sulfate/sulfite reduction in the genomes of organisms from thirteen bacterial and archaeal phyla, thereby more than doubling the number of microbial phyla associated with this process. Eight of the thirteen newly identified groups are candidate phyla that lack isolated representatives, a finding only possible given genomes from metagenomes. Organisms from Verrucomicrobia and two candidate phyla, Candidatus Rokubacteria and Candidatus ...
A critical step in the biogeochemical cycle of sulfur on Earth is microbial sulfate reduction, yet organisms from relatively few lineages have been implicated in this process. Previous studies using functional marker genes have detected abundant, novel dissimilatory sulfite reductases (DsrAB) that could confer the capacity for microbial sulfite/sulfate reduction but were not affiliated with known organisms. Thus, the identity of a significant fraction of sulfate/sulfite-reducing microbes has remained elusive. Here we report the discovery of the capacity for sulfate/sulfite reduction in the genomes of organisms from thirteen bacterial and archaeal phyla, thereby more than doubling the number of microbial phyla associated with this process. Eight of the thirteen newly identified groups are candidate phyla that lack isolated representatives, a finding only possible given genomes from metagenomes. Organisms from Verrucomicrobia and two candidate phyla, Candidatus Rokubacteria and Candidatus ...
Recently, Guenter Schwarz and colleagues published an elegant study in the Biochemical Journal (2019) 476, 1805-1815 which combines kinetic and spectroscopic studies with protein engineering to provide a mechanism for sulfite oxidase (SO)-catalyzed nitrite reduction that yields nitric oxide (NO). This work is noteworthy as it demonstrates that (i) for NO generation, both sulfite and nitrite must bind to the same molybdenum (Mo) center; (ii) upon sulfite reduction, Mo is reduced from +6 (MoVI) to +4 (MoIV) and MoIV reduces nitrite to NO yielding MoV; (iii) the heme moiety, linked to the Mo-center by an 11 amino acid residue tether, gets reduced by intramolecular electron transfer (IET) resulting in MoV being oxidized to MoVI; (iv) the reduced heme transfers its electron to a second nitrite molecule converting it to NO; (v) the authors demonstrate steady-state NO production in the presence of the natural electron acceptor cytochrome c; (vi) Finally, the authors use protein engineering to shorten ...
siroheme: the heme prosthetic group of the hemoprotein of E coli NADPH-sulfite reductase; reduces sulfite to sulfide or nitrite to ammonia; structure
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Oxidative stress can damage the active site cysteine of the antioxidant enzyme peroxiredoxin (Prx) to the sulfinic acid form, Prx-SO(2)(-). This modification leads to inactivation. Sulfiredoxin (Srx) utilizes a unique ATP-Mg(2+)-dependent mechanism to repair the Prx molecule. Using selective protein engineering that involves disulfide bond formation and site-directed mutagenesis, a mimic of the enzyme.substrate complex has been trapped. Here, we present the 2.1 A crystal structure of human Srx in complex with PrxI, ATP, and Mg(2+). The Cys(52) sulfinic acid moiety was substituted by mutating this residue to Asp, leading to a replacement of the sulfur atom with a carbon atom. Because the Srx reaction cannot occur, the structural changes in the Prx active site that lead to the attack on ATP may be visualized. The local unfolding of the helix containing C52D resulted in the packing of Phe(50) in PrxI within a hydrophobic pocket of Srx. Importantly, this structural rearrangement positioned one of ...
A sulfur cycle-based bioprocess for co-treatment of wet flue gas desulfurization (WFGD) wastes with freshwater sewage has been developed. In this process the removal of organic carbon is mainly associated with biological sulfate or sulfite reduction. Thiosulfate is a major intermediate during biological sulfate/sulfite reduction, and its reduction to sulfide is the rate-limiting step. In this stud ...
Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. May contribute to disulfide bond formation in a variety of secreted proteins (By similarity).
In the course of the reaction of EC 1.11.1.15, peroxiredoxin, its cysteine residue is alternately oxidized to the sulfenic acid, S-hydroxycysteine, and reduced back to cy
Abstract. An organodiselenide catalyzed the aerobic oxidation of thiols into disulfides in practical yields without any reagents/additives, base, and light source. The synthesized diselenide also catalyzes the reduction of hydrogen peroxide into water.. ...
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Sulfonamides are any amide of a sulfonic acid, i.e., RS(=O)2NR′2. Sulfinamides are amides of sulfinic acid and contain a sulfur-oxygen double bond and a sulfur-nitrogen single bond.
Properties : Sodium sulphite occurs as colorless, transparent crystals, odorless and having a cooling, saline, sulphurous taste. It is freely soluble in water ( ...
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Prof.Dr. ELİF EROĞLU BÜYÜKÖNER; Altunizade Hastanesi lokasyonunda Kardiyoloji bölümünde çalışmaktadır. Bilgi ve randevu için tıklayın.
Peroxiredoxins (Prxs) are peroxidases that catalyze the reduction of reactive oxygen species (ROS). The active site cysteine residue of members of the 2-Cys Prx subgroup (Prx I to IV) of Prxs is hyperoxidized to cysteine sulfinic acid (Cys-SO2) during catalysis with concomitant loss of peroxidase activity. Reactivation of the hyperoxidized Prx is catalyzed by sulfiredoxin (Srx). Ethanol consumption induces the accumulation of cytochrome P450 2E1 (CYP2E1), a major contributor to ethanol-induced ROS production in the liver. We now show that chronic ethanol feeding markedly increased the expression of Srx in the liver of mice in a largely Nrf2-dependent manner. Among Prx I to IV, only Prx I was found to be hyperoxidized in the liver of ethanol-fed wildtype mice, and the level of Prx I-SO2 increased to ≈30% to 50% of total Prx I in the liver of ethanol-fed Srx−/− mice. This result suggests that Prx I is the most active 2-Cys Prx in elimination of ROS from the liver of ethanol-fed mice and ...
TY - JOUR. T1 - Mechanism of L-leucyl-L-leucine methyl ester-mediated killing of cytotoxic lymphocytes. T2 - Dependence on a lysosomal thiol protease, dipeptidyl peptidase I, that is enriched in these cells. AU - Thiele, Dwain L. AU - Lipsky, Peter E.. PY - 1990. Y1 - 1990. N2 - Exposure of murine or human lymphocytes to L-leucyl-L-leucine methyl ester (Leu-Leu-OMe) results in selective killing of cytotoxic lymphocytes, whereas helper T cells and B cells remain functionally intact. Cytolytic lymphocytes incubated in the presence of toxic concentrations of Leu-Leu-OMe were found to contain membranolytic metabolites of the structure (Leu-Leu)n-OMe, where n ≥ 3. The sensitivity of cytotoxic lymphocytes to Leu-Leu-OMe was found to be dependent upon production of these metabolites by a lysosomal thiol protease, dipeptidyl peptidase I, which is present at far higher levels in cytotoxic lymphocytes than in cells without cytolytic potential or not of bone marrow origin. Thus, this granule enzyme is ...
According to the study, the first enzyme catalyzes the reaction, which adds two oxygen atoms to the first amino acid of the ERF protein. This first amino acid at the N-terminus (also known as amino terminus) of ERFs is cysteine. The Flashman lab proved that a plant cysteine oxidase (PCO) catalyzes this oxidation and that this oxidation occurs in a single step. So far, this PCO is the first discovered plant cysteine dioxygenase.. The oxidation of the cysteine to cysteine sulfinic acid tags the ERF protein for the attack by the second enzyme. The lab headed by Nico Dissmeyer identified the second enzyme as arginine transferase. The arginine transferase recognizes the cysteine sulfinic acid residue as its substrate and adds one arginine molecule to the N-terminus of the ERF protein.. Proteins with arginine at their N-terminus often have a extremely short life span because their N-terminus marks them for degradation. The proteasome related enzymes recognize the arginine at the end of the ERFs and ...
3UST: Crystal structure of Bombyx mori nucleopolyhedrovirus ORF75 reveals a pseudo-dimer of thiol oxidase domains with a putative substrate-binding pocket
A denaturing gradient gel electrophoresis (DGGE) method was developed to assess the diversity of dsrB (dissimilatory sulfite reductase beta-subunit)-genes in sulfate-reducing communities. For this purpose a PCR primer pair was optimized for the amplification of a similar to 350 bp dsrB gene fragment that after DGGE gel electrophoresis enabled us to discriminate between dsrB
Three methods Ive used with success are to: 1) design your primers with restriction sites. Make sure to add 4-6 extra bases so that restriction sites are not at the very end of the amplified product. This makes the cloning routine. 2) Ive made my own T-ended cloning vector using a protocol in the Red Book (Current Protocols in Molecular Biology). Basically, use any vector (one with color selection is a good choice) cut with a restriciton enzyme that leave a blunt cut (like EcoRV) and incubate with Taq Polymerase in the presense of dTTP only. This adds a T compatible with the A so often introduced on your PCR product. 3) Blunt the PCR product ends with something like T4 DNA polymerase and clone the resulting blunted product into a blunt-cut vector. Again, color selection can be helpful here. Hope this is helpful. Mike ,Im a PhD student working in microbial ecology. For quite some months Ive ,been trying to clone the dissimilatory sulfite reductase (dsr) gene from ,environmental samples. As ...
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Oxidative protein folding is mediated by a proteinaceous electron relay system, in which the concerted action of protein disulfide isomerase and Ero1 delivers the electrons from thiol groups to the final acceptor. Oxygen appears to be the final oxidant in aerobic living organisms, although the existence of alternative electron acceptors, e.g. fumarate or nitrate, cannot be excluded. Whilst the protein components of the system are well-known, less attention has been turned to the role of low molecular weight electron carriers in the process. The function of ascorbate, tocopherol and vitamin K has been raised recently. In vitro and in vivo evidence suggests that these redox-active compounds can contribute to the functioning of oxidative folding. This review focuses on the participation of small molecular weight redox compounds in oxidative protein folding.
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Preventive as well as therapeutic treatment to alleviate the symptoms of disturbed keratinization, consisting of the topical application of a solution, gel, lotion, cream, ointment, stick, powder or spray containing one or more cysteic acid compounds, is disclosed. The compounds include free acid, ammonium salt, amine salt, metal chelate and metallic salt forms of cysteic acid, cysteine sulfinic acid and homocysteic acid. The efficacious compositions may include the active ingredients present in a total amount of from 0.1 to 30 percent by weight. Topical application to affected areas has been found to achieve from a substantial to a complete remission of dry skin, keratoses, warts and palmar and plantar hyperkeratosis. Used as a hair dressing, the compositions have been found to give the hair excellent grooming and luster.
This article describes features of plant Srx that add a new dimension to our understanding of the versatility of this Srx. It is shown that Srx from plant has a dual chloroplast and mitochondrial localization, can reduce the inactive sulfinic form of atypical plant Prx IIF and human Prx V, and interacts with its targets Trxo and Prx IIF.. Srx and its target 2-Cys Prx have been localized specifically in the chloroplast from Arabidopsis (Baier and Dietz, 1997; Liu et al., 2006; Rey et al., 2007). However, (1) the conditional mitochondrial localization in mammalia in response to oxidative stress (Noh et al., 2009) and (2) the high probability of dual targeting to chloroplast and mitochondrion in pea predicted by our bioinformatic analysis, stimulated us to investigate the intracellular localization of Srx from pea and Arabidopsis in detail.. In this work, we have demonstrated by several lines of evidence that plant Srx, in addition to its known chloroplast function, has a mitochondrial ...
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