• Applied Biological Chemistry
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• v.41 no.8
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• pp.611-612
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• 1998

The transition state analog for metal catalyzed hydrolysis of an ester through cooperative interactions between metal ions as Lewis acid and peroxide was discussed.

• Journal of the Korean Chemical Society
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• v.68 no.3
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• pp.139-145
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• 2024

This study aims to elucidate the mechanism involved in the hydrolysis of the hexacyanoferrate(III) complex ion (Fe(CN)₆^3-) and the mechanism leading to the formation of Prussian blue (Fe^III₄[Fe_II(CN)₆]₃·xH₂O, PB) in acidic aqueous solutions at moderately elevated temperatures. Hydrolysis constitutes a crucial step in generating PB through the widely used single-source or precursor method. Recent PB syntheses predominantly rely on the single-source method, where hexacyanoferrate(II/III) is the exclusive reactant, as opposed to the co-precipitation method employing bare metal ions and hexacyanometalate ions. Despite the widespread adoption of the single-source method, mechanistic exploration remains largely unexplored and speculative. Utilizing UV-vis spectrophotometry, negative-ion mode liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS), and a devised reaction, this study identifies crucial intermediates, including aqueous Fe^2+/3+ ions and hydrocyanic acid (HCN) in the solution. These two intermediates eventually combine to form thermodynamically stable PB. The findings presented in this research significantly contribute to understanding the fundamental mechanism underlying the acid-catalyzed hydrolysis of the hexacyanoferrate(III) complex ion and the subsequent formation of PB, as proposed in the sequential mechanism introduced herein. This finding might contribute to the cost-effective synthesis of PB by incorporating diverse metal ions and potassium cyanide.

• Journal of Environmental Science International
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• v.5 no.5
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• pp.579-583
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• 1996

This study is involved to develop new catalysts to decompose plastics, detergents and surfactants containing synthetic peptide bonds. As the first year research, the catalytic-hydrolysis of amide bond in copper complex was accomplished. The hydrolysis reaction in aqueous solution was monitored by UV/VIS spectroscopy. As the pH of the solution Is increased and the temperature is raised, the reaction rate increases. The reaction rate is observed as the first order kinetic behavior for the copper complex. The metal catalyzed hydrolysis mechanism is proposed cia metal-hydroxide in the pH region of 5.5 to 6.3. The results of characterization of the catalytic reaction mechanism can be applied to develop new catalysts for peptide bond degradation in further research.

• Applied Biological Chemistry
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• v.48 no.2
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• pp.115-119
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• 2005

The catalytic hydrolysis reactivities of dinuclear nickel (II) complex, ${\mu}-aquapentaaqua[{\mu}-3,6-bis(6'-methyl-2'-pyridyl)pyridazine]chlorodinickel\;(II)$ trichloride trihydrate (APNT) for bis(p-nitrophenyl) phosphate (BNPP) as a DNA model compound were investigated. The dissociation constants of APNT were $pKa_1=7.9$ and $pKa_2=9.6$, respectively. The hydrolysis rate constant of BNPP compound by APNT was showed the rate enhancement of about 370,000 times in the case of none catalyst at pH 7.0 and $50^{\circ}C$. Based on the findings, we proposed the catalytic cycle for the hydrolysis of BNPP by APNT complex. The metal ions of dinuclear nickel (II) complex significantly enhance the transfer rate of phosphoryl group in the catalytic process and the water molecules as nucleophile and proton transfer agent act in different steps.

• Journal of Pharmaceutical Investigation
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• v.20 no.3
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• pp.145-152
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• 1990

Zirconium pyrithione complex was prepared by reaction of sodium-pyrithione solution and zirconyl chloride solution. The physico-chemical properties of the complex was examined by means of IR, XRD, DSC and NMR. And the stability of Zr-complex was investigated on the basis of accelerated stability analysis under conditions of temp. elevation, UV radiation and pH dependence. The result indicates that the ratio of the ligand to metal in Zr-pyrithione complex was determined 4:1, and its stability constant was $4.643{\times}10^4$. The rate order of decomposition of the complex was apparent first-order reaction of which rate constant and the decomposition rate was not only accelerated by effect of heat and UV radiation but was catalyzed by specific acid-base catalysis considered the pH dependence for the hydrolysis of the complex and the suspension was most stable over the range pH 4-8 indicating that solvent catalysis is the primary made of reaction in this region.

• Journal of Soil and Groundwater Environment
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• v.20 no.1
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• pp.56-64
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• 2015

Acid mine drainage occurrence is a serious environmental problem by mining industry, it usually contains high levels of metal ions, such as iron, copper, zinc, aluminum, and manganese, as well as metalloids of which arsenic is generally of the greatest concern. An indigenous plant extract was used to produce calcium carbonate from Canavalia ensiformis as effective biomaterial, and its ability to form the calcium carbonate under stable conditions was compared to that of purified urease. X-ray diffraction and scanning electron microscopy were employed to elucidate the mechanism of calcium carbonate formation from the crude plant extracts. The results revealed that urease in the plant extracts catalyzed the hydrolysis of urea in liquid state cultures and decreased heavy metal amounts in the contaminated soil. The heavy metal amounts were decreased in the leachate from the treated mine soil; 31.7% of As, 65.8% of Mn, 50.6% of Zn, 51.6% of Pb, 45.1% of Cr, and 49.7% of Cu, respectively. The procedure described herein is a simple and beneficial method of calcium carbonate biomineralization without cultivation of microorganisms or further purification of crude extracts. This study suggests that crude plant extracts of Canavalia ensiformis have the potential to be used in place of purified forms of the enzyme during remediation of heavy metal contaminated soil.

• Membrane and Water Treatment
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• v.9 no.6
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• pp.405-419
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• 2018

Persulfates (i.e., peroxymonosulfate and peroxydisulfate) are capable of oxidizing a wide range of organic compounds via direct reactions, as well as by indirect reactions by the radical intermediates. In aqueous solution, persulfates undergo self-decomposition, which is accelerated by thermal, photochemical and metal-catalyzed methods, which usually involve the generation of various radical species. The chemistry of persulfates has been studied since the early twentieth century. However, its environmental application has recently gained attention, as persulfates show promise in in situ chemical oxidation (ISCO) for soil and groundwater remediation. Persulfates are known to have both reactivity and persistence in the subsurface, which can provide advantages over other oxidants inclined toward either of the two properties. Besides the ISCO applications, recent studies have shown that the persulfate oxidation also has the potential for wastewater treatment and disinfection. This article reviews the chemistry regarding the hydrolysis, photolysis and catalysis of persulfates and the reactions of persulfates with organic compounds in aqueous solution. This article is intended to provide insight into interpreting the behaviors of the contaminant oxidation by persulfates, as well as developing new persulfate-based oxidation technologies.

• Journal of Microbiology and Biotechnology
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• v.16 no.2
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• pp.272-279
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• 2006

The gene encoding Thermus sp. T351 alkaline phosphatase (T351 APase) was cloned and sequenced. The gene consisted of 1,503 bp coding for a protein with 500 amino acid residues including a signal peptide. The deduced amino acid sequence of T351 APase showed relatively low similarity to other Thermus APases. The T351 APase gene was expressed under the control of the T7lac promoter on the expression vector pET-22b(+) in Escherichia coli BL21 (DE3). The expressed enzyme was purified by heat treatment, and $UNO^{TM}$ Q and $HiTrap^{TM}$ Heparin HP column chromatographies. The purified enzyme exhibited high activity at extremely alkaline pHs, reaching a maximum at pH 12.0. The optimum temperature of the enzyme was $80^{\circ}C$, and the half-life at $85^{\circ}C$ was approximately 103 min. The enzyme activity was found to be dependent on metal ions: the addition of $Mg^{2+}$ and $CO^{2+}$ increased the activity, whereas EDTA inhibited it. With p-nitrophenyl phosphate as the substrate, T351 APase had a Michaelis constant ($K_{m}$) of $3.9{\times}10^{-5}M$. The enzyme catalyzed the hydrolysis of a wide variety of phosphorylated compounds.