• Journal of the Korean Chemical Society
• /
• v.39 no.12
• /
• pp.932-939
• /
• 1995

Rates of the decomposition of hydrogen peroxide by copper(Ⅱ)-Schiff base complexes were measured at various concentrations of hydrogen peroxide. Decomposition rates of hydrogen peroxide increased with increasing pH for CuⅡBSDT and CuⅡBSTP but then decreased with the same variation of the pH for CuⅡBSTT. A possible mechanism in accord with experimental results was proposed. The mechanism involves the deprotonation of copper(Ⅱ)-Schiff base complexes of hydrogen peroxide, followed by the formation of peroxo complexes at the rate-determining step.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.32 no.3
• /
• pp.444-449
• /
• 2003

To investigate the long term effect of buchu (Chinese chives) diet on ROS formation in the liver and stin tissue of ICR mice, one of control, 2% or 5% buchu-added diet was fed to ICR mice for 12 months. Superoxide anion (O2ㆍ), hydrogen peroxide($H_2O$$_2$) and hydroxyl radical (ㆍOH) contents were measured in cytosol, microsome, mitochondria of liver and skin of mice, respectively. Behu diet showed a significant decrease of superoxide anion, hydrogen peroxide and hydroxyl radical contents in liver and skin tissues compared to control diet, and this effect is especially higer at 5% than at 2% buchu diet level. ICR mice showed an age-dependent increase in ROS contents, while the group fed buchu diet decreased its ROS contents significantly and ROS contents of liver appeared to be 2 fold higher than skin. The results of the present study suggest that antioxidative components and sulfur-compounds in buchu diet appear to be responsible for the inhibition of ROS formation in ICR mice.

• BMB Reports
• /
• v.36 no.5
• /
• pp.488-492
• /
• 2003

Neurofilament-L (NF-L) is a major element of neuronal cytoskeletons and known to be important for neuronal survival in vivo. Since oxidative stress might play a critical role in the pathogenesis of neurodegenerative diseases, we investigated the role of copper and peroxide in the modification of NF-L. When disassembled NF-L was incubated with copper ion and hydrogen peroxide, then the aggregation of protein was proportional to copper and hydrogen peroxide concentrations. Dityrosine crosslink formation was obtained in copper-mediated NF-L aggregates. The copper-mediated modification of NF-L was significantly inhibited by thiol antioxidants, N-acetylcysteine, glutathione, and thiourea. A thioflavin-T binding assay was performed to determine whether the copper/$H_2O_2$ system-induced in vitro aggregation of NF-L displays amyloid-like characteristics. The aggregate of NF-L displayed thioflavin T reactivity, which was reminiscent of amyloid. This study suggests that copper-mediated NF-L modification might be closely related to oxidative reactions which may play a critical role in neurodegenerative diseases.

• Bulletin of the Korean Chemical Society
• /
• v.35 no.2
• /
• pp.431-435
• /
• 2014

Zinc peroxide nanoparticles ($ZnO_2$ NPs) were prepared by reacting zinc(II) isobutylcarbamate, as an organometallic precursor, with hydrogen peroxide ($H_2O_2$) at $60^{\circ}C$. Polyethylene glycol and polyvinylpyrrolidone were used as stabilizers, which suppressed aggregation of the $ZnO_2$ NPs. Conditions such as concentrations of $H_2O_2$ and the stabilizer were systemically controlled to determine their effect on the formation of nano-sized $ZnO_2$ NPs. The formation of stable $ZnO_2$ NPs was confirmed by UV-vis, Raman spectroscopy, X-ray photoelectron spectroscopy, transmission electron microscopy (TEM), scanning electron microscopy (SEM), and X-ray diffraction. The TEM images revealed that polyvinylpyrrolidone-stabilized $ZnO_2$ NPs (diameter, 10-30 nm) were well dispersed in the organic solvent. Quite pure ZnO NPs were obtained from the peroxide powder by simple heat treatment of $ZnO_2$. The transition temperature of $170^{\circ}C$ was determined by differential scanning calorimetry.

• Bulletin of the Korean Chemical Society
• /
• v.22 no.4
• /
• pp.362-366
• /
• 2001

To show the effects of metallothionein (MT) on the activity of enzymes involved in the removal of reactive oxygen species, MT has been added to the assay systems of superoxide dismutase (SOD), catalase and peroxidase. We have used assay systems of SOD based on NADPH oxidation and nitrite formation from hydroxylammonium chloride as an assay of superoxide breakdown rate. The two assay systems showed different results at the high concentration of MT. MT showed the scavenging of superoxide in the SOD assay system in the presence and absence of SOD. MT added to the SOD assay system behaved as an activator of SOD, but apo-MT behaved as an inhibitor. When MT was added to the assay system in the presence of a fixed amount of SOD, the breakdown rate of superoxide increased. The effects of MT on the decomposition of hydrogen peroxide and the activity of catalase and peroxidase decomposing hydrogen peroxide were evaluated. MT decreased the activities of catalase and peroxidase. We have concluded that the function of MT as an antioxidant might effect the level of superoxide scavenging and not the level of hydrogen peroxide.

• Proceedings of the Zoological Society Korea Conference
• /
• 1998.10b
• /
• pp.164.1-164
• /
• 1998

No Abstract, See Full Text

• BMB Reports
• /
• v.31 no.4
• /
• pp.307-327
• /
• 1998

Cytochrome c peroxidase (CcP) is a yeast mitochondrial enzyme which catalyzes the reduction of hydrogen peroxide to water using two equivalents of ferrocytochrome c. The CcP/cytochrome c system has many features which make it a very useful model for detailed investigation of heme protein structure/function relationships including activation of hydrogen peroxide, protein-protein interactions, and long-range electron transfer. Both CcP and cytochrome c are single heme, single subunit proteins of modest size. High-resolution crystallographic structures of both proteins, of one-to-one complexes of the two proteins, and a number of active-site mutants are available. Site-directed mutagenesis studies indicate that the distal histidine in CcP is primarily responsible for rapid utilization of hydrogen peroxide implying significantly different properties of the distal histidine in the peroxidases compared to the globins. CcP and cytochrome c bind to form a dynamic one-to-one complex. The binding is largely electrostatic in nature with a small, unfavorable enthalpy of binding and a large positive entropy change upon complex formation. The cytochrome c-binding site on CcP has been mapped in solution by measuring the binding affinities between cytochrome c and a number of CcP surface mutations. The binding site for cytochrome c in solution is consistent with the crystallographic structure of the one-to-one complex. Evidence for the involvement of a second, low-affinity cytochrome c-binding site on CcP in long-range electron transfer between the two proteins is reviewed.

• Proceedings of the Korea Technical Association of the Pulp and Paper Industry Conference
• /
• 1999.04a
• /
• pp.84-88
• /
• 1999

In chlorine dioxide delignigication or bleaching, chlorate is mainly formed by the reaction between chlorite and hypochlorous acid, thus scavengers of chlorine or hypochlorous acid can be used to reduce the formation of chlorate which is unfavorable to environment. In this study, additives such as sulfamic acid, DMSO, hydrogen peroxide, or sodium chlorite was added to chlorine solution or pure $ClO_2$ solution to check their reactivity with $Cl_2$ and $ClO_2$. These additives were also added directly into general $ClO_2$ solution which contained certain amount of chlorine, then the additive-treated $ClO_2$ solution were used in bleaching stages. The aim of this procedure was to remove the original amount of chlorine that was thought to be possibly the main reason for the formation of chlorate and AOX. The additives were found to be able to eliminate chlorine very fast and selectively, but $H_2$ $O_2$ should be used under pH4, otherwise it also reacts with $ClO_2$. After the additives reacted With $Cl_2$, DMSO turned into an inactive product $(CH_3)_2SO_2$, While Sulfamic acid turned into $HClSO_3H$ that still remained active in oxidation, and $NaClO_2$ produced $ClO_2$. The addition of $HNaClO_2$ showed significant improvement in delignification but the deeper delignification led to higher formation of chlorate. When the additive-treated chlorine dioxide solutions were used in bleaching, both sulfamic acid, DMSO, and hydrogen peroxide showed no significant changes of DE brightness and Kappa number. The formation of chlorate was reduced by addition of sulfamic acid, DMSO and hydrogen peroxide.

• Journal of the Korean Chemical Society
• /
• v.4 no.1
• /
• pp.10-12
• /
• 1957

On the performance of the hydrogen peroxide method for Th-determination we encountered some difficulties, namely the formation of the insoluble matter occured in the nearly neutral solution after evaporation. We carried out the Th-determination in the mixture of the Th and some kind of the rare earth, and found that the insoluble matter was not formed in case of the mixture of Th and some kind of rare earth, but formed in case of Monazite. The formation of the insoluble matter in the case of Monazite sand, however, could be avoid by using the beaker instead of the evaporating dish and by adding the water repeatedly before it was completely evaporated to dryness.

• Herbal Formula Science
• /
• v.29 no.1
• /
• pp.1-8
• /
• 2021

Objectives : The purpose of this study was to investigate the antioxidant activity of water extract of Ojayeonjonghwan (OYH) in GC-1 germ cell lines. Methods : DPPH radical scavenging activity and cell viability assays in GC-1 germ cell lines were performed. In addition, the protective effects of OYH against hydrogen peroxide-induced oxidative stress in GC-1 germ cell lines were examined by measuring cell viability after H2O2 treatmet. The formation of ROS and the antioxidant enzymes activity such as SOD and catalase were measured in the same condition. Results : OYH scavenged DPPH radical dose-dependent manner and the IC50 was 63.79 ㎍/ml. OYH showed no cytotoxicity at concentration of 1, 10, 100 ㎍/ml. The hydrogen peroxide-induced cytotoxicity of GC-1 germ cell lines was protected to 53.66% by OYH at concentration of 10 ㎍/ml. OYH effectively inhibited ROS production in GC-1 germ cell lines. Mn SOD and catalase protein expression were significantly increased in GC-1 germ cell lines, but Cu/Zn SOD protein expression was not significantly changed. Conclusions : In conclusion, OYH has antioxidant activities against hydrogen peroxide-induced oxidative stress in GC-1 germ cell lines.