• Bulletin of the Korean Chemical Society
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• v.31 no.6
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• pp.1615-1620
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• 2010

Bis-[dipyrido[3,2-$\alpha$:2',3'-c]phenazine)$_2$(1,10-phenanthroline)$_2Ru_2$]$^{2+}$ complexes (bis-Ru(II) complexes) tethered by linkers of various lengths were synthesized and their binding properties to DNA investigated by normal absorption and linear dichroism spectra, and fluorescence techniques in this study. Upon binding to DNA, the bis-Ru(II) complex with the longest linker (1,3-bis-(4-pyridyl)-propane), exhibited a negative $LD^r$ signal whose intensity was as large as that in the DNA absorption region, followed by a complicate $LD^r$ signal in the metal-to-ligand charge transfer region. The luminescence intensity of this bis-Ru(II) complex was enhanced. The observed $LD^r$ and luminescence results resembled that of the [Ru(1,10-phenanthroline)$_2$ dipyrido[3,2-$\alpha$:2',3'-c]phenazine]$^{2+}$ complex, whose dipyrido[3,2-$\alpha$:2',3'-c]phenazine (dppz) ligand has been known to intercalate between DNA bases. Hence, it is conclusive that both dppz ligands of the bis-Ru(II) complex intercalate. The binding stoichiometry, however, was a single intercalated dppz per ~ 2.3 bases, which violates the "nearest binding site exclusion" model for intercalation. The length between the two Ru(II) complexes may be barely long enough to accommodate one DNA base between the two dppz ligands, but not for two DNA bases. When the linker was shorter (4,4'-bipyridine or 1,2-bis-(4-pyridyl)-ethane), the magnitude of the LD in the dppz absorption region, as well as the luminescence intensity of both bis-Ru(II) complexes, was half that of the bis-Ru(II) complex bearing a long linker. This observation can be elucidated by a model whereby one of the dppz ligands intercalates while the other is exposed to the aqueous environment.

• Journal of the Korean Chemical Society
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• v.57 no.6
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• pp.703-711
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• 2013

In the present investigation, kinetic studies of oxidation of formic acid with and without catalyst and promoter in aqueous acid media were studied under the pseudo-first order conditions [formic acid]T ${\gg}[Cr(VI)]_T$ at room temperature. In the 1,10-phenanthroline (phen) promoted path, the cationic Cr(VI) phen complex is the main active oxidant species undergoes a nucleophilic attack by the substrate to form a ternary complex which subsequently experiences a redox decomposition through several steps leading to the products $CO_2$ and $H_2$ along with the Cr(III) phen complex. The anionic surfactant (i.e., sodium dodecyl sulfate, SDS) and neutral surfactant (i.e., Triton X-100, TX-100) act as catalyst and the reaction undergo simultaneously in both aqueous and micellar phase with an enhanced rate of oxidation in the micellar phase. Whereas the cationic surfactant (i.e., N-cetyl pyridinium chloride, CPC) acts as an inhibitor restricts the reaction to aqueous phase. The observed net enhancement of rate effects has been explained by considering the hydrophobic and electrostatic interaction between the surfactants and reactants. The neutral surfactant TX-100 has been observed as the suitable micellar catalyst for the phen promoted chromic acid oxidation of formic acid.

• Microbiology and Biotechnology Letters
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• v.26 no.5
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• pp.420-426
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• 1998

An extracellular glutamyl aminopeptidase (EC 3.4.11.7) producing bacterium was isolated from soil and identified as Bacillus licheniformis based on its morphological and physiological characteristics. The aminopeptidase was purified to homogeneity by ammonium sulfate precipitation, Phenyl Sepharose, Resource Q, and Superose 12 column chromatographies. The specific activity of the purified aminopeptidase was 9.2 unit/mg for glutamyl p-nitroanilide with 17.6 purification folds. The purified aminopeptidase had an estimated molecular mass of 64 kDa consists of two different subunits (42 kDa and 22 kDa), and its isoeletric point was 5.2 measured by isoelectric focusing. The optimum pH and temperature of the aminopeptidase were 8.0 and 55$^{\circ}C$, respectively. The aminopeptidase was inhibited by EDTA and 1,10-phenanthroline, suggesting it be a metalloenzyme. Comparing with other aminopeptidase, the enzyme showed relatively high activity against peptide having glutamic acid as N-terminal.

• Biomedical Science Letters
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• v.6 no.4
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• pp.261-268
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• 2000

Fibrinolytic enzyme (FE-2) was purified from the fruiting bodies of Tricholoma saponaceum using DEAE-Cellulose chromatography and Mono-S column chromatography, The enzyme has a molecular weight of 18.23 kDa and include Zn$^{2+}$ ion as found by ICP/MS. The N-terminal amino acid sequence of the enzyme was A-L-Y-V-G-X-S-P-X-Q-Q-S-L-L-V It has a pH optimum at pH 7.5, suggested that FE-2 was a neutral pretense. The activity of FE-2 was highly inhibited by EDTA and 1,10-phenanthroline, indicating that the enzyme is a metalloprotease. The activity of FE-2 was increased by $Mg^{2+}$, Zn$^{2+}$, Fe$^{2+}$, and Co$^{2+}$, but the enzyme activity was totally inhibited by Hg$^{2+}$. No inhibition was found with PMSF, E-64, pepstatin and 2-mercaptoethanol. The enzyme hydrolyzed both $A\alpha$ and B$\beta$ chains of human fibrinogen. The $\gamma$ chain was resistant to hydrolysis by FE-2.

• Proceedings of the Korean Vacuum Society Conference
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• 2011.02a
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• pp.270-270
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• 2011

유기발광소자는 자발광소자의 강점들과 낮은 구동 전압으로 발광효율이 높아 디스플레이 소자와 백색 조명 광원으로 응용 가능성 때문에 발광효율 증진에 대한 연구가 활발히 진행되고 있다. 유기물 내에서의 정공의 이동도가 전자의 이동도보다 높아 발광층에서 정공과 전자의 수의 불균형이 나타나 재결합율이 떨어져 발광효율이 낮아지는 문제점이 있다. 본 연구에서는 전자의 이동도의 향상을 통한 발광층에서의 정공과 전자 재결합 효율을 향상하기 위해 전자수송층과 발광층으로 사용되는 tris(8-hydroxyquinolate)aluminum (Alq3)층에 Alq3보다 높은 전자이동도를 가지는 7-diphenyl-1,10-phenanthroline (BPhen)을 전자 수송층에 도핑하여 유기발광소자를 제작하였다. 2,9-dimethyl-4,7-diphenyl-1,10-phenanthroline을 정공저지층으로 사용하여 제작된 단일전자 소자를 이용하여 BPhen이 도핑된 전자 수송층을 사용한 소자가 Alq3만을 전자 수송층으로 사용한 소자보다 같은 전압에서 더 높은 전류밀도를 나타내었다. 전류밀도-전압특성 측정으로 전하 수송 메카니즘을 관찰하였다. 두 가지 전자 수송층을 사용하여 발광 소자를 제작하여 발광세기와 발광효율을 측정한 결과 도핑 된 전자 수송층을 사용하여 제작된 발광소자에서 발광세기와 발광효율이 향상되었다. 발광세기와 발광효율이 향상된 원인은 도핑된 전자수송층에서 높아진 전자의 이동도로 인하여 발광층에서 정공과 전자의 이동도가 균형을 이루어 전자-정공의 재결합 확률이 증가하기 때문이다. 도핑 된 전자 수송층을 사용하여 제작된 유기발광소자의 발광효율 향상에 대한 원인을 실험결과를 사용하여 설명 할 것이다.

• Proceedings of the Korean Vacuum Society Conference
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• 2012.02a
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• pp.472-472
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• 2012

유기발광소자는 빠른 응답속도, 높은 색재현성, 높은 명암비의 장점을 가지고 있어 차세대 디스플레이로 각광 받고 있으며, 이미 소형 디스플레이로 상용화되고 있다. 유기발광소자에서는 발광효율을 높이기 위해서 전하들의 균형이 매우 중요하다. 유기발광소자 내 정공의 이동도는 전자의 이동도보다 빠르기 때문에 정공의 이동도를 감소하거나, 전자의 이동도를 증가하여 전하들의 균형을 형성함으로 유기발광소자의 효율을 증진시키는 연구가 진행되고 있다. 본 연구는 유기발광소자의 전자 수송층을 다층구조로 적층하여 전자의 이동도를 증가하여 효율이 증진하는 메커니즘을 기본으로 하였다. 전자 수송층을 tris(8-hydroxyquinoloine)aluminum ($Alq_3$) 단일층, 4,7-diphenyl-1, 10-phenanthroline (BPhen)과 $Alq_3$의 혼합층및 BPhen과 $Alq_3$ 다층 구조로 제작한 유기발광소자의 전기적, 발광 특성을 비교 분석하였다. BPhen은 lowest unoccupied molecular orbital (LUMO) 준위가 $Alq_3$의 LUMO 준위와 유사하여 전자 주입이 효율적으로 일어나며, 또한 낮은 highest occupied molecular orbital (HOMO) 준위는 정공 저지층의 역할을 하여 발광층 내에서 전하의 균형을 효율적으로 맞춰준다. 유기발광소자는 N,N,'-bis-(1-naphthyl)-N,N'-diphenyl1-1'-biphenyl-4,4'-diamine (NPB)/ $Alq_3$/ 다양한 전자수송층 / lithium quinolate (Liq)/ aluminium (Al) 음극 전극으로 각각 증착하여 제작하였다. 전자수송층을 다층 구조로 사용한 유기발광소자는 발광효율이 혼합층과 단일층에 비해 높았으며, 최대 발광효율은 전류밀도가 273 mA/cm2일때 4.5 cd/A였다. 다층구조의 전자수송층에서 다층으로 증착된 BPhen이 효율적인 전자 주입 및 전공 저지하는 역할을 최적화 하여 발광층에 더 많은 엑시톤이 형성하여, 유기발광소자의 효율을 증진시켜 준다는 사실을 알 수 있었다.

• Analytical Science and Technology
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• v.8 no.4
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• pp.869-876
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• 1995

The active sites of the nickel and iron-containing enzyme, carbon monoxide dehydrogenase (CODH) from clostridium thermoaceticum were investigated using Electron Paramagnetic Resonance (EPR) technique. CODH exhibits several spectral features called NiFeC, $g_{ave}=1.82$, $g_{ave}=1.86$. FCII signals which are originated from different clusters in this enzyme. CODH is know to catalyze two different kinds of reactions - acetyl-CoA synthesis and CO oxidation. The acetyl-CoA synthesis activity can be followed by monitoring CO/acetyl-CoA exchange. The addition of 1,10-phenanthroline (phen) to CODH selectively destroyed the CO/acetyl-CoA exchange activity and eliminated the NiFeC signal completely. CO oxidation activity and other EPR signals were unaffected. Such behavior demonstrates that CODH has two distinct active sites and that the NiFe complex is only responsible for the CO/acctyl-CoA exchange activity. Phen caused the removal of only 30% of Ni in the NiFe complex ($0.3Ni/{\alpha}{\beta}$) as shown by the quantitative metal analysis. The phen-treated CODH could be reactivated fully by incubation In $Ni^{2+}$ solution. Radioactive $^{63}Ni^{2+}$ was used to quantitate the amount of the $Ni^{2+}$ incorporated into phen-treated enzyme and showed that the amount was the same as the removed by the phen treatment. i.e. $0.3Ni/{\alpha}{\beta}$. This indicates that only 30% of NiFe complexes are labile and responsible for the CO/acctyl-CoA exchange activity, the other 70% are non-labile and have no exchange activity. This is the first clear evidence that the NiFe complex is heterogencous and labile and non-labile Ni sites arc interacting differently with substrates and chelating agents like phen.

• Journal of the Korean Chemical Society
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• v.36 no.1
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• pp.81-86
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• 1992

The electrophilic and nucleophilic reactions of M(S-S,ph)(N-N,H) (M = Ni(II), Pd(II), Pt(II); (S-S,ph) = 1,2-diphenylethylenedithiolate; (N-N,H)=1,10-phenanthroline) complexes have been investigated. Reaction with norbornadiene depended upon the back donating ability of the central metal ion and produced 2,5-dithia-3,4-diphenyl-tricyclo[4,4,1,0]-undeca-3,8-diene. In the reaction with methyl iodide, the effect of cleavage of (N-N,H) ligand affected the yield of methylated $M(S-S,ph)_2$ product. The structure of the thermolysis product, ${\alpha},{\alpha}{\prime}$-bismethylthiostibene $(CH_3S-SCH_3,ph)$ of methylated complexes indicates that the main product of the nucleophilic reaction is $M(CH_3S-SCH_3,ph)(S-S,ph)$. We have synthesized a new mixed-ligand complex M(S-S,CN)(N-N,H)((S-S,CN) = 1,2-dicyanoethylenedithiolate) through the nucleophilic reaction of ligand.

• Applied Biological Chemistry
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• v.41 no.5
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• pp.349-354
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• 1998

The protease produced by Bacillus subtilis YG-95 was purified by precipitating with ammonium sulfate, DEAE-sepharose 6B and Sephadex G-100 column chromatogtaphies and its purified enzymological characteritics were investigated. The molecular weight of purified protease was estimated about 43kilodalton by SDS PAGE The optimum pH and temperature for the purified protease activity were pH 10.0 and $55^{\circ}C$, respectively. The enzyme was stable in broad range of pH 5.0 to 12.0. and at the below $45^{\circ}C$. The purified enzyme activty was inhibited by $Fe^{3+}$ and $Al^{3+}$. The activity was significantly inhibited more than 80% by O-Phenanthroline, PMSF and SDS. The $K_m$ value of the purified enzyme against Soy Protein Isolate as a substrate was 1.28 mg/ml.

• Journal of the Korean Chemical Society
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• v.38 no.7
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• pp.485-495
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• 1994

Several new symmetric and asymmetric homo and hetero dinuclear complexes of the type $[Cl(dppp)(NO)_2M({\mu}-pyz)M'(NO)_2(dppp)Cl][ClO_4]_2$ and $[Cl(phen)(NO)_2M({\mu}-pyz)M'(NO)_2(dppp)Cl][ClO_4]_2$(M,M'= Mo or W; phen = 1,10-phenanthroline; dppp = 1,3-bis(diphenylphosphino)propane; pyz = 1,4-pyrazine) were synthesized in three-steps starting from $[M(NO)_2Cl_2]_n(M = Mo, W)$. The final products were purified by eluting it through silica gel column ($2{\times}20$ cm) with acetone as the eluent. Characterization of these complexes and some related complexes was accomplished through UV-vis., $^1H$-NMR, $^{13}C$-NMR and IR spectroscopies as well as elemental analysis. The infrared spectra indicate that the NO groups occupy cis-positions of the octahedral. The $^1H$ and $^{13}C-NMR$ data for the new compounds revealed a dimeric structures with bridged pyz.