Relevant bibliographies by topics / NADH

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'NADH'

Author: Grafiati
Published: 4 June 2021
Last updated: 8 June 2024

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Journal articles on the topic "NADH"

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Tsai, Hsieh-Chin, Cheng-Hung Hsieh, Ching-Wen Hsu, Yau-Heiu Hsu, and Lee-Feng Chien. "Cloning and Organelle Expression of Bamboo Mitochondrial Complex I Subunits Nad1, Nad2, Nad4, and Nad5 in the Yeast Saccharomyces cerevisiae." International Journal of Molecular Sciences 23, no. 7 (April 6, 2022): 4054. http://dx.doi.org/10.3390/ijms23074054.

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Mitochondrial respiratory complex I catalyzes electron transfer from NADH to ubiquinone and pumps protons from the matrix into the intermembrane space. In particular, the complex I subunits Nad1, Nad2, Nad4, and Nad5, which are encoded by the nad1, nad2, nad4, and nad5 genes, reside at the mitochondrial inner membrane and possibly function as proton (H+) and ion translocators. To understand the individual functional roles of the Nad1, Nad2, Nad4, and Nad5 subunits in bamboo, each cDNA of these four genes was cloned into the pYES2 vector and expressed in the mitochondria of the yeast Saccharomyces cerevisiae. The mitochondrial targeting peptide mt gene (encoding MT) and the egfp marker gene (encoding enhanced green fluorescent protein, EGFP) were fused at the 5′-terminal and 3′-terminal ends, respectively. The constructed plasmids were then transformed into yeast. RNA transcripts and fusion protein expression were observed in the yeast transformants. Mitochondrial localizations of the MT-Nad1-EGFP, MT-Nad2-EGFP, MT-Nad4-EGFP, and MT-Nad5-EGFP fusion proteins were confirmed by fluorescence microscopy. The ectopically expressed bamboo subunits Nad1, Nad2, Nad4, and Nad5 may function in ion translocation, which was confirmed by growth phenotype assays with the addition of different concentrations of K+, Na+, or H+.
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Scholz, T. D., M. R. Laughlin, R. S. Balaban, V. V. Kupriyanov, and F. W. Heineman. "Effect of substrate on mitochondrial NADH, cytosolic redox state, and phosphorylated compounds in isolated hearts." American Journal of Physiology-Heart and Circulatory Physiology 268, no. 1 (January 1, 1995): H82—H91. http://dx.doi.org/10.1152/ajpheart.1995.268.1.h82.

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The effect of metabolic substrates on the relation among cytosolic redox state (NADHc/NAD+) mitochondrial NADH (NADHm), and [ATP]/([ADP] x [Pi]) was studied in isolated working rabbit hearts. Substrates were varied from 5.6 mM glucose alone to glucose in combination with 10 mM lactate and/or 10 mM pyruvate while afterload and preload were held constant. Changes in NADHm were determined from epicardial NADH fluorescence. The ratio of glycerol 3-phosphate (G-3-P) to dihydroxyacetone phosphate (DHAP), determined from tissue extracts, was used as an index of cytosolic redox. Myocardial 31P metabolites were measured using nuclear magnetic resonance spectroscopy. The addition of pyruvate to the perfusion medium caused increases in myocardial oxygen consumption (MVo2), NADHm fluorescence, phosphocreatine (PCr), and [ATP]/([ADP] x [Pi]) and a decrease in NADHc/NADc+ (decreased G-3-P/DHAP). Although the addition of lactate to the perfusion medium caused an increase in NADHm similar to pyruvate, MVo2 and PCr did not change significantly, [ATP]/([ADP] x [Pi]) increased less than with pyruvate, and there was an increase in NADHc/NADc+. The findings suggest that variations in the cytosolic redox state do not necessarily result in obligatory changes in either the mitochondrial redox state or in the [ATP]/([ADP] x [Pi]). This implies that under the conditions of this study an equilibrium is not maintained between [ATP]/([ADP] x [Pi]) and NADHc/NADc+. Furthermore, similar levels of NADHm can be associated with different values for [ATP]/([ADP] x [Pi]) and MVo2, depending on the substrates available to the heart.
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Qi, Xiangying, Kaiqi Wang, Liping Yang, Zhenshan Deng, and Zhihong Sun. "The complete mitogenome sequence of the coral lily (Lilium pumilum) and the Lanzhou lily (Lilium davidii) in China." Open Life Sciences 15, no. 1 (December 31, 2020): 1060–67. http://dx.doi.org/10.1515/biol-2020-0102.

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AbstractBackgroundThe mitogenomes of higher plants are conserved. This study was performed to complete the mitogenome of two China Lilium species (Lilium pumilum Redouté and Lilium davidii var. unicolor (Hoog) cotton).MethodsGenomic DNA was separately extracted from the leaves of L. pumilum and L. davidii in triplicate and used for sequencing. The mitogenome of Allium cepa was used as a reference. Genome assembly, annotation and phylogenetic tree were analyzed.ResultsThe mitogenome of L. pumilum and L. davidii was 988,986 bp and 924,401 bp in length, respectively. There were 22 core protein-coding genes (including atp1, atp4, atp6, atp9, ccmB, ccmC, ccmFc, ccmFN1, ccmFN2, cob, cox3, matR, mttB, nad1, nad2, nad3, nad4, nad4L, nad5, nad6, nad7 and nad9), one open reading frame and one ribosomal protein-coding gene (rps12) in the mitogenomes. Compared with the A. cepa mitogenome, the coding sequence of the 24 genes and intergenic spacers in L. pumilum and L. davidii mitogenome contained 1,621 and 1,617 variable sites, respectively. In the phylogenetic tree, L. pumilum and L. davidii were distinct from A. cepa (NC_030100).ConclusionsL. pumilum and L. davidii mitogenomes have far distances from other plants. This study provided additional information on the species resources of China Lilium.
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TURNER, William L., Jeffrey C. WALLER, and Wayne A. SNEDDEN. "Identification, molecular cloning and functional characterization of a novel NADH kinase from Arabidopsis thaliana (thale cress)." Biochemical Journal 385, no. 1 (December 14, 2004): 217–23. http://dx.doi.org/10.1042/bj20040292.

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NADH kinase (NADHK; ATP:NADH 2′-phosphotransferase; EC 2.7.1.86), an enzyme that preferentially utilizes NADH as the diphosphonicotinamide nucleotide donor, has been identified for the first time in plants. Low activity (0.4 nmol of NADPH produced/min per mg of protein) was observed in clarified protein extracts from Arabidopsis thaliana (thale cress) cell suspension cultures. However, unlike an NADHK from yeast (Saccharomyces cerevisiae) (POS5), the enzyme from Arabidopsis did not associate with the mitochondria. NADHK was cloned (gi:30699338) from Arabidopsis and studied as a recombinant protein following affinity purification from Escherichia coli. The enzyme had a pH optimum for activity of 7.9 and a subunit molecular mass of 35 kDa. Analytical gel filtration demonstrated that the recombinant enzyme exists as a dimer. Hyperbolic saturation kinetics were observed for the binding of NADH, ATP, free Mg2+ and NAD+, with respective Km values of 0.042, 0.062, 1.16, and 2.39 mM. While NADHK could phosphorylate NADH or NAD+, the specificity constant (Vmax/Km) for NADH was 100-fold greater than for NAD+. The enzyme could utilize UTP, GTP and CTP as alternative nucleotides, although ATP was the preferred substrate. PPi or poly-Pi could not substitute as phospho donors. PPi acted as a mixed inhibitor with respect to both NADH and ATP. NADHK was inactivated by thiol-modifying reagents, with inactivation being decreased in the presence of NADH or ATP, but not NAD+. This study suggests that, in Arabidopsis, NADP+/NADPH biosynthetic capacity could, under some circumstances, become uncoupled from the redox status of the diphosphonicotinamide nucleotide pool.
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GAETANI, Gian F., Anna M. FERRARIS, Paola SANNA, and Henry N. KIRKMAN. "A novel NADPH:(bound) NADP+ reductase and NADH:(bound) NADP+ transhydrogenase function in bovine liver catalase." Biochemical Journal 385, no. 3 (January 24, 2005): 763–68. http://dx.doi.org/10.1042/bj20041495.

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Many catalases have the shared property of containing bound NADPH and being susceptible to inactivation by their own substrate, H2O2. The presence of additional (unbound) NADPH effectively prevents bovine liver and human erythrocytic catalase from becoming compound II, the reversibly inactivated state of catalase, and NADP+ is known to be generated in the process. The function of the bound NADPH, which is tightly bound in bovine liver catalase, has been unknown. The present study with bovine liver catalase and [14C]NADPH and [14C]NADH revealed that unbound NADPH or NADH are substrates for an internal reductase and transhydrogenase reaction respectively; the unbound NADPH or NADH cause tightly bound NADP+ to become NADPH without becoming tightly bound themselves. This and other results provide insight into the function of tightly bound NADPH.
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Xia, Weiliang, Zheng Wang, Qing Wang, Jin Han, Cuiping Zhao, Yunyi Hong, Lili Zeng, Le Tang, and Weihai Ying. "Roles of NAD / NADH and NADP+ / NADPH in Cell Death." Current Pharmaceutical Design 15, no. 1 (January 1, 2009): 12–19. http://dx.doi.org/10.2174/138161209787185832.

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Nozato, Naoko, Kenji Oda, Katsuyuki Yamato, Eiji Ohta, Miho Takemura, Kinya Akashi, Hideya Fukuzawa, and Kanji Ohyama. "Cotranscriptional expression of mitochondrial genes for subunits of NADH dehydrogenase, nad5, nad4, nad2, in Marchantia polymorpha." Molecular and General Genetics MGG 237, no. 3 (March 1993): 343–50. http://dx.doi.org/10.1007/bf00279437.

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Griendling, Kathy K., and Masuko Ushio-Fukai. "NADH/NADPH Oxidase and Vascular Function." Trends in Cardiovascular Medicine 7, no. 8 (November 1997): 301–7. http://dx.doi.org/10.1016/s1050-1738(97)00088-1.

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Marbaix, Alexandre Y., Georges Chehade, Gaëtane Noël, Pierre Morsomme, Didier Vertommen, Guido T. Bommer, and Emile Van Schaftingen. "Pyridoxamine-phosphate oxidases and pyridoxamine-phosphate oxidase-related proteins catalyze the oxidation of 6-NAD(P)H to NAD(P)+." Biochemical Journal 476, no. 20 (October 28, 2019): 3033–52. http://dx.doi.org/10.1042/bcj20190602.

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Abstract 6-NADH and 6-NADPH are strong inhibitors of several dehydrogenases that may form spontaneously from NAD(P)H. They are known to be oxidized to NAD(P)+ by mammalian renalase, an FAD-linked enzyme mainly present in heart and kidney, and by related bacterial enzymes. We partially purified an enzyme oxidizing 6-NADPH from rat liver, and, surprisingly, identified it as pyridoxamine-phosphate oxidase (PNPO). This was confirmed by the finding that recombinant mouse PNPO oxidized 6-NADH and 6-NADPH with catalytic efficiencies comparable to those observed with pyridoxine- and pyridoxamine-5′-phosphate. PNPOs from Escherichia coli, Saccharomyces cerevisiae and Arabidopsis thaliana also displayed 6-NAD(P)H oxidase activity, indicating that this ‘side-activity’ is conserved. Remarkably, ‘pyridoxamine-phosphate oxidase-related proteins’ (PNPO-RP) from Nostoc punctiforme, A. thaliana and the yeast S. cerevisiae (Ygr017w) were not detectably active on pyridox(am)ine-5′-P, but oxidized 6-NADH, 6-NADPH and 2-NADH suggesting that this may be their main catalytic function. Their specificity profiles were therefore similar to that of renalase. Inactivation of renalase and of PNPO in mammalian cells and of Ygr017w in yeasts led to the accumulation of a reduced form of 6-NADH, tentatively identified as 4,5,6-NADH3, which can also be produced in vitro by reduction of 6-NADH by glyceraldehyde-3-phosphate dehydrogenase or glucose-6-phosphate dehydrogenase. As 4,5,6-NADH3 is not a substrate for renalase, PNPO or PNPO-RP, its accumulation presumably reflects the block in the oxidation of 6-NADH. These findings indicate that two different classes of enzymes using either FAD (renalase) or FMN (PNPOs and PNPO-RPs) as a cofactor play an as yet unsuspected role in removing damaged forms of NAD(P).
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Marienfeld, J. R., and K. J. Newton. "The maize NCS2 abnormal growth mutant has a chimeric nad4-nad7 mitochondrial gene and is associated with reduced complex I function." Genetics 138, no. 3 (November 1, 1994): 855–63. http://dx.doi.org/10.1093/genetics/138.3.855.

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Abstract The molecular basis of the maternally inherited, heteroplasmic NCS2 mutant of maize was investigated. Analysis of the NCS2 mtDNA showed that it closely resembles the progenitor cmsT mitochondrial genome, except that the mutant genome contains a fused nad4-nad7 gene and is deleted for the small fourth exon of nad4. The rearrangement has occurred at a 16-bp repeat present in the third intron of the nad4 gene and in the second intron of the nad7 gene. Transcripts containing exon 4 of the nad4 gene are greatly reduced in mtRNA preparations from heteroplasmic NCS2 plants; larger transcripts are associated with the first three nad4 exons. Identical 5' ends of the nad4 transcripts have been mapped 396 and 247 bp upstream of the start codon in mtRNAs from both NCS2 and related non-NCS plants. The putative transcription termination signal of nad4 is deleted in mutant DNA, resulting in the production of the unique longer transcripts. The complex transcript pattern associated with nad7 is also altered in the mutant. Both nad4 and nad7 encode subunits of complex I (NADH dehydrogenase) of the mitochondrial electron transfer chain. Oxygen uptake experiments show that the functioning of complex I is specifically reduced in mitochondria isolated from NCS2 mutant plants.
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Dissertations / Theses on the topic "NADH"

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Roeschlaub, Carl Andrew. "The design and synthesis of novel reductively activated molecular sensors." Thesis, University of Surrey, 2000. http://epubs.surrey.ac.uk/843218/.

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NADH and NADPH are ubiquitous biological reducing agents essential for both respiration and biosynthesis. The discovery that increased pentose-phosphate pathway activity in cervical cancer cells leads to increased levels of NAD(P)H, emphasises the need for a sensitive detection system as an indication of cellular viability and vitality. The remit of this project was to design and synthesise a novel molecular sensor system whose emissive properties are "switched on" upon reduction by NAD(P)H. Research using the reducible, non-fluorescent dye, resazurin, has shown that, in the presence of a non-enzymic electron transfer agent phenazinium methosulphate (PMS)-NADH can effect reduction to the highly fluorescent dye resorufin. Mechanistic studies have shown that the reduction proceeds via a two-electron hydride transfer to the heterocyclic mediator, followed by a one electron transfer to the dye and disproportionation to furnish the final fluorescent product. It has been shown that direct reduction by NADH does not occur and that the reaction depends upon there being an electron transfer agent present. A new type of reagent for the detection of NAD(P)H has been synthesised, comprising a reducible heterocycle and a masked fluorophore. It has been shown that reduction of the precursor conjugate by NADH results in the release of a detectable fluorescent moiety methylumbelliferone. The synthesis of an analogous conjugate probe containing a known hindered dioxetane moiety is described. Prepared using a previously unreported route, the key vinyl ether intermediate is generated via a Wadsworth-Emmons reductive coupling of an alkoxy phosphonate to 2-adamantanone. Reduction by NADH and subsequent cleavage of a conjugate ether link generates an electron rich phenolate substituted dioxetane which is metastable, resulting in emission from the generated excited product. Work towards a dioxetane containing functionalised alkyl group for conjugation to a fluorophore is also outlined.
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Shuler, Elizabeth. "The effects of flavonoids on mitochondrial membrane-associated reduced pyridine nucleotide-utilizing systems of adult Hymenolepis diminuta (cestoda) and Ascaris suum (nematoda)." Bowling Green State University / OhioLINK, 2013. http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1367950138.

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Crowley, Louis J. "Structure-function studies of conserved sequence motifs of cytochrome b5 reductase." [Tampa, Fla] : University of South Florida, 2007. http://purl.fcla.edu/usf/dc/et/SFE0001913.

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Farooqi, Mohammed Junaid. "METHODS FOR IN SITU PIEZOPHYSIOLOGICAL STUDIES: OPTICAL SECTIONING VIA STRUCTURED ILLUMINATION AND FLUORESCENCE BASED CHARACTERIZATION OF NADH CONFORMATION." Oxford, Ohio : Miami University, 2009. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=miami1249225952.

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Melo, Ana Margarida Nunes Portugal Carvalho. "Characterization of NAD(P)H dehydrogenases from neurospora mitochondria." Doctoral thesis, Porto : Edição do Autor, 2001. http://hdl.handle.net/10216/64566.

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Melo, Ana Margarida Nunes Portugal Carvalho. "Characterization of NAD(P)H dehydrogenases from neurospora mitochondria." Tese, Porto : Edição do Autor, 2001. http://catalogo.up.pt/F?func=find-b&local_base=UPB01&find_code=SYS&request=000088166.

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Leman, Géraldine. "Régulation de la fonction mitochondriale par le rapport NADH/NAD+ : le rôle clef du complexe I." Thesis, Angers, 2014. http://www.theses.fr/2014ANGE0016/document.

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Le NAD+ apparaît comme un régulateur majeur du fonctionnement mitochondrial. En effet, ce cofacteur régule non seulement l’activité de nombreuses enzymes impliqués dans le métabolisme énergétique (enzymes de la β-oxydation des acides gras, du cycle de Krebs) mais joue également un rôle dans la production d’espèces réactives de l’oxygène (ROS). Le NAD+ est aussi le cofacteur des sirtuines, des enzymes déacétylases régulatrices notamment du métabolisme mitochondrial. De plus, la mitochondrie est l’organite au sein duquel la concentration en NAD+ est la plus élevée (jusqu’à 70% du NAD cellulaire). Le complexe I, qui possède une activité NADH déshydrogénase, pourrait être l’un des régulateurs majeurs du rapport NADH/NAD+ mitochondrial. L’objectif de ce travail de thèse a été d’étudier le rôle du rapport NADH/NAD+ mitochondrial dans le métabolisme énergétique et l’implication du complexe I dans les pathologies mitochondriales. Nous avons mis en évidence qu’une modulation du rapport NADH/NAD+ mitochondrial (augmentation par un activateur pharmacologique ou diminution consécutive à une mutation touchant une sous-unité du complexe I, modifie de manière drastique le métabolisme énergétique notamment en activant ou inhibant la protéine SIRT3, isoforme mitochondriale des sirtuines. Le complexe I semble jouer un rôle majeur dans cette modulation. Le resveratrol, ciblant le complexe I, ainsi que le NMN, un précurseur du NAD+, permettent de restaurer ce rapport et d’améliorer ainsi le métabolisme mitochondrial. Nos résultats suggèrent donc que le rapport NADH/NAD+ pourrait être une cible thérapeutique particulièrement intéressante dans les déficits du complexe I
NAD+ appears as a main regulator of the mitochondrial function. Indeed, this compound not only regulates the enzymatic activity of enzymes involved in energetic metabolism (fatty acid oxidation, tricarboxylic acid cycle) but is also involved in ROS production. NAD+ is also the cofactor of sirtuins, deacetylase enzymes, in particular regulating the mitochondrial function. Moreover, mitochondria sequester most of the cellular NAD+ (up to 70 %). The complex I, which possesses an NADH dehydrogenase activity, is thought to be the most important regualtor of the mitochondrial NADH/NAD+ ratio. The work presented here aimed at studying the role of the mitochondrial NADH/NAD+ ratio in mitochondrial metabolism and to test the involvement of the complex I in mitochondrial disorders. We show that a modulation of the mitochondrial NADH/NAD+ ratio (increase by a pharmacological agent or decrease in complex-I mutated fibroplasts) severely affects the mitochondrial energetic function especially by interacting with SIRT3 a mitochondrial sirtuin isoform. The NADH/NAD+ ratio is highly regulated by complex I activity. Resveratrol, which targets the complex I, as well as NMN, a NAD+ precursor, improves the mitochondrial NADH/NAD+ ratio and consequently increases the mitochondrial metabolism. Our results strongly suggest that the mitochondrial NADH/NAD+ ratio could be an interesting therapeutic target especially in complex I- deficient patients
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Marx, Stefanie. "Die Co-Evolution der Cytochrom-c-Reduktase und der mitochondrialen Prozessierungsprotease." [S.l. : s.n.], 2000. http://deposit.ddb.de/cgi-bin/dokserv?idn=960312099.

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Khalily, Mohammad Aref. "Synthesis Of New Mediators For Electrochemical Nad/nadh Recycling." Master's thesis, METU, 2011. http://etd.lib.metu.edu.tr/upload/12612961/index.pdf.

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The synthesis of enantiopure compounds can be achieved by using dehydrogenases as biocatalysts. For instance, reduction reactions of prochiral compounds (ketones, aldehydes and nitriles) into chiral compounds can be achieved by dehydrogenases. These dehydrogenases are cofactor dependent where cofactor is Nicotinamide Adenin Dinucleotite having some restrictions that confines usage of dehydrogenases in organic synthesis including instability of cofactor in water and high cost. Therefore, suitable recycling methods are required and developed which are enzymatic and electrochemical. We will use an electrochemical approach for the regeneration of reduced co-factors. All active compounds
mediator, cofactor and enzyme, will be immobilized on the electrode surface of the constructed reactor surface. Therefore only educts and products will exist in the reactor medium. A gas diffusion electrode will be employed as a counter electrode
which delivers clear protons to the system. Mediator will carry electrons to the cofactor for cofactor regeneration. Then, enzyme will utilize the cofactor and change the substrates to the products in high stereoselectivity. Our aim in this project is the synthesis of mediators and suitable linkers for enzyme, cofactor and mediator immobilization. In the first part of the study, mediators were synthesized which are pentamethylcyclopentadienyl rhodium bipyridine complexes. In the second part of the study, a conductive monomer (SNS) and linker were synthesized for immobilization of the enzyme. In the last part of the study, the reaction of galactitol dehydrogenase with monomer (SNS) was achieved.
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Meijers, Rob. "The activation of NADH in liver alcohol dehydrogenase." [S.l. : Amsterdam : s.n.] ; Universiteit van Amsterdam [Host], 2001. http://dare.uva.nl/document/60889.

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Books on the topic "NADH"

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Mayevsky, Avraham. Mitochondrial Function In Vivo Evaluated by NADH Fluorescence. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-16682-7.

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George, Christina L. Characterisation of the NADH dehydrogenase from Paracoccus denitrificans. Birmingham: University of Birmingham, 1986.

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Birkmayer, Georg D. NADH, the biological hydrogen: The secret of our life energy. Laguna Beach, CA: Basic Health Publications, 2009.

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Singh, Ranji. The modulation of NADPH, NADH, and a-ketoglutarate in Pseudomonas fluorescens exposed to oxidative stress. Sudbury, Ont: Laurentian University, School of Graduate Studies, 2005.

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G, Cochrane Charles, and Gimbrone Michael A, eds. Biological oxidants: Generation and injurious consequences. San Diego: Academic Press, 1992.

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Birkmayer, Georg D. NADH the energizing coenzyme: How an important, yet little-known coenzyme enhances cellular energy in brain and body functions. New Canaan, CT: Keats Pub., 1998.

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Chen, Feng-Ling. Studies on the two isoenzymes of NADH-dependent glutamate synthase in root nodules of "Phaseolus vulgaris L". [s.l.]: typescript, 1988.

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David, Dolphin, Avramović Olga, and Poulson Rozanne, eds. Pyridine nucleotide coenzymes: Chemical, biochemical, and medical aspects. New York: Wiley, 1987.

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Liyanage, Anudini Chandrika. The NADH-specific [beta]-ketoacyl (acyl carrier protein) reductase from the plastids of avocado (Persea americana) fruit mesocarp. Birmingham: University of Birmingham, 1993.

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Asamara nada-nadī. Guwāhāṭi: Anveshā, 2014.

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Book chapters on the topic "NADH"

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Peretó, Juli. "NADH, NADPH." In Encyclopedia of Astrobiology, 1105. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-11274-4_1039.

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Peretó, Juli. "NADH, NADPH." In Encyclopedia of Astrobiology, 1655. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-44185-5_1039.

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Peretó, Juli. "NADH, NADPH." In Encyclopedia of Astrobiology, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27833-4_1039-2.

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Peretó, Juli. "NADH, NADPH." In Encyclopedia of Astrobiology, 2040. Berlin, Heidelberg: Springer Berlin Heidelberg, 2023. http://dx.doi.org/10.1007/978-3-662-65093-6_1039.

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Krüger, Susanne, and Michael Böttger. "NADH or NADPH ?" In Plasma Membrane Oxidoreductases in Control of Animal and Plant Growth, 105–14. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-8029-0_12.

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Riley, David S. "Nadidum (NADH)." In Materia Medica of New and Old Homeopathic Medicines, 171–72. Berlin, Heidelberg: Springer Berlin Heidelberg, 2018. http://dx.doi.org/10.1007/978-3-662-54192-0_49.

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Schomburg, D., M. Salzmann, and D. Stephan. "NADH peroxidase." In Enzyme Handbook 7, 721–25. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78521-4_137.

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Schomburg, D., M. Salzmann, and D. Stephan. "NADH dehydrogenase." In Enzyme Handbook 7, 395–401. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78521-4_77.

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Riley, David S. "Nadidum (NADH)." In Materia Medica of New and Old Homeopathic Medicines, 189–90. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-030-65920-2_57.

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Schomburg, Dietmar, and Dörte Stephan. "NADH kinase." In Enzyme Handbook 13, 1027–30. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-59176-1_195.

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Conference papers on the topic "NADH"

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Lim, Shey-Li. "Real-time monitoring of the dynamics of NADPH and NADH/NAD+ ratio in Arabidopsis thaliana during photosynthesis." In ASPB PLANT BIOLOGY 2020. USA: ASPB, 2020. http://dx.doi.org/10.46678/pb.20.1374653.

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Schramm, Werner, Wolfgang Hoehne, Herbert G. Stepp, and Andreas Leunig. "Noninvasive NADH measurements for clinical applications." In BiOS Europe '96, edited by Hans-Jochen Foth, Renato Marchesini, and Halina Podbielska. SPIE, 1996. http://dx.doi.org/10.1117/12.260634.

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von Ketteler, A., D. Siegberg, D. P. Herten, C. Horn, and W. Petrich. "Fluorescence lifetime-based glucose sensor using NADH." In SPIE BiOS, edited by Robert J. Nordstrom and Gerard L. Coté. SPIE, 2012. http://dx.doi.org/10.1117/12.908834.

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Coremans, J. M. C. C., C. Ince, Hajo A. Bruining, and Gerwin J. Puppels. "NADH fluorescence/UV reflectance ratio provides a semi-quantitative measure for NADH fluorometry of blood-perfused rat heart." In BiOS Europe '96, edited by Hans-Jochen Foth, Renato Marchesini, and Halina Podbielska. SPIE, 1996. http://dx.doi.org/10.1117/12.260640.

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Bezludnaya, Irina S., Svetlana P. Chernova, and Alexander B. Pravdin. "Photobleaching of fluorescence of NADH in gelatin gel." In Saratov Fall Meeting '99, edited by Valery V. Tuchin, Dmitry A. Zimnyakov, and Alexander B. Pravdin. SPIE, 2000. http://dx.doi.org/10.1117/12.381500.

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Schramm, Werner, and M. Naundorf. "NADH-fluorescence in medical diagnostics: first experimental results." In Berlin - DL tentative, edited by Lars O. Svaasand. SPIE, 1991. http://dx.doi.org/10.1117/12.48226.

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Rueck, Angelika C. "FLIM based optical redox ratio of NADH, FAD and FMN versus metabolic index of NADH. Improved algorithms for metabolic imaging." In Multiphoton Microscopy in the Biomedical Sciences XXI, edited by Ammasi Periasamy, Peter T. So, and Karsten König. SPIE, 2021. http://dx.doi.org/10.1117/12.2589315.

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Dolgikh, Angelina, Olga Stelmashchuk, Andrey Vinokurov, Evgeny Zherebtsov, and Andrey Abramov. "Measurements of mitochondrial NADH pool and NADH production rate in acute brain slices and primary cell cultures using live cell imaging." In Saratov Fall Meeting 2020: Optical and Nano-Technologies for Biology and Medicine, edited by Valery V. Tuchin and Elina A. Genina. SPIE, 2021. http://dx.doi.org/10.1117/12.2590804.

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Díaz, Paola Monterroso, and Narasimhan Rajaram. "Fluorescence Lifetime Imaging of NADH and FAD in Ex Vivo Young and Old Mouse Cortical Tissue." In Optical Molecular Probes, Imaging and Drug Delivery. Washington, D.C.: Optica Publishing Group, 2023. http://dx.doi.org/10.1364/omp.2023.om2e.2.

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Young and old murine cortical tissue in fresh, snap frozen, and DMSO-preserved form were investigated with two-photon microscopy. Shorter mean NADH and FAD lifetimes were found in old cortical tissue compared to young.
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Raju, Gagan, Gireesh Gangadharan, Vishwanath Managuli, KK Mahato, and Nirmal Mazumder. "Unveiling metabolic changes in ex vivo brain tissue through intrinsic NADH autofluorescence imaging using the advanced non-linear optical modality." In Laser Science. Washington, D.C.: Optica Publishing Group, 2023. http://dx.doi.org/10.1364/ls.2023.ld1.8.

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Study explores the application of two photon fluorescence lifetime imaging modality to reveal metabolic alterations in ex vivo brain tissue by analyzing intrinsic NADH autofluorescence, providing valuable insights into brain metabolism and potential disease mechanisms.
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Reports on the topic "NADH"

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Barstad, Louise. Purification and characterization of NADH oxidase and peroxidase from Lactobacillus casei. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.2785.

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Xi, Wenjun. Determination of NAD+ and NADH level in a Single Cell Under H2O2 Stress by Capillary Electrophoresis. Office of Scientific and Technical Information (OSTI), January 2008. http://dx.doi.org/10.2172/939381.

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Bagwell, Kyle, Robert Staiger, and Ali Yurukoglu. "Nash-in-Nash" Tariff Bargaining with and without MFN. Cambridge, MA: National Bureau of Economic Research, October 2017. http://dx.doi.org/10.3386/w23894.

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Collard-Wexler, Allan, Gautam Gowrisankaran, and Robin Lee. “Nash-in-Nash” Bargaining: A Microfoundation for Applied Work. Cambridge, MA: National Bureau of Economic Research, October 2014. http://dx.doi.org/10.3386/w20641.

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Alioğulları, Zeynel Harun, and Mehmet Barlo. Entropic selection of Nash equilibrium. Sabancı University, February 2012. http://dx.doi.org/10.5900/su_fass_wp.2012.18910.

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Christopher, Anita, S. K. Singh, Rakesh Sarwal, Neena Bhatia, Robert Johnston, William Joe, Esha Sarswat, Purnima Menon, and Phuong Hong Nguyen. State nutrition profile: Tamil Nadu. New Delhi, India: International Food Policy Research Institute, 2022. http://dx.doi.org/10.2499/p15738coll2.135305.

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Chatterjee, Krishnendu, Marcin Jurdzinski, and Rupak Majumdar. On Nash Equilibria in Stochastic Games. Fort Belvoir, VA: Defense Technical Information Center, October 2003. http://dx.doi.org/10.21236/ada603326.

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Bogner, Alexander. Nach Corona. Reflexionen für zukünftige Krisen. Verlag der Österreichischen Akademie der Wissenschaften, December 2023. http://dx.doi.org/10.1553/978oeaw95696.

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Welche Lehren lassen sich aus der Corona-Pandemie für den Umgang mit zukünftigen Krisen ziehen? Dieser Band bietet konkrete Antworten. Er bündelt die Ergebnisse des Corona-Aufarbeitungsprozesses, der von der österreichischen Bundesregierung im Frühjahr 2023 angestoßen wurde. Im Mittelpunkt von fünf sozialwissenschaftlichen Analysen stehen politisch hochkontroverse Themen wie die Impfpflicht und die Schulschließungen. Die Rolle der Medien, das Problem der Wissenschaftsskepsis und die Organisation wissenschaftlicher Politikberatung in Krisenzeiten sind weitere Themenschwerpunkte. Empfehlungen für zukünftige Krisen wurden auch von Bürgerinnen und Bürgern im Rahmen österreichweiter Dialogveranstaltungen formuliert. Die reichhaltige Dokumentation dieses Dialogprozesses rundet den Band ab.
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Felmy, A. R., D. Rai, and R. W. Fulton. The solubility of Cr(OH){sub 3}(am) in concentrated NaOH and NaOH-NaNO{sub 3} solutions. Office of Scientific and Technical Information (OSTI), August 1994. http://dx.doi.org/10.2172/10107403.

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Pan, Yaodong, Tankut Acarman, and Umit Ozguner. Nash Solution by Extremum Seeking Control Approach. Fort Belvoir, VA: Defense Technical Information Center, December 2002. http://dx.doi.org/10.21236/ada409514.

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