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Статті в журналах з теми "NADH-dehydrogenase activity"

Автор: Grafiati

Опубліковано: 21 лютого 2024

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1

Murray, G. I., M. D. Burke, and S. W. Ewen. "Enzyme histochemical demonstration of NADH dehydrogenase on resin-embedded tissue." Journal of Histochemistry & Cytochemistry 36, no. 7 (1988): 815–19. http://dx.doi.org/10.1177/36.7.3385192.

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We describe a method for enzyme histochemical demonstration of NADH dehydrogenase in cold (4 degrees C)-processed resin-embedded tissue. The effects on NADH dehydrogenase activity of processing tissue through a variety of dehydrating agents and embedding in three different acrylic resins were evaluated. The optimal procedure to maintain NADH dehydrogenase activity used a short (3-hr) fixation in 1% paraformaldehyde solution, followed by dehydration in acetone and embedding in glycol methacrylate resin. Embedding of tissue in resin combined preservation and accurate localization of NADH dehydro

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2

Small, W. Curtis, and Lee McAlister-Henn. "Identification of a Cytosolically Directed NADH Dehydrogenase in Mitochondria of Saccharomyces cerevisiae." Journal of Bacteriology 180, no. 16 (1998): 4051–55. http://dx.doi.org/10.1128/jb.180.16.4051-4055.1998.

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ABSTRACT The reoxidation of NADH generated in reactions within the mitochondrial matrix of Saccharomyces cerevisiae is catalyzed by an NADH dehydrogenase designated Ndi1p (C. A. M. Marres, S. de Vries, and L. A. Grivell, Eur. J. Biochem. 195:857–862, 1991). Gene disruption analysis was used to examine possible metabolic functions of two proteins encoded by open reading frames having significant primary sequence similarity to Ndi1p. Disruption of the gene designated NDH1 results in a threefold reduction in total mitochondrial NADH dehydrogenase activity in cells cultivated with glucose and in a

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3

Hayashi, Takeshi, Tsuyoshi Kato, and Kensuke Furukawa. "Respiratory Chain Analysis of Zymomonas mobilis Mutants Producing High Levels of Ethanol." Applied and Environmental Microbiology 78, no. 16 (2012): 5622–29. http://dx.doi.org/10.1128/aem.00733-12.

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ABSTRACTWe previously isolated respiratory-deficient mutant (RDM) strains ofZymomonas mobilis, which exhibited greater growth and enhanced ethanol production under aerobic conditions. These RDM strains also acquired thermotolerance. Morphologically, the cells of all RDM strains were shorter compared to the wild-type strain. We investigated the respiratory chains of these RDM strains and found that some RDM strains lost NADH dehydrogenase activity, whereas others exhibited reduced cytochromebd-type ubiquinol oxidase or ubiquinol peroxidase activities. Complementation experiments restored the wi

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4

Thiagalingam, Sam, and Tsanyen Yang. "Purification and characterization of NADH dehydrogenase from Bacillus megaterium." Canadian Journal of Microbiology 39, no. 9 (1993): 826–33. http://dx.doi.org/10.1139/m93-123.

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NADH dehydrogenase of Bacillus megaterium was isolated from the sonicate soluble fraction. The enzyme was purified approximately 61-fold by a combination of ammonium sulfate fractionation and column chromatography on DEAE-Sephadex and hydroxyapatite. The purified enzyme has an apparent molecular weight of 42 000 as determined by SDS-polyacrylamide gel electrophoresis and activity staining for NADH-MTT (3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl-tetrazolium bromide) oxidoreductase. The enzyme is specific for NADH and has a pH optimum of 7.5–7.8. The apparent Km values for NADH are 15.7, 34.8, an

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5

Marchenko, M. M., and O. N. Voloshchuk. "The state of the mitochondrial energy-supplying system of blood leukocytes in the dynamics of guerin's carcinoma growth under the low-level irradiation conditions." Biomeditsinskaya Khimiya 60, no. 6 (2014): 631–35. http://dx.doi.org/10.18097/pbmc20146006631.

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Mitochondrial NADH-dehydrogenase, succinate dehydrogenase and cytochrome oxidase activities of peripheral blood leukocytes of rats with the grafted Guerin's carcinoma were studied in the dynamics of oncogenesis under the conditions of the preliminary low-level irradiation. Tumor growth was accompanied by a decrease in NADH-dehydrogenase activity, an increase of succinate dehydrogenase activity. Cytochrome oxidase activity of leucocytes remained at the control level up to the terminal stages of tumor growth. Preliminary low-level irradiation of the tumor bearing animals caused a tendency to the

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6

Huston, Scott, John Collins, Fangfang Sun, et al. "An activity transition from NADH dehydrogenase to NADH oxidase during protein denaturation." Biotechnology and Applied Biochemistry 65, no. 3 (2017): 286–93. http://dx.doi.org/10.1002/bab.1607.

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7

Miesel, Lynn, Torin R. Weisbrod, Jovita A. Marcinkeviciene, Robert Bittman, and William R. Jacobs. "NADH Dehydrogenase Defects Confer Isoniazid Resistance and Conditional Lethality in Mycobacterium smegmatis." Journal of Bacteriology 180, no. 9 (1998): 2459–67. http://dx.doi.org/10.1128/jb.180.9.2459-2467.1998.

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ABSTRACT Isoniazid (INH) is a highly effective drug used in the treatment and prophylaxis of Mycobacterium tuberculosis infections. Resistance to INH in clinical isolates has been correlated with mutations in the inhA, katG, andahpC genes. In this report, we describe a new mechanism for INH resistance in Mycobacterium smegmatis. Mutations that reduce NADH dehydrogenase activity (Ndh; type II) cause multiple phenotypes, including (i) coresistance to INH and a related drug, ethionamide; (ii) thermosensitive lethality; and (iii) auxotrophy. These phenotypes are corrected by expression of one of t

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8

Chapuy-Regaud, Sabine, Frédérique Duthoit, Laurence Malfroy-Mastrorillo, Pierre Gourdon, Nic D. Lindley, and Marie-Claude Trombe. "Competence Regulation by Oxygen Availability and by Nox Is Not Related to Specific Adjustment of Central Metabolism inStreptococcus pneumoniae." Journal of Bacteriology 183, no. 9 (2001): 2957–62. http://dx.doi.org/10.1128/jb.183.9.2957-2962.2001.

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ABSTRACT In Streptococcus pneumoniae oxygen availability is a major determinant for competence development in exponentially growing cultures. NADH oxidase activity is required for optimal competence in cultures grown aerobically. The implication of oxidative metabolism and more specifically of Nox on central metabolism has been examined. Glycolytic flux throughout exponential growth revealed homolactic fermentation with a lactate production/glucose utilization ratio close to 2, whatever the aerobiosis level of the culture. Loss-of-function mutations in nox, which encodes NADH oxidase, did not

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9

Powell, Charles S., and Robert M. Jackson. "Mitochondrial complex I, aconitase, and succinate dehydrogenase during hypoxia-reoxygenation: modulation of enzyme activities by MnSOD." American Journal of Physiology-Lung Cellular and Molecular Physiology 285, no. 1 (2003): L189—L198. http://dx.doi.org/10.1152/ajplung.00253.2002.

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Both NADH dehydrogenase (complex I) and aconitase are inactivated partially in vitro by superoxide ([Formula: see text]) and other oxidants that cause loss of iron from enzyme cubane (4Fe-4S) centers. We tested whether hypoxia-reoxygenation (H-R) by itself would decrease lung epithelial cell NADH dehydrogenase, aconitase, and succinate dehydrogenase (SDH) activities and whether transfection with adenoviral vectors expressing MnSOD (Ad.MnSOD) would inhibit oxidative enzyme inactivation and thus confirm a mechanism involving [Formula: see text]. Human lung carcinoma cells with alveolar epithelia

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10

Smyth, G. E., and B. A. Orsi. "Nitroreductase activity of NADH dehydrogenase of the respiratory redox chain." Biochemical Journal 257, no. 3 (1989): 859–63. http://dx.doi.org/10.1042/bj2570859.

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1. An NADH-dependent nitroreductase from the inner membrane of ox liver mitochondria copurified with Complex I of the respiratory redox chain (NADH:ubiquinone oxidoreductase, EC 1.6.5.3). 2. The corresponding nitroreductase from ox heart mitochondria co-purified with the NADH-cytochrome c reductase of Mahler, Sarkar & Vernon [(1952) J. Biol. Chem. 199, 585-597] [NADH: (acceptor) oxidoreductase, EC 1.6.99.3], a component of Complex I that contains the FMN. 3. The mitochondrial nitroreductase activity is attributed to the flavoprotein component of Complex I.

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11

Brass, Eric P., William R. Hiatt, Andrew W. Gardner, and Charles L. Hoppel. "Decreased NADH dehydrogenase and ubiquinol-cytochromec oxidoreductase in peripheral arterial disease." American Journal of Physiology-Heart and Circulatory Physiology 280, no. 2 (2001): H603—H609. http://dx.doi.org/10.1152/ajpheart.2001.280.2.h603.

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Peripheral arterial disease (PAD) is associated with muscle metabolic changes that may contribute to the disability in these patients. However, the biochemical defects in PAD have not been identified. The present study was undertaken to test the hypothesis that PAD is associated with specific defects in skeletal muscle electron transport chain activity. Seventeen patients with PAD and nine age-matched controls underwent gastrocnemius muscle biopsies. There were no differences in the mitochondrial content per gram of skeletal muscle as assessed by citrate synthase activity between the PAD patie

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12

Tsai, C. S. "Nitroreductase activity of heart lipoamide dehydrogenase." Biochemical Journal 242, no. 2 (1987): 447–52. http://dx.doi.org/10.1042/bj2420447.

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A novel reaction catalysed by lipoamide dehydrogenase is described. In the presence of NADH, lipoamide dehydrogenase reduces the nitro group of 4-nitropyridine and 4-nitropyridine N-oxide. The elution profiles from a DEAE-cellulose column for the dehydrogenase and nitroreductase activities are identical. Chemical modifications of critical amino acid residues suggest that the two activities share a common catalytic domain. Nitro reduction catalysed by lipoamide dehydrogenase was monitored spectrophotometrically and chromatographically. The major product from the enzymic reduction of 4-nitropyri

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13

Lopez de Felipe, Felix, Michiel Kleerebezem, Willem M. de Vos, and Jeroen Hugenholtz. "Cofactor Engineering: a Novel Approach to Metabolic Engineering in Lactococcus lactis by Controlled Expression of NADH Oxidase." Journal of Bacteriology 180, no. 15 (1998): 3804–8. http://dx.doi.org/10.1128/jb.180.15.3804-3808.1998.

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ABSTRACT NADH oxidase-overproducing Lactococcus lactis strains were constructed by cloning the Streptococcus mutans nox-2gene, which encodes the H2O-forming NADH oxidase, on the plasmid vector pNZ8020 under the control of the L. lactis nisA promoter. This engineered system allowed a nisin-controlled 150-fold overproduction of NADH oxidase at pH 7.0, resulting in decreased NADH/NAD ratios under aerobic conditions. Deliberate variations on NADH oxidase activity provoked a shift from homolactic to mixed-acid fermentation during aerobic glucose catabolism. The magnitude of this shift was directly

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14

Cheema-Dhadli, S., F. A. Halperin, K. Sonnenberg, V. MacMillan, and M. L. Halperin. "Regulation of ethanol metabolism in the rat." Biochemistry and Cell Biology 65, no. 5 (1987): 458–66. http://dx.doi.org/10.1139/o87-059.

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The purpose of these experiments was to examine the factors which regulate ethanol metabolism in vivo. Since the major pathway for ethanol removal requires flux through hepatic alcohol dehydrogenase, the activity of this enzyme was measured and found to be 2.9 μmol/(min∙g liver). Ethanol disappearance was linear for over 120 min in vivo and the blood ethanol fell 0.1 mM/min; this is equivalent to removing 20 μmol ethanol/min and would require that flux through alcohol dehydrogenase be about 60% of its measured maximum velocity. To test whether ethanol metabolism was limited by the rate of remo

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15

Soloveva, Ekaterina R., O. V. Karaseva, M. F. Vasileva, S. V. Petrichuk, I. V. Samokhina, and K. E. Khmel’nitskiy. "THE EFFECT OF MICROWAVES OF A DECIMETER RANGE ON THE FUNCTIONAL ACTIVITY OF MITOCHONDRIA IN DESTRUCTIVE APPENDICITIS IN CHILDREN." Russian Journal of Pediatric Surgery 22, no. 2 (2018): 72–77. http://dx.doi.org/10.18821/1560-9510-2018-22-2-72-77.

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Introduction. The article assessed the effectiveness of decimeter wave therapy (DWT) in the postoperative period after laparoscopic appendectomy for destructive appendicitis in children. Authors relate positive clinical effects with the activation of mitochondrial energy metabolism. Material and methods. The study included 132 patients (46 destructive appendicitis cases, 86 h appendicular peritonitis patients). Among them, there were 75 (56.8 percent) boys and 57 (43.2 percent) girls aged of from 3 to 17 years (mean age of 10.7 ± 3.07 years). Patients of the main group received DWT procedures

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16

Kim, Youngnyun, L. O. Ingram, and K. T. Shanmugam. "Dihydrolipoamide Dehydrogenase Mutation Alters the NADH Sensitivity of Pyruvate Dehydrogenase Complex of Escherichia coli K-12." Journal of Bacteriology 190, no. 11 (2008): 3851–58. http://dx.doi.org/10.1128/jb.00104-08.

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ABSTRACT Under anaerobic growth conditions, an active pyruvate dehydrogenase (PDH) is expected to create a redox imbalance in wild-type Escherichia coli due to increased production of NADH (>2 NADH molecules/glucose molecule) that could lead to growth inhibition. However, the additional NADH produced by PDH can be used for conversion of acetyl coenzyme A into reduced fermentation products, like alcohols, during metabolic engineering of the bacterium. E. coli mutants that produced ethanol as the main fermentation product were recently isolated as derivatives of an ldhA pflB double mutant. In

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17

Schempp, H., H. Ulrich, and E. F. Elstner. "Stereospecific Reduction of /R(+)-Thioctic Acid by Porcine Heart Lipoamide Dehydrogenase/Diaphorase." Zeitschrift für Naturforschung C 49, no. 9-10 (1994): 691–92. http://dx.doi.org/10.1515/znc-1994-9-1023.

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Abstract R(+)-thioctic acid is the naturally occurring cofactor in α-ketoacid dehydrogenases. We show both photo metrically by NADH + H+ oxidation and by HPLC product analysis that this enantiomer is rapidly reduced by NADH + H+ catalyzed by porcine heart lipoamide dehydrogenase/diaphorase. The racemate exhibits approxi mately 40% activity as compared to the R (+) form while the S (-) enantiomer photometrically shows little activity and yields no detectable reduced lipoic acid.

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18

Bakker, Barbara M., Christoffer Bro, Peter Kötter, Marijke A. H. Luttik, Johannes P. van Dijken, and Jack T. Pronk. "The Mitochondrial Alcohol Dehydrogenase Adh3p Is Involved in a Redox Shuttle in Saccharomyces cerevisiae." Journal of Bacteriology 182, no. 17 (2000): 4730–37. http://dx.doi.org/10.1128/jb.182.17.4730-4737.2000.

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ABSTRACT NDI1 is the unique gene encoding the internal mitochondrial NADH dehydrogenase of Saccharomyces cerevisiae. The enzyme catalyzes the transfer of electrons from intramitochondrial NADH to ubiquinone. Surprisingly, NDI1is not essential for respiratory growth. Here we demonstrate that this is due to in vivo activity of an ethanol-acetaldehyde redox shuttle, which transfers the redox equivalents from the mitochondria to the cytosol. Cytosolic NADH can be oxidized by the external NADH dehydrogenases. Deletion of ADH3, encoding mitochondrial alcohol dehydrogenase, did not affect respiratory

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19

Reed, David W., Jack Millstein, and Patricia L. Hartzell. "H2O2-Forming NADH Oxidase with Diaphorase (Cytochrome) Activity from Archaeoglobus fulgidus." Journal of Bacteriology 183, no. 24 (2001): 7007–16. http://dx.doi.org/10.1128/jb.183.24.7007-7016.2001.

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ABSTRACT An enzyme exhibiting NADH oxidase (diaphorase) activity was isolated from the hyperthermophilic sulfate-reducing anaerobeArchaeoglobus fulgidus. N-terminal sequence of the protein indicates that it is coded for by open reading frame AF0395 in theA. fulgidus genome. The gene AF0395 was cloned and its product was purified from Escherichia coli. Like the native NADH oxidase (NoxA2), the recombinant NoxA2 (rNoxA2) has an apparent molecular mass of 47 kDa, requires flavin adenine dinucleotide for activity, has NADH-specific activity, and is thermostable. Hydrogen peroxide is the product of

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20

Sales, Cristina R. G., Anabela Bernardes da Silva, and Elizabete Carmo-Silva. "Measuring Rubisco activity: challenges and opportunities of NADH-linked microtiter plate-based and 14C-based assays." Journal of Experimental Botany 71, no. 18 (2020): 5302–12. http://dx.doi.org/10.1093/jxb/eraa289.

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Abstract Rubisco is central to carbon assimilation, and efforts to improve the efficiency and sustainability of crop production have spurred interest in phenotyping Rubisco activity. We tested the hypothesis that microtiter plate-based methods provide comparable results to those obtained with the radiometric assay that measures the incorporation of 14CO2 into 3-phosphoglycerate (3-PGA). Three NADH-linked assays were tested that use alternative coupling enzymes: glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and glycerolphosphate dehydrogenase (GlyPDH); phosphoenolpyruvate carboxylase (PEPC)

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21

Pearson, J. K., and D. W. Sickles. "Enzyme activity changes in rat soleus motoneurons and muscle after synergist ablation." Journal of Applied Physiology 63, no. 6 (1987): 2301–8. http://dx.doi.org/10.1152/jappl.1987.63.6.2301.

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Quantitative enzyme histochemical methods have been used to determine the effect of ablation of synergists on the oxidative metabolism of the alpha-motoneurons and muscle fibers of the rat soleus. Sixty days postablation, the NADH-tetrazolium reductase (NADH-TR) activity of soleus motoneurons decreased 12.5% from 0.327 +/- 0.005 (mean +/- SE; optical density units) to 0.286 +/- 0.007. In the muscle fibers, the alpha-glycerophosphate dehydrogenase activity (glycolytic enzyme) decreased from 0.114 +/- 0.010 to 0.074 +/- 0.009, a change of 35.1%, and the NADH-TR activity decreased 21.2% from 0.34

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22

Huo, Heyu, Guangxiao Yao, and Shizhen Wang. "Economy Assessment for the Chiral Amine Production with Comparison of Reductive Amination and Transamination Routes by Multi-Enzyme System." Catalysts 10, no. 12 (2020): 1451. http://dx.doi.org/10.3390/catal10121451.

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Chiral amines are key building blocks for pharmaceuticals. Economic assessment of commercial potential of bioprocesses is needed for guiding research. Biosynthesis of (S)-α-methylbenzylamine (MBA) was selected as case study. For transamination route, transaminase coupled with glucose dehydrogenase and lactate dehydrogenase catalyzed the reaction with NADH (Nicotinamide adenine dinucleotide) regeneration. Amine dehydrogenase coupled with NADH oxidase, which catalyzed the reductive amination process. Comparison of biosynthesis cost by reductive amination and transamination routes was carried out

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23

Кислова, О. В. "ВПЛИВ ЗАМІЩЕННОГО НІКОТИНАМІДУ ТА ЙОГО МОЖЛИВИХ МЕТАБОЛІТІВ НА АКТИВНІСТЬ ФЕРМЕНТІВ ОБМІНУ ЕТАНОЛУ". Bulletin of the Kyiv National University of Technologies and Design. Technical Science Series 144, № 2 (2020): 98–104. http://dx.doi.org/10.30857/1813-6796.2020.2.10.

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To study the influence of N-phenyl-N-(1-cyclopropylethyl)nicotinamide and its possible metabolites: hydrochlorides of N-(1-cyclopropylethyl)amine and N-phenyl-N-(1-cyclopropylethyl)amine - on the activity of main ethanol oxidation enzymes in vitro and kinetic nature of their interaction. The studies were carried out using alcohol dehydrogenase and aldehyde dehydrogenase of rat liver subcellular fractions, which were obtained by differential centrifugation. The enzyme activity was determined spectrophotometrically. The kinetic nature of alcohol dehydrogenase and isozyme form of aldehyde dehydro

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24

Singh, Ranji, Ryan J. Mailloux, Simone Puiseux-Dao, and Vasu D. Appanna. "Oxidative Stress Evokes a Metabolic Adaptation That Favors Increased NADPH Synthesis and Decreased NADH Production in Pseudomonas fluorescens." Journal of Bacteriology 189, no. 18 (2007): 6665–75. http://dx.doi.org/10.1128/jb.00555-07.

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ABSTRACT The fate of all aerobic organisms is dependent on the varying intracellular concentrations of NADH and NADPH. The former is the primary ingredient that fuels ATP production via oxidative phosphorylation, while the latter helps maintain the reductive environment necessary for this process and other cellular activities. In this study we demonstrate a metabolic network promoting NADPH production and limiting NADH synthesis as a consequence of an oxidative insult. The activity and expression of glucose-6-phosphate dehydrogenase, malic enzyme, and NADP+-isocitrate dehydrogenase, the main g

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25

Sangiorgi, S., M. Mochi, R. Riva, et al. "Abnormal Platelet Mitochondrial Function in Patients Affected by Migraine With and Without Aura." Cephalalgia 14, no. 1 (1994): 21–23. http://dx.doi.org/10.1046/j.1468-2982.1994.1401021.x.

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To investigate energy metabolism in migraine, we determined platelet mitochondrial enzyme activities in 40 patients with migraine with aura and in 40 patients with migraine without aura during attack-free intervals and in 24 healthy control subjects. NADH-dehydrogenase, citrate synthase and cytochrome-c-oxidase activities in both patient groups were significantly lower than in controls ( p < 0.01), while NADH-cytochrome-c-reductase activity was reduced only in migraine with aura ( p < 0.01). No alteration in succinate-dehydrogenase was observed. Monoamine-oxidase activity differed betwee

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26

Jensen, Manfred, Guido B. Feige, and Anna Waterkotte. "Mannitol-1-Phosphate Dehydrogenase in Pseudevernia Furfuracea." Lichenologist 23, no. 2 (1991): 187–96. http://dx.doi.org/10.1017/s0024282991000336.

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AbstractMannitol-1-phosphate dehydrogenase [EC 1.1.1.17] activity was demonstrated in extracts of Pseudevernia furfuracea and Hypogymnia physodes. The reaction was found to be highly substrate specific for fructose-6-phosphate/NADH or mannitol-1-phosphate/NAD+. The pH optimum for fructose-6-phosphate reduction was 7.1, and apparent Km values were 1.2 mM for fructose-6-phosphate and 20 μM for NADH. The reaction did not require Mg++ or Ca++. For conversion of mannitol-1-phosphate into mannitol, the occurrence of mannitol-1-phosphatase in Pseudevernia furfuracea is postulated.

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27

Ke, Dangyang, Elhadi Yahia, Betty Hess, Lili Zhou, and Adel A. Kader. "Regulation of Fermentative Metabolism in Avocado Fruit under Oxygen and Carbon Dioxide Stresses." Journal of the American Society for Horticultural Science 120, no. 3 (1995): 481–90. http://dx.doi.org/10.21273/jashs.120.3.481.

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`Hass' avocado (Persea americana Mill.) fruit were kept in air, 0.25% O2 (balance N2), 20 % O2 + 80% CO2, or 0.25% O2 + 80% CO2 (balance N2) at 20C for up to 3 days to study the regulation of fermentative metabolism. The 0.25% 02 and 0.25% 02 + 80% CO2 treatments caused accumulations of acetaldehyde and ethanol and increased NADH concentration, but decreased NAD level. The 20% O2 + 80% CO2 treatment slightly increased acetaldehyde and ethanol concentrations without significant effects on NADH and NAD levels. Lactate accumulated in avocadoes kept in 0.25 % 02. The 80% CO, (added to 0.25% O2) di

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28

DUARTE, Margarida, Markus PETERS, Ulrich SCHULTE, and Arnaldo VIDEIRA. "The internal alternative NADH dehydrogenase of Neurospora crassa mitochondria." Biochemical Journal 371, no. 3 (2003): 1005–11. http://dx.doi.org/10.1042/bj20021374.

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An open reading frame homologous with genes of non-proton-pumping NADH dehydrogenases was identified in the genome of Neurospora crassa. The 57 kDa NADH:ubiquinone oxidoreductase acts as internal (alternative) respiratory NADH dehydrogenase (NDI1) in the fungal mitochondria. The precursor polypeptide includes a pre-sequence of 31 amino acids, and the mature enzyme comprises one FAD molecule as a prosthetic group. It catalyses specifically the oxidation of NADH. Western blot analysis of fungal mitochondria fractionated with digitonin indicated that the protein is located at the inner face of th

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29

BOWKER-KINLEY, Melissa M., I. Wilhelmina DAVIS, Pengfei WU, A. Robert HARRIS, and M. Kirill POPOV. "Evidence for existence of tissue-specific regulation of the mammalian pyruvate dehydrogenase complex." Biochemical Journal 329, no. 1 (1998): 191–96. http://dx.doi.org/10.1042/bj3290191.

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Tissue distribution and kinetic parameters for the four isoenzymes of pyruvate dehydrogenase kinase (PDK1, PDK2, PDK3 and PDK4) identified thus far in mammals were analysed. It appeared that expression of these isoenzymes occurs in a tissue-specific manner. The mRNA for isoenzyme PDK1 was found almost exclusively in rat heart. The mRNA for PDK3 was most abundantly expressed in rat testis. The message for PDK2 was present in all tissues tested but the level was low in spleen and lung. The mRNA for PDK4 was predominantly expressed in skeletal muscle and heart. The specific activities of the isoe

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30

Dickinson, F. M., and G. W. Haywood. "The role of the metal ion in the mechanism of the K+-activated aldehyde dehydrogenase of Saccharomyces cerevisiae." Biochemical Journal 247, no. 2 (1987): 377–84. http://dx.doi.org/10.1042/bj2470377.

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The effect of K+ on assays of the enzyme was studied and it appears that the activation occurs slowly by a two-step process. Kinetic measurements suggest that the enzyme-catalysed reaction can proceed slowly (0.4%) in the complete absence of K+. The enzyme exhibits a K+-activated esterase activity, which is further activated by NAD+ or NADH. Stopped-flow studies indicated that the principal effect of K+ on the dehydrogenase reaction is to accelerate a step (possibly acyl-enzyme hydrolysis) associated with a fluorescence and small absorbance transient that occurs after hydride transfer and befo

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31

Topham, R., M. Goger, K. Pearce, and P. Schultz. "The mobilization of ferritin iron by liver cytosol. A comparison of xanthine and NADH as reducing substrates." Biochemical Journal 261, no. 1 (1989): 137–43. http://dx.doi.org/10.1042/bj2610137.

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Considerable evidence suggests that the release of iron from ferritin is a reductive process. A role in this process has been proposed for two hepatic enzymes, namely xanthine oxidoreductase and an NADH oxidoreductase. The abilities of xanthine and NADH to serve as a source of reducing power for the enzyme-mediated release of ferritin iron (ferrireductase activity) were compared with turkey liver and rat liver homogenates. The maximal velocity (Vmax.) for the reaction with NADH was 50 times greater than with xanthine; however, the substrate concentration required to achieve half-maximal veloci

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32

Kanbe, Chiyuki, and Kinji Uchida. "NADH Dehydrogenase Activity ofPediococcus halophilusas a Factor Determining its Reducing Force." Agricultural and Biological Chemistry 51, no. 2 (1987): 507–14. http://dx.doi.org/10.1080/00021369.1987.10868072.

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33

Popov, Kirill M., Natalia Y. Kedishvili, and Robert A. Harris. "Coenzyme A- and NADH-dependent esterase activity of methylmalonate semialdehyde dehydrogenase." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1119, no. 1 (1992): 69–73. http://dx.doi.org/10.1016/0167-4838(92)90236-7.

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34

Wharton, M., D. L. Granger, and D. T. Durack. "Mitochondrial iron loss from leukemia cells injured by macrophages. A possible mechanism for electron transport chain defects." Journal of Immunology 141, no. 4 (1988): 1311–17. http://dx.doi.org/10.4049/jimmunol.141.4.1311.

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Abstract Activated macrophages inhibit replication of murine lymphoblastic leukemia L1210 cells without lysis. This inhibition of replication is associated with abnormalities of mitochondrial electron transport at the level of NADH dehydrogenase (NADH-DH) and succinate dehydrogenase (SDH). The mechanism of inhibition is unknown, although it has been demonstrated that as NADH-DH and SDH activity is lost, iron is released from cells. Because both NADH-DH and SDH contain numerous iron-sulfur clusters, damage to these structures may be one result of injury by activated macrophages. L1210 cells wer

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35

Alissandratos, Apostolos, Hye-Kyung Kim, Hayden Matthews, James E. Hennessy, Amy Philbrook, and Christopher J. Easton. "Clostridium carboxidivorans Strain P7T Recombinant Formate Dehydrogenase Catalyzes Reduction of CO2to Formate." Applied and Environmental Microbiology 79, no. 2 (2012): 741–44. http://dx.doi.org/10.1128/aem.02886-12.

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ABSTRACTRecombinant formate dehydrogenase from the acetogenClostridium carboxidivoransstrain P7T, expressed inEscherichia coli, shows particular activity towards NADH-dependent carbon dioxide reduction to formate due to the relative binding affinities of the substrates and products. The enzyme retains activity over 2 days at 4°C under oxic conditions.

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36

González-Pajuelo, María, Isabelle Meynial-Salles, Filipa Mendes, Philippe Soucaille, and Isabel Vasconcelos. "Microbial Conversion of Glycerol to 1,3-Propanediol: Physiological Comparison of a Natural Producer, Clostridium butyricum VPI 3266, and an Engineered Strain, Clostridium acetobutylicum DG1(pSPD5)." Applied and Environmental Microbiology 72, no. 1 (2006): 96–101. http://dx.doi.org/10.1128/aem.72.1.96-101.2006.

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ABSTRACT Clostridium acetobutylicum is not able to grow on glycerol as the sole carbon source since it cannot reoxidize the excess of NADH generated by glycerol catabolism. Nevertheless, when the pSPD5 plasmid, carrying the NADH-consuming 1,3-propanediol pathway from C. butyricum VPI 3266, was introduced into C. acetobutylicum DG1, growth on glycerol was achieved, and 1,3-propanediol was produced. In order to compare the physiological behavior of the recombinant C. acetobutylicum DG1(pSPD5) strain with that of the natural 1,3-propanediol producer C. butyricum VPI 3266, both strains were grown

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37

Sheeran, Freya L., Julie Angerosa, Norman Y. Liaw, Michael M. Cheung, and Salvatore Pepe. "Adaptations in Protein Expression and Regulated Activity of Pyruvate Dehydrogenase Multienzyme Complex in Human Systolic Heart Failure." Oxidative Medicine and Cellular Longevity 2019 (February 7, 2019): 1–11. http://dx.doi.org/10.1155/2019/4532592.

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Pyruvate dehydrogenase (PDH) complex, a multienzyme complex at the nexus of glycolytic and Krebs cycles, provides acetyl-CoA to the Krebs cycle and NADH to complex I thus supporting a critical role in mitochondrial energy production and cellular survival. PDH activity is regulated by pyruvate dehydrogenase phosphatases (PDP1, PDP2), pyruvate dehydrogenase kinases (PDK 1-4), and mitochondrial pyruvate carriers (MPC1, MPC2). As NADH-dependent oxidative phosphorylation is diminished in systolic heart failure, we tested whether the left ventricular myocardium (LV) from end-stage systolic adult hea

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38

Omar, M. S., and A. M. S. Raoof. "Onchocerca fasciata: histochemical demonstration of succinate and NADH dehydrogenase." Journal of Helminthology 70, no. 1 (1996): 47–51. http://dx.doi.org/10.1017/s0022149x00015121.

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AbstractThe activities of selected enzymes of the respiratory chain system in Onchocerca fasciata (Filarioidea: Onchocercidae) have been investigated histochemically. Thus, the localization and distributions of NADH dehydrogenase (EC 1.6.99.3), succinate dehydrogenase (SDH) (EC 1.3.99.1) and cytochrome oxidase (EC 1.9.3.1) were investigated in various tissues of the adult female worm by employing MTT, Nitro BT (dehydrogenases) and DAB (cytochrome oxidase). Different tissues varied considerably in their enzymatic activities. The hypodermis and reproductive tissues showed strong and identical lo

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39

Granat, Lucy, Debbra Y. Knorr, Daniel C. Ranson, et al. "Yeast NDI1 reconfigures neuronal metabolism and prevents the unfolded protein response in mitochondrial complex I deficiency." PLOS Genetics 19, no. 7 (2023): e1010793. http://dx.doi.org/10.1371/journal.pgen.1010793.

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Mutations in subunits of the mitochondrial NADH dehydrogenase cause mitochondrial complex I deficiency, a group of severe neurological diseases that can result in death in infancy. The pathogenesis of complex I deficiency remain poorly understood, and as a result there are currently no available treatments. To better understand the underlying mechanisms, we modelled complex I deficiency in Drosophila using knockdown of the mitochondrial complex I subunit ND-75 (NDUFS1) specifically in neurons. Neuronal complex I deficiency causes locomotor defects, seizures and reduced lifespan. At the cellula

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40

CA, Murphy, Large PJ, C. Wadforth, Dack SJ, and Boulton CA. "Strain‐dependent variation in the NADH‐dependent diacetyl reductase activities of larger‐ and alebrewing yeasts." Biotechnology and Applied Biochemistry 23, no. 1 (1996): 19–22. http://dx.doi.org/10.1111/j.1470-8744.1996.tb00359.x.

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Significant differences were observed in the zymogram patterns of NAD(+)‐dependent ethanol dehydrogenase and acetoin dehydrogenase activity in seven strains of brewer's yeast examined by non‐denaturing PAGE. Bottom‐fermenting (lager) strains contained quite different activity bands of acetoin dehydrogenase activity compared with top‐fermenting (ale) strains. These differences were confirmed when cell‐free extracts of ale yeasts were heated at 55 degrees C. This destroyed most of the diacetyl reductase activity, while leaving acetaldehyde reductase and other reductase activities unaffected. In

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41

Burgess, Shawn C., Katsumi Iizuka, Nam Ho Jeoung, et al. "Carbohydrate-response Element-binding Protein Deletion Alters Substrate Utilization Producing an Energy-deficient Liver." Journal of Biological Chemistry 283, no. 3 (2007): 1670–78. http://dx.doi.org/10.1074/jbc.m706540200.

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Livers from mice lacking the carbohydrate-responsive element-binding protein (ChREBP) were compared with wild type (WT) mice to determine the effect of this transcription factor on hepatic energy metabolism. The pyruvate dehydrogenase complex was considerably more active in ChREBP-/- mice because of diminished pyruvate dehydrogenase kinase activity. Greater pyruvate dehydrogenase complex activity caused a stimulation of lactate and pyruvate oxidation, and it significantly impaired fatty acid oxidation in perfused livers from ChREBP-/- mice. This shift in mitochondrial substrate utilization led

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42

Marbaix, Alexandre Y., Georges Chehade, Gaëtane Noël, et al. "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 (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′-ph

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43

Kalnenieks, Uldis, Malda M. Toma, Nina Galinina, and Robert K. Poole. "The paradoxical cyanide-stimulated respiration of Zymomonas mobilis: cyanide sensitivity of alcohol dehydrogenase (ADH II)." Microbiology 149, no. 7 (2003): 1739–44. http://dx.doi.org/10.1099/mic.0.26073-0.

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The respiratory inhibitor cyanide stimulates growth of the ethanologenic bacterium Zymomonas mobilis, perhaps by diverting reducing equivalents from respiration to ethanol synthesis, thereby minimizing accumulation of toxic acetaldehyde. This study sought to identify cyanide-sensitive components of respiration. In aerobically grown, permeabilized Z. mobilis cells, addition of 200 μM cyanide caused gradual inhibition of ADH II, the iron-containing alcohol dehydrogenase isoenzyme, which, in aerobic cultures, might be oxidizing ethanol and supplying NADH to the respiratory chain. In membrane prep

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44

Wang, Yaping, Yanhong Peng, Xiaoyan Liu, et al. "Efficient 2,3-Butanediol/Acetoin Production Using Whole-Cell Biocatalyst with a New Nadh/Nad(+) Regeneration System." Catalysts 11, no. 12 (2021): 1422. http://dx.doi.org/10.3390/catal11121422.

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An auto-inducing expression system was developed that could express target genes in S. marcescens MG1. Using this system, MG1 was constructed as a whole-cell biocatalyst to produce 2,3-butanediol/acetoin. Formate dehydrogenase (FDH) and 2,3-butanediol dehydrogenase were expressed together to build an NADH regeneration system to transform diacetyl to 2,3-butanediol. After fermentation, the extract of recombinant S. marcescens MG1ABC (pETDuet-bdhA-fdh) showed 2,3-BDH activity of 57.8 U/mg and FDH activity of 0.5 U/mg. And 27.95 g/L of 2,3-BD was achieved with a productivity of 4.66 g/Lh using en

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45

Ogura, Masato, Junko Yamaki, Miwako K. Homma, and Yoshimi Homma. "Mitochondrial c-Src regulates cell survival through phosphorylation of respiratory chain components." Biochemical Journal 447, no. 2 (2012): 281–89. http://dx.doi.org/10.1042/bj20120509.

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Mitochondrial protein tyrosine phosphorylation is an important mechanism for the modulation of mitochondrial functions. In the present study, we have identified novel substrates of c-Src in mitochondria and investigated their function in the regulation of oxidative phosphorylation. The Src family kinase inhibitor PP2 {amino-5-(4-chlorophenyl)-7-(t-butyl) pyrazolo [3,4d] pyrimidine} exhibits significant reduction of respiration. Similar results were obtained from cells expressing kinase-dead c-Src, which harbours a mitochondrial-targeting sequence. Phosphorylation-site analysis selects c-Src ta

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46

Mankovska, I. M., O. O. Gonchar, and L. V. Bratus. "THE EFFECT OF MEXIDOL ON GLUTATHIONE SYSTEM IN RAT BRAIN UNDER MODELING OF PARKINSON’S DESEASE." Fiziolohichnyĭ zhurnal 68, no. 1 (2022): 13–19. http://dx.doi.org/10.15407/fz68.01.013.

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We studied the effects of mexidol (3-oxy-6-methyl-2-ethylpiridine succinate) on the antioxidant glutathione system in rat brain mitochondria in experimental Parkinson’s disease induced by rotenone administration. Wistar rats were divided into the following groups of 6 in each: I - intact rats (control); II - rotenone (3 mg/kg per day) was injected subcutaneously for 2 weeks; III - after rotenone intoxication, mexidol (50 mg/kg per day) was injected intraperitoneally for 2 weeks. In the suspension of brain mitochondria, the activity of NADH dehydrogenase (complex I of the mitochondrial respirat

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47

Boyer, B., and R. Odessey. "Quantitative control analysis of branched-chain 2-oxo acid dehydrogenase complex activity by feedback inhibition." Biochemical Journal 271, no. 2 (1990): 523–28. http://dx.doi.org/10.1042/bj2710523.

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The potential for branched-chain 2-oxo acid dehydrogenase complex (BCOADC) activity to be controlled by feedback inhibition was investigated by calculating the Elasticity Coefficients for several feedback inhibitors. We suggest that feedback inhibition is a quantitatively important regulatory mechanism by which branched-chain 2-oxo acid dehydrogenase activity is regulated. The potential for control of enzyme activity is greater for NADH than for the acyl-CoA products, and suggests that factors that alter the redox potential may physiologically regulate BCOADC activity through a feedback inhibi

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48

Camacho Carvajal, Margarita M., André H. M. Wijfjes, Ine H. M. Mulders, Ben J. J. Lugtenberg, and Guido V. Bloemberg. "Characterization of NADH Dehydrogenases of Pseudomonas fluorescens WCS365 and Their Role in Competitive Root Colonization." Molecular Plant-Microbe Interactions® 15, no. 7 (2002): 662–71. http://dx.doi.org/10.1094/mpmi.2002.15.7.662.

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The excellent-root-colonizing Pseudomonas fluorescens WCS365 was selected previously as the parental strain for the isolation of mutants impaired in root colonization. Transposon mutagenesis of WCS365 and testing for root colonization resulted in the isolation of mutant strain PCL1201, which is approximately 100-fold impaired in competitive tomato root colonization. In this manuscript, we provide evidence that shows that the lack of NADH dehydrogenase I, an enzyme of the aerobic respiratory chain encoded by the nuo operon, is responsible for the impaired root-colonization ability of PCL1201. T

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49

Marcillat, O., Y. Zhang, and K. J. A. Davies. "Oxidative and non-oxidative mechanisms in the inactivation of cardiac mitochondrial electron transport chain components by doxorubicin." Biochemical Journal 259, no. 1 (1989): 181–89. http://dx.doi.org/10.1042/bj2590181.

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The quinonoid anthracycline, doxorubicin (Adriamycin) is a potent anti-neoplastic agent whose clinical use is limited by severe cardiotoxicity. Mitochondrial damage is a major component of this cardiotoxicity, and rival oxidative and non-oxidative mechanisms for inactivation of the electron transport chain have been proposed. Using bovine heart submitochondrial preparations (SMP) we have now found that both oxidative and non-oxidative mechanisms occur in vitro, depending solely on the concentration of doxorubicin employed. Redox cycling of doxorubicin by Complex I of the respiratory chain (whi

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50

Hirashima, Y., A. A. Farooqui, and L. A. Horrocks. "Fluorimetric coupled enzyme assay for lysoplasmalogenase activity in liver." Biochemical Journal 260, no. 2 (1989): 605–8. http://dx.doi.org/10.1042/bj2600605.

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We developed a continuous spectrofluorimetric assay of lysoplasmalogenase activity with the use of horse liver alcohol dehydrogenase as a coupling enzyme. In this method the disappearance of NADH is measured spectrofluorimetrically. The excitation and emission monochromators were set at 340 and 460 nm respectively. The assay is 10 times as sensitive as the previous u.v. spectrophotometric method. We could detect approx. 0.02 nmol of aldehyde produced/min per ml.

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