• Korean Journal of Materials Research
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• v.33 no.11
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• pp.447-457
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• 2023

Single-atom Pd clusters anchored on t-BaTiO₃ material was synthesized using hydrothermal and ultrasonic methods for the effective piezoelectric catalytic degradation of pollutants using vibration energy. XRD patterns of BaTiO₃ loaded with monoatomic Pd were obtained before and after calcining, and showed typical cubic-phase BTO. TEM and HAADF-STEM images indicated single-atom Pd clusters were successfully introduced into the BaTiO₃. The piezoelectric current density of the prepared Pd-BaTiO₃ binary composite was significantly higher than that of the pristine BaTiO₃. Under mechanical vibration, the nanomaterial exhibited a tetracycline decomposition rate of ~95 % within 7 h, which is much higher than the degradation rate of 56.7 % observed with pure BaTiO₃. Many of the piezo-induced electrons escaped to the Pd-doped BaTiO₃ interface because of Pd's excellent conductivity. Single-atom Pd clusters help promote the separation of the piezo-induced electrons, thereby achieving synergistic catalysis. This work demonstrates the feasibility of combining ultrasonic technology with the piezoelectric effect and provides a promising strategy for the development of ultrasonic and piezoelectric materials.

• Journal of the Microelectronics and Packaging Society
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• v.30 no.4
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• pp.17-31
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• 2023

Amidst escalating global warming fueled by indiscriminate fossil fuel consumption, concerted efforts are underway worldwide to mitigate atmospheric carbon dioxide (CO₂) levels. Electrochemical CO₂ reduction technology is recognized as a promising and environmentally friendly approach to convert CO₂ into valuable hydrocarbon compounds, deemed essential for achieving carbon neutrality. Copper, among the various materials used as CO₂ reduction electrodes, is known as the sole metal capable of generating C₂₊ compounds. However, low conversion efficiency and selectivity have hindered its widespread commercialization. This review highlights diverse research endeavors to address these challenges. It explores various studies focused on utilizing copper-based electrodes for CO₂ reduction, offering insights into potential solutions for advancing this crucial technology.

• The Korean Journal of Zoology
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• v.39 no.1
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• pp.36-46
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• 1996

An endogenous phenoloxidase (EPO) from earthworm, Lumbricus rubellus, has been purified and characterized. The purified EPO using ammonium sulfate fractionation, Blue-2, Phenyl-, and Q-sepharose chromatography steps was revealed in SDS-PAGE as a single protein banri with Mr. of 59 kl)a. A native strudure of the enzyme was examined with an in situ staining of a nondenatudng-PAGE using DL-dopa as a substrate. The result showed that a single band due to the EPO activity was located siighdy above a standard polypeptide with Mr. of 210 kl)a. These fads indicate that the EPO is an oligomeric enzyme. The presence of a monophenolase activity of the purified EPO, which hydroxylates tyrosine to dopa, was confirmed by observing dopachrome accumulation at 475 nm at PH 8.0 with a typical lag phase during 60 mm. of meausrement. A series of inhibition study has been performed for the enzyme with several divalent cation chelators such as phenyithiourea (Flu), 1, lO-phenanthroline, EDTA, and EGTA. Among them, only V'flj inhibited the enzyme with 1C0.5 of 65 MM, which indicated that copper was critical for the catalysis of EPO. The enzyme was maximally active at 35'C and pH 8.0 when L-dopa to dopachrome conversion was spectrophotometricaily monitored at 475 nm. The apparent Km values of P0 for L-opa were obtained as 1.86 mM and 13.8 mM at pH 6.5 and 8.0, respectively. The catalytic efficiencies at both pH were almost identical [(kat/Km)pH8.0/(kcat/Km)pH6.5 = O.92] while the Vmax at p11 8.0 was 6.6-fold higher than that at pH 6.5. This fact may indicate that pH affeds the catalysis at substrate and/or enzyme-substrate complex level rather than the enzyme itself. Taken together, the EPO was an oligomeric enzyme which did not require proteolysis for its activation. These results also indicated that the enzyme can exist, at least, in part as a latent form In vivo, which might be distinct from the prophenoloxidase activating system. Therefore, it is pertinent to consider that there must be certain regulatory molecules or phenomena in L. rubellus which make the 1,0 in a latent form in vivo before the foreign invasions.

• Applied Chemistry for Engineering
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• v.8 no.5
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• pp.777-783
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• 1997

$TiO_2$ powders were synthesized via hydrolysis reaction of titanium n-propoxide in n-propanol solvent and the reaction rates were studied by use of UV-vis spectroscopic method. Concentration of water, reaction temperature, reaction time and acid-base effects of the solution were investigated to determine the optimum conditions for $TiO_2$ powder synthesis. The reaction were controlled to proceed to pseudo-first orders reaction in the presence of excess water in n-propanol solvent. The rate constants which varied with temperature and concentration of water were calculated by Guggenheim method. Reaction using $D_2O$ was also carried out to determine the catalytic character of water. $TiO_2$ powders were synthesized only in the neutral and basic solution and those were almost spheric forms having average particle size of $0.4-0.7{\mu}m$ diameter. Particle size decreased with increasing concentration of water and reaction temperature, however, increased with increasing reaction time. Associative $S_N2$ mechanism for the hydrolysis was proposed from the data of n-value in the transition state and thermodynamic parameter. $D_2O$ solvent isotope effect showed that $H_2O$ molecules reacted as nucleophilic catalysis.

• Journal of Korean Society of Environmental Engineers
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• v.28 no.9
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• pp.955-960
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• 2006

Catalytic decomposition over HZSM-5 was carried out in semi-batch reactor to recover gasoline from waste plastics(HDPE). To enhance the liquid yield with a molecule range of gasoline, the properties of catalytic decomposition were investigated over a commercial Si/ZSM-5 catalyst and HZSM-5 catalysts modified with P and Mg. Optimum loadings of P and Mg on HZSM-5 were 0.5 wt% and 2.0 wt%, respectively, based on conversion and liquid yield. $NH_3-TPD$ profile indicated that strong and weak acid sites totally decreased in P loading on HZSM-5 catalyst, strong acid sites moderately decreased and weak acid sites sharply reduced in Mg loading on HZSM-5 catalyst. In the case of Si/ZSM-5 catalyst, all acid sites almost disappeared, subsequently, catalytic decomposition significantly decreased, and little liquid product was produced. When HZSM-5 catalyst was modified with P and Mg, the carbon distribution of liquid product was shifted to lower carbon number and its all components was within a molecular range of gasoline($C_5-C_{11}$). Especially, over Mg(2.0 wt%)/ZSM-5 catalyst, 55.8% of liquid yield with 100% of a molecular range of gasoline, was obtained at $400^{\circ}C$, suggesting it as a promising catalyst for recycle of waste plastics.

• Journal of Life Science
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• v.19 no.2
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• pp.228-233
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• 2009

The purpose of this study is to evaluate the activities of five different antioxidant enzymes in various tissues of Papilio xuthus during pupal stage. Superoxide dismutase (SOD) activity in haemolymph was the highest just after pupation and then decreased gradually until 7 days after pupation but the activity in other tissue was constant during metamorphosis. This result indicates that primary antioxidant process of reactive oxygen species proceed in haemolymph. Catalase (CAT) activity in studied tissues was also the highest just after pupation and its relative activity was also high during pupal stage, suggesting that CAT is the primary enzyme in catalysis of hydrogen peroxide. Glutathion peroxidase (GPX) activity was constant and its relative activity was very low in all tested tissues. Glutathione S-transferase (GST) activity in haemolymph was high at 3 days and 5 days after pupation, and the activity in fat body was the highest at the 1 day after pupation and then decreased gradually for 7 days after pupation. Glutathion reductase (GR) activity in haemolymph and fat body was high at 1 day after pupation, but relatively low GR activity was detected in the rest tissues. Based on these results, GST activity was higher than that of GPX and GR, and it is also believed that GST was more involved in reduction process through lipid peroxidation than GPX.

• Journal of Life Science
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• v.20 no.12
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• pp.1777-1783
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• 2010

Plants generate reactive oxygen species (ROS) as a by-product of normal aerobic metabolism or when exposed to a variety of stress conditions, which can cause widespread damage to biological macromolecules. To protect themselves from oxidative stress, plant cells are equipped with a wide range of antioxidant proteins. However, the detailed reaction mechanisms of these are still unknown. Peroxiredoxins (Prxs) are ubiquitous thiol-containing antioxidants that reduce hydrogen peroxide with an N-terminal cysteine. The active-site cysteine of peroxiredoxins is selectively oxidized to cysteine sulfinic acid during catalysis, which leads to inactivation of peroxidase activity. This oxidation was thought to be irreversible. Recently identified small protein sulphiredoxin (Srx1), which is conserved in higher eukaryotes, reduces cysteine.sulphinic acid in yeast peroxiredoxin. Srx1 is highly induced by $H_2O_2$-treatment and the deletion of its gene causes decreased yeast tolerance to $H_2O_2$, which suggest its involvement in the metabolism of oxidants. Moreover, Srx1 is required for heat shock and oxidative stress induced functional, as well as conformational switch of yeast cytosolic peroxiredoxins. This change enhances protein stability and peroxidase activity, indicating that Srx1 plays a crucial role in peroxiredoxin stability and its regulation mechanism. Thus, the understanding of the molecular basis of Srx1 and its regulation is critical for revealing the mechanism of peroxiredoxin action. We postulate here that Srx1 is involved in dealing with oxidative stress via controlling peroxiredoxin recycling in Arabidopsis. This review article thus will be describing the functions of Prxs and Srx in Arabidopsis thaliana. There will be a special focus on the possible role of Srx1 in interacting with and reducing hyperoxidized Cys-sulphenic acid of Prxs.

• Korean Journal of Materials Research
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• v.11 no.7
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• pp.603-608
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• 2001

$MO-SiO_2$ (M = Zn, Sn, In, Ag, Ni) binary silica gels were synthesized by sol-gel method and their structural change with the kind of metal ions was characterized by XRD, FT- IR and $^{29}$Si-NMR. Although X-ray analysis showed partial recrystallization of $AgNO_3$ in $Ag-SiO_2$gel, crystalline phase formed by the bonding between metal ion and the silica matrix didn't appear in all $MO-SiO_2$ gels. The FT-IR analysis showed that Zn, Sn and in partially formed Si-O-M bonding in silica matrix and made an shift of absorption peak to by Si-O-Si symmetrical vibration. In addition, $^{29}Si-NMR$ studies showed that Zn, Sn and In didn't affect sol-gel process of silica and were linked with non-bridging oxygen of the linear silica structure, which formed imperfect network because of low temperature sol-gel process. Ag and Ni make a role of catalysis on sol-gel process, resulting in densifying the silica network structure.

• Journal of Microbiology and Biotechnology
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• v.14 no.5
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• pp.1075-1080
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• 2004

Dextransucrase (DSRB742) from Leuconostoc mesenteroides NRRL B-742CB is a glucosyltransferase that catalyzes the synthesis of dextran using sucrose, or the synthesis of oligosaccharides when acceptor molecules, like maltose, are present. The DSRB742 gene (dsrB742) was cloned and the properties were characterized. In order to identify critical amino acid residues, the DSRB742 amino acid sequence was aligned with glucosyltransferase sequences, and three amino acid residues reported as sucrose binding amino acids in Streptococcus glucosyltransferases were selected for site-directed mutagenesis experiments. Asp-533, Asp-536, and His-643 were independently replaced with Ala or Asn. D533A and D536A dextransucrases showed reduced dextran synthesis activities, 2.3% and 40.8% of DSRB742 dextransucrase, respectively, and D533N, D536N, H643A, end H643N dextransucrases showed complete suppression of dextran synthesis activities altogether. Additionally, D536N dextransucrase showed complete suppression of oligosaccharide synthesis activities. However, modifications at Asp-533 or at His-643 retained acceptor reaction activities in the range of 8.4% to 21.3% of DSRB742 acceptor reaction activity. Thus at least two carboxyl groups of Asp-533 and Asp-536, and His-643 as a proton donor, are essential for the catalysis process.

• Applied Biological Chemistry
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• v.48 no.3
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• pp.189-200
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• 2005

Biological nitrogen fixation is an important process for academic and industrial aspects. This review will briefly compare industrial and biological nitrogen fixation and cover the characteristics of biological nitrogen fixation studied in Azotobacter vinelandii. Various organisms can carry out biological nitrogen fixation and recently the researches on the reaction mechanism were concentrated on the free-living microorganism, A. vinelandii. Nitrogen fixation, which transforms atmospheric $N_2$ into ammonia, is chemically a reduction reaction requiring electron donation. Nitrogenase, the biological nitrgen fixer, accepts electrons from biological electron donors, and transfers them to the active site, FeMo-cofactor, through $Fe_4S_4$ cluster in Fe protein and P-cluster in MoFe protein. The electron transport and the proton transport are very important processes in the nitrogenase catalysis to understand its reaction mechanism, and the interactions between FeMo-cofactor and nitrogen molecule are at the center of biological nitrogen fixation mechanism. Spectroscopic studies including protein X-ray crystallography, EPR and $M{\ddot{o}}ssbauer$, biochemical approaches including substrate and inhibitor interactions as well as site-directed mutation study, and chemical approach to synthesize the FeMo-cofactor model compounds were used for biological nitrogen fixation study. Recent research results from these area were presented, and finally, a new nitrogenase reaction mechanism will be proposed based on the various research results.