• Title/Summary/Keyword: NADH

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Photocatalytic Systems of Pt Nanoparticles and Molecular Co Complexes for NADH Regeneration and Enzyme-coupled CO2 Conversion

  • Kim, Ellen;Jeon, Minkyung;Kim, Soojin;Yadav, Paras Nath;Jeong, Kwang-Duk;Kim, Jinheung
    • Rapid Communication in Photoscience
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    • v.2 no.2
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    • pp.42-45
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    • 2013
  • Natural photosynthesis utilizes solar energy to convert carbon dioxide and water to energy-rich carbohydrates. Substantial use of sunlight to meet world energy demands requires energy storage in useful fuels via chemical bonds because sunlight is intermittent. Artificial photosynthesis research focuses the fundamental natural process to design solar energy conversion systems. Nicotinamide adenine dinucleotide ($NAD^+$) and $NADP^+$ are ubiquitous as electron transporters in biological systems. Enzymatic, chemical, and electrochemical methods have been reported for NADH regeneration. As photochemical systems, visible light-driven catalytic activity of NADH regeneration was carried out using platinum nanoparticles, molecular rhodium and cobalt complexes in the presence of triethanolamine as a sacrificial electron donor. Pt nanoparticles showed photochemical NADH regeneration activity without additional visible light collector molecules, demonstrating that both photoactivating and catalytic activities exist together in Pt nanoparticles. The NADH regeneration of the Pt nanoparticle system was not interfered with the reduction of $O_2$. Molecular cobalt complexes containing dimethylglyoxime ligands also transfer their hydrides to $NAD^+$ with photoactivation of eosin Y in the presence of TEOA. In this photocatalytic reaction, the $NAD^+$ reduction process competed with a proton reduction.

Effects of Local Anesthetics on Electron Transport and Generation of Superoxide Radicals in Mitochondria (국소마취제가 Mitochondria에서의 전자이동 및 Superoxide Radicals의 생성에 미치는 영향)

  • Lee, Chung-Soo;Shin, Yong-Kyoo;Lee, Kwang-Soo
    • The Korean Journal of Pharmacology
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    • v.23 no.2
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    • pp.113-121
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    • 1987
  • Local anesthetics were investigated for their effects on mitochondrial electron transport system, production of superoxide radical from submitochondrial particles and malondialdehyde production through lipid per oxidation. Local anesthetics had various effects on activities of enzymes in electron transport chain. The activities of NADH dehydrogenase, NADH oxidase and NADH-ubiquinone oxidoreductase were effectively inhibited by lidocaine, procaine and dibucaine but slightly influenced by cocaine. The activities of succinate dehydrogenase, succinate-cytochrome c oxidoreductase and succinate-ubiquinone oxidoreductase were inhibited by lidocaine and dibucaine, but the succinate oxidase activity was stimulated by local anesthetics. Both dihydroubiquinone-cytochrome c oxidoreductase and cytochrome c oxidase activities were inhibited by local anesthetics. In these reactions, the response of Complex I segment to local anesthetics was greater than other Complex segments. Local anesthetics inhibited both the superoxide production from submitochondrial particles supplemented with succinate or NADH and the enhanced production of superoxide radicals by antimycin. The malondialdehyde production by oxygen free radicals was inhibited by local anesthetics. These results suggest that the inhibition of superoxide and malondialdehyde production caused by local anesthetics may be brought by suppression of the electron transport in mitochondria at sites in or near complex I segment.

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Evidence for Singlet Oxygen Involvement in Cell-free Myeloperoxidase/$H_2O_2$/ Chloride Sytem: Exclusion of Hydroxyl Radical Involvement (Cell-free Myeloperoxidase/$H_2O_3$/Chloride System에서 Singlet Oxygen이 관여한다는 실험적 증거)

  • Chung Myung-Hee;Kim Yong-Sik
    • The Korean Journal of Pharmacology
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    • v.20 no.1 s.34
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    • pp.1-11
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    • 1984
  • The present study was performed to determine oxygen metabolites involved in cell-free MPO/$H_2O_2/Cl^-$ system by observing the effects of their scavengers on NADH oxidation and ethylene production from methional by the action of MPO prepared from human leukocytes. It was clearly demonstrated that NADH was oxidized by the cell-free MPO/$H_2O_2/Cl^-$ system as evidenced by complete inhibition of the oxidation of the substrate in the presence of eiher azide or catalase, or by omitting $Cl^-$. The MPO-mediated oxidation of NADH was completely abolished by a $^1O_2$ quencher, DABCO but not by $OH{\cdot}$ scavengers, mannitol, benzoate, formate and methanol. In ethylene assay, no ethylene was detected from methional in the MPO/$H_2O_2/Cl^-$ system with evident production of the gas by xanthine-oxidase and $Cu^{++}-H_2O_2$ systems which are suggested to generate $OH{\cdot}$. From the results obtained, it is concluded that $^1O_2$ is a major mediator with exclusion of $OH{\cdot}$ involvement in the cell-free MPO-mediated oxidation.

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Purification of xylose reductase from Candida sp. BT001 and characterization of its properties (Candida sp. BT001의 xylose reductase의 정제 및 성질)

  • Hwang, In-Gyun;Lee, Sang-Hyub;Lee, Wang-Sik;Bang, Won-Gi
    • Applied Biological Chemistry
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    • v.36 no.3
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    • pp.178-183
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    • 1993
  • Xylose reductase (alditol: $NADP^+$ 1-oxidoreductase, EC 1.1.1.21) from the xylose-fermenting yeast, Candida sp. BT001, was purified via salt fractionation, ion-exchange, gel filtration and affinity chromatography, and its properties were characterized. The enzyme from the yeast was active with both NADPH and NADH as coenzyme. The xylose reductase activity with NADH was approximately 51% of that with NADPH and the specific activities of purified enzyme with NADPH and NADH were 11.78 U/mg and 6.01 U/mg, respectively. Molecular weight of the purified enzyme was 31,000 on SDS-PAGE and 61,000 on gel filtration. The Km for D-xylose, NADPH, and NADH was $94.2{\times}10^{-3}M,\;0.011{\times}10^{-3}M\;and \;0.032{\times}10^{-3}M$, respectively. The purified xylose reductase had relatively higher substrate affinity for L-arabinose than other aldoses tested. The optimal pH was 6.2 and the optimal reaction temperature was $45^{\circ}C$. The thermal stability of the enzyme was for 20 minutes at $30^{\circ}C$.

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Effect of Exercise on Muscle Recovery of Sciatic Nerve Injured Rats (궁둥신경 손상을 유발한 흰쥐에서 운동이 근육재생에 미치는 영향)

  • Ro, Hyo-Lyun
    • Proceedings of the KAIS Fall Conference
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    • 2010.05b
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    • pp.855-858
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    • 2010
  • 이 연구의 목적은 흰쥐의 궁둥신경의 손상을 준 뒤 달리기운동을 시켜 운동이 근육재생에 효과가 있는지를 밝힐 목적으로 시행하였다. 수컷 Sprague-Dawley계 흰쥐의 궁둥신경을 압궤손상을 준후, 하루 60분 씩 주 5회 운동을 시켰다. 궁둥신경 압궤손상 후 12일(5일간 운동), 19일(10일간 운동), 26일(15일간 운동), 33일(20일간 운동 및 61일(40일간 운동)에 흰쥐를 희생시켜 장딴지근육을 절취하여 냉동절편을 만들었으며 중간세사인 desmin과 vimentin에 대한 면역조직화학적 염색방법을 시행하였고 NADH-TR을 이용한 효소조직화학적 방법으로 뼈대근육의 변성 등을 관찰하였다. 중간세사단백 중 desmin은 근육섬유의 변성 및 재생과정 모두에서 발현되며 vimentin은 재생과정에서만 발현되었다. 대조군보다 실험군에서 desmin과 vimentin의 면역 반응성이 높았고, 실험군의 근육섬유들은 손상 후 61일째에 횡단면에서 각을 갖고 있어 정상 근육섬유임을 입증해 주었으나 대조군의 근육섬유는 정상으로 회복되지 않은 둥근 근육섬유가 관찰되었다. 19일째의 NADH-TR반응에서 대조군에서는 근육 섬유형 군집(fiber type grouping)으로 인해 diformazan 과립이 뭉쳐져 있음을 볼 수 있으나 실험군에서는 점점 diformazan 과립이 고르게 분포됨을 볼 수 있었다. 재신경지배가 일어 날 때 나타나는 표적근육섬유(target fiber)는 NADH-TR반응에서 26일 실험군의 일부 근육섬유에서 처음으로 관찰되었다. 61일째 NADH-TR반응에서 대조군은 아직도 diformazan 과립이 근육섬유성 군집을 보였으나 실험군에서는 정상군과 다름없는 염색성이 관찰되었다. 이상의 결과로 흰쥐 궁둥신경 압궤손상 후 트레드밀 달리기 운동이 흰쥐 다리 뼈대근육의 중간세사발현에 효과가 있다고 생각된다.

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Electrochemical Reduction of Xylose to Xylitol by Whole Cells or Crude Enzyme of Candida peltata

  • Park Sun Mi;Sang Byung In;Park Dae Won;Park Doo Hyun
    • Journal of Microbiology
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    • v.43 no.5
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    • pp.451-455
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    • 2005
  • In this study, whole cells and a crude enzyme of Candida peltata were applied to an electrochemical bioreactor, in order to induce an increment of the reduction of xylose to xylitol. Neutral red was utilized as an electron mediator in the whole cell reactor, and a graphite-Mn(IV) electrode was used as a catalyst in the enzyme reactor in order to induce the electrochemical reduction of $NAD^+$ to NADH. The efficiency with which xylose was converted to xylitol in the electrochemical bioreactor was five times higher than that in the conventional bioreactor, when whole cells were employed as a biocatalyst. Meanwhile, the xylose to xylitol reduction efficiency in the enzyme reactor using the graphite-Mn (IV) electrode and $NAD^+$ was twice as high as that observed in the conventional bioreactor which utilized NADH as a reducing power. In order to use the graphite-Mn(IV) electrode as a catalyst for the reduction of $NAD^+$ to NADH, a bioelectrocatalyst was engineered, namely, oxidoreductase (e.g. xylose reductase). $NAD^+$ can function in this biotransformation procedure without any electron mediator or a second oxidoreductase for $NAD^+/NADH$ recycling