Relevant bibliographies by topics / NADH-dehydrogenase activity

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Academic literature on the topic 'NADH-dehydrogenase activity'

Author: Grafiati
Published: 21 February 2024

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Journal articles on the topic "NADH-dehydrogenase activity"

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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