• KIEE International Transactions on Electrophysics and Applications
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• v.2C no.5
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• pp.246-252
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• 2002

Two-dimensional steady state simulations of planar type radio frequency inductively coupled plasma (RFICP) have been performed. The characteristics of RFICP were investigated in terms of power transfer efficiency, equivalent circuit analysis, spatial distribution of plasma density and electron temperature. Plasma density and electron temperature were determined from the equations of ambipolar diffusion and energy conservation. Joule heating, ionization, excitation and elastic collision loss were included as the source terms of the electron energy equation. The electromagnetic field was calculated from the vector potential formulation of ampere's law. The peak electron temperature decreases from about 4eV to 2eV as pressure increases from 5 mTorr to 100 mTorr. The peak density increases with increasing pressure. Electron temperatures at the center of the chamber are almost independent of input power and electron densities linearly increase with power level. The results agree well with theoretical analysis and experimental results. A single turn, edge feeding antenna configuration shows better density uniformity than a four-turn antenna system at relatively low pressure conditions. The thickness of the dielectric window should be minimized to reduce power loss. The equivalent resistance of the system increases with both power and pressure, which reflects the improvement of power transfer efficiency.

• Journal of Microbiology and Biotechnology
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• v.30 no.8
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• pp.1261-1271
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• 2020

Cytochrome c_L (Cytc_L) is an essential protein in the process of methanol oxidation in methylotrophs. It receives an electron from the pyrroloquinoline quinone (PQQ) cofactor of methanol dehydrogenase (MDH) to produce formaldehyde. The direct electron transfer mechanism between Cytc_L and MDH remains unknown due to the lack of structural information. To help gain a better understanding of the mechanism, we determined the first crystal structure of heme c containing Cytc_L from the aquatic methylotrophic bacterium Methylophaga aminisulfidivorans MP^T at 2.13 Å resolution. The crystal structure of Ma-Cytc_L revealed its unique features compared to those of the terrestrial homologues. Apart from Fe in heme, three additional metal ion binding sites for Na⁺, Ca⁺, and Fe²⁺ were found, wherein the ions mostly formed coordination bonds with the amino acid residues on the loop (G93-Y111) that interacts with heme. Therefore, these ions seemed to enhance the stability of heme insertion by increasing the loop's steadiness. The basic N-terminal end, together with helix α4 and loop (G126 to Y136), contributed positive charge to the region. In contrast, the acidic C-terminal end provided a negatively charged surface, yielding several electrostatic contact points with partner proteins for electron transfer. These exceptional features of Ma-Cytc_L, along with the structural information of MDH, led us to hypothesize the need for an adapter protein bridging MDH to Cytc_L within appropriate proximity for electron transfer. With this knowledge in mind, the methanol oxidation complex reconstitution in vitro could be utilized to produce metabolic intermediates at the industry level.

• Polymer(Korea)
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• v.31 no.2
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• pp.136-140
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• 2007

Charge transfer interaction as a hybridization mechanism of silsesquioxane/polymer was tested using carbazole (electron donor) group and dinitrobenzene (electron acceptor) group. Hybridization test was conducted using films made from mixing/casting of poly (carbazole-styrene) (PS/D) and dimtrobenzyl silsesquioxane (Cube/A), and transparent hybrid films were successfully obtained under some conditions. $^1H-NMR$ of PS/D and Cube/A, and W absorption test of hybrid films showed that one acceptor and one donor can form one charge transfer complex when no silsesquioxane molecule was included in films, but transparent hybrids with no phase separation were obtained only at acceptor/donor ratios less than 0.7 : 1. These results also suggested that on average 4 charge transfer complexes form per one silsesquioxane.

• Bulletin of the Korean Chemical Society
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• v.27 no.3
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• pp.381-385
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• 2006

The temperature dependence on the electron transfer rate constant $(k_{app})$ for hydroquinone redox center in $H_2Q(CH_2)_n$SH-SAMs (n = 1, 4, 6, 8, 10, and 12) on gold electrode was investigated to obtain reorganization energy $(\lambda)$ using Laviron’s formalism and Arrhenius plot of ln $[k_{app}/T^{1/2}]$ vs. T^{-1} based on the Marcus densityof-states model. All the symmetry factors measured for the SAMs were relatively close to unity and rarely varied to temperature change as expected. The electron tunneling constant $(\beta)$ determined from the dependence of the $k_{app}$ on the distance between the redox center and the electrode surface gives almost the same $\beta$ values which are quite insensitive to temperature change. Good linear relationship of Arrhenius plot for all $H_2Q(CH_2)_n$SH-SAMs on gold electrode was obtained in the temperature range from 273 to 328 K. The slopes n Arrhenius plot deduced that $\lambda$ of hydroquinone moiety is ca. 1.3-1.4 eV irrespectively of alkyl chain length of the electroactive SAM.

• BMB Reports
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• v.29 no.4
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• pp.300-307
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• 1996

ATP and ADP are potential regulators of mitochondtial respiration and at physiological concentrations they affect the rate of electron transfer between cytochrome c and cytochrome c oxidase. The electron transfer, however, depends on the electrostatic interaction between the two proteins. In order to exclude any nonspecific ionic effects by these polyvalent nucleotides, we used 2'-O-(2,4,6)trinitro(TNP)-derivatives of ATP and ADP which have three orders of magnitude higher affinity for cytochrome c oxidase. A simple titration of the fluorescence intensity of TNP by cytochrome c oxidase showed a binding stoichiometry of 2:1 cytochrome c:cytochrome c oxidase. Higher ionic strength was required for TNP-ATP than for TNP-ADP to be dissociated from cytochrome c oxidase, indicating that the negative charges on the phosphate group are at least partially responsible for the binding. In both spectrophotometric and polarographic assays, addition of ATP (and ADP to a less extent) showed an enhanced cytochrome c oxidase activity. Both electron paramagnetic resonance and fluorescence spectra indicate that there is no Significant change in the cytochrome c-cytochrome c oxidase interaction. Instead, reduction levels of the cytochromes at steadystate suggest that the increased activity of nucleotide-bound cytochrome c oxidase is due to faster electron transfer from cytochrome ${\alpha}$ to cytochrome ${\alpha}_3$, which is known to be the fate limiting step in the oxygen reduction by cytochrome c oxidase.

• Journal of The Korean Astronomical Society
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• v.22 no.2
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• pp.127-140
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• 1989

Problem of the diffuse radiation (DFR) transfer is solved exactly for pure hydrogen nebulae of uniform density, and accuracies of the on-the-spot (OTS) approximation are critically examined. For different values of density and spectral types of the central star, we have calculated the degree of ionization and the kinetic temperature of electrons as functions of distance from the central star, and compared them with the corresponding results of the OTS approximation. At most locations inside an HII region. the DFR ionizes considerable amount of hydrogen; therefore, the OTS approximation under-estimates the size of ionized regions. The exact treatment of the DFR transfer results in an about 10 to 20 percent increase in the classical $Str{\ddot{o}}mgren$ radius. The OTS approximation overestimates the local heating rate by raising the density of neutral hydogens. Consequently, it predicts higher values for the local electron temperature. The OTS approximation also exaggerates the dependence of electron temperature on density. When the hydrogen density is changed from $10/cm^3$ to $10^3/cm^3$ with an 06.5V star, the OTS approximation shows an about 3,000 K difference in the electron temperature, while the exact treatment of the DFR-transfer reduces the difference to about 1,000 K. The OTS approximation fails to demonstrate the brightening of the electron temperature close to the ionization boundary.

• Journal of the Korean Chemical Society
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• v.39 no.4
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• pp.275-280
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• 1995

The electron transfer reactions between cis-[Co(en)2(NO2)2]+ and rac-[Co(Y)]2-(Y=EDTA, PDTA, CyDTA) have been investigated in the presence of hydrogen ion. From the kinetic data, it has been found that electron transfer reactions between cis-[Co(en)2(NO2)2]+ and rac-[Co(Y)]2- proceed via inner-sphere pathway by catalysis of hydogen ion. The stereoselectivity in the electron transfer reactions between optically active △-cis-[Co(en)2(NO2)2]+ and rac-[Co(Y)]2- produced 6.0, 2.9, 3.0% e.e.(e.e.=enantiomeric excess) of △-[Co(EDTA)]-, △-[Co(PDTA)]- and △-[Co(CyDTA)]-, respectively. Based upon this observation, it seems that △-cis-[Co(en)2(NO2)2]+ is associated with rac-[Co(Y)]2- at first, and followed by the electron transfer reaction. Therefore, it was suggested that stereoselective electron transfer reaction between △-cis-[Co(en)2(NO2)2]+ and rac-[Co(Y)]2- proceed through both inner-sphere by the proton catalysis and outer-sphere with ionic association.

• Bulletin of the Korean Chemical Society
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• v.28 no.12
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• pp.2271-2278
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• 2007

Electron transfer of a redox protein at a bare gold electrode is too slow to observe the redox peaks. A novel Nafion-riboflavin functional membrane was constructed during this study and electron transfer of cytochrome c, superoxide dismutase, and hemoglobin were carried out on the functional membrane-modified gold electrode with good stability and repeatability. The immobilized protein-modified electrodes showed quasireversible electrochemical redox behaviors with formal potentials of 0.150, 0.175, and 0.202 V versus Ag/AgCl for the cytochrome c, superoxide dismutase and hemoglobin, respectively. Whole experiment was carried out in the 50 mM MOPS buffer solution with pH 6.0 at 25 oC. For the immobilized protein, the cathodic transfer coefficients were 0.67, 0.68 and 0.67 and electron transfer-rate constants were evaluated to be 2.25, 2.23 and 2.5 s?1, respectively. Hydrogen peroxide concentration was measured by the peroxidase activity of hemoglobin and our experiment revealed that the enzyme was fully functional while immobilized on the Nafion-riboflavin membrane.

• Journal of the Korean Institute of Electrical and Electronic Material Engineers
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• v.17 no.12
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• pp.1337-1340
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• 2004

The self-assembled monolayers of alkane derivatives with sulfur containing head groups on gold substrates have been widely examined recently, since the binding between S atoms and Au surface is strong. The viologen has been widely investigated their well-behaved electrochemistry including electron transfer mediation, the surface-enhanced of the adsorption and the behavior of supramolecular assemblies at electrode surfaces in theses and various studies. Yiologen monolayers are formed onto QCM by self-assembly method. We studied the relationship of electron transfer from changing the anions in 0.1 M NaCl and NaClO$_4$ electrolyte solution. The EQCM measurements revealed the anions transfer during reduction and oxidation, respectively From the EQCM data, the well-defined shape peaks were nearly equal charges by cyclic voltammetry.

• Journal of the Korean Chemical Society
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• v.38 no.8
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• pp.598-602
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• 1994

Light-induced electron transfer reaction within binuclear complex $(NC)_5FeII-L-CoIII(NH_3)_5$ was studied with steady-state photolysis and the rate constants were measured for various bridging lignands. klight and quantum yields for BP, PHEN, DAP having conjugation between metal binding sites were about $3{\times}10^{-2} sec^{-1}$ and 1, and for BPEA having no conjugation were about $2{\times}10^{-4} sec^{-1}$ and 0.03. Light-induced electron transfer reaction within binuclear complex was proved to be the chemical mechanism which had charge transfer excited state MLCT*.