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PQQ AND NADH

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https://www.readbyqxmd.com/read/27230956/identification-of-lactate-dehydrogenase-as-a-mammalian-pyrroloquinoline-quinone-pqq-binding-protein
#1
Mitsugu Akagawa, Kenji Minematsu, Takahiro Shibata, Tatsuhiko Kondo, Takeshi Ishii, Koji Uchida
Pyrroloquinoline quinone (PQQ), a redox-active o-quinone, is an important nutrient involved in numerous physiological and biochemical processes in mammals. Despite such beneficial functions, the underlying molecular mechanisms remain to be established. In the present study, using PQQ-immobilized Sepharose beads as a probe, we examined the presence of protein(s) that are capable of binding PQQ in mouse NIH/3T3 fibroblasts and identified five cellular proteins, including l-lactate dehydrogenase (LDH) A chain, as potential mammalian PQQ-binding proteins...
2016: Scientific Reports
https://www.readbyqxmd.com/read/27156055/synergistic-effect-of-pyrroloquinoline-quinone-and-graphene-nano-interface-for-facile-fabrication-of-sensitive-nadh-biosensor
#2
Shanying Han, Tianyu Du, Hui Jiang, Xuemei Wang
A self-assembly composite of graphene-pyrroloquinoline quinone (PQQ) was fabricated and modified on glassy carbon electrode (GCE) for sensitive detection of nicotinamide adenine dinucleotide (NADH). Chitosan (CTS) was applied to disperse graphene to form a stable robust film on GCE. A synergistic effect between PQQ and graphene was observed during the electrocatalytic oxidation of NADH, with about 260mV reduction in the oxidation potential and 2.5-fold increase in the oxidation current compared with those on the bare GCE...
April 27, 2016: Biosensors & Bioelectronics
https://www.readbyqxmd.com/read/26646764/pyrroloquinoline-quinone-resists-denervation-induced-skeletal-muscle-atrophy-by-activating-pgc-1%C3%AE-and-integrating-mitochondrial-electron-transport-chain-complexes
#3
Yung-Ting Kuo, Ping-Hsiao Shih, Shu-Huei Kao, Geng-Chang Yeh, Horng-Mo Lee
Denervation-mediated skeletal muscle atrophy results from the loss of electric stimulation and leads to protein degradation, which is critically regulated by the well-confirmed transcriptional co-activator peroxisome proliferator co-activator 1 alpha (PGC-1α). No adequate treatments of muscle wasting are available. Pyrroloquinoline quinone (PQQ), a naturally occurring antioxidant component with multiple functions including mitochondrial modulation, demonstrates the ability to protect against muscle dysfunction...
2015: PloS One
https://www.readbyqxmd.com/read/25864379/bridging-the-two-worlds-a-universal-interface-between-enzymatic-and-dna-computing-systems
#4
Shay Mailloux, Yulia V Gerasimova, Nataliia Guz, Dmitry M Kolpashchikov, Evgeny Katz
Molecular computing based on enzymes or nucleic acids has attracted a great deal of attention due to the perspectives of controlling living systems in the way we control electronic computers. Enzyme-based computational systems can respond to a great variety of small molecule inputs. They have the advantage of signal amplification and highly specific recognition. DNA computing systems are most often controlled by oligonucleotide inputs/outputs and are capable of sophisticated computing as well as controlling gene expressions...
May 26, 2015: Angewandte Chemie
https://www.readbyqxmd.com/read/24755484/involvement-of-erk1-2-pathway-in-neuroprotective-effects-of-pyrroloquinoline-quinine-against-rotenone-induced-sh-sy5y-cell-injury
#5
Q Zhang, J Zhang, C Jiang, J Qin, K Ke, F Ding
Pyrroloquinoline quinone (PQQ), a redox cofactor in the mitochondrial respiratory chain, has been shown to protect neurons against glutamate-induced damage both in vitro and in vivo. In this study, specific inhibitors to each of the mitochondrial complexes were used to find out which reactive oxygen species (ROS)-generating sites could be affected by PQQ. Then we established an in vitro model of Parkinson's disease (PD) by exposing cultured SH-SY5Y dopaminergic cells to rotenone, a complex I inhibitor. The neuroprotective effects of PQQ were observed by pretreatment of SH-SY5Y cells with PQQ before rotenone injury, and the possible involvement of certain signaling pathways were investigated...
June 13, 2014: Neuroscience
https://www.readbyqxmd.com/read/20802042/molecular-and-catalytic-properties-of-the-aldehyde-dehydrogenase-of-gluconacetobacter-diazotrophicus-a-quinoheme-protein-containing-pyrroloquinoline-quinone-cytochrome-b-and-cytochrome-c
#6
S Gómez-Manzo, J L Chavez-Pacheco, M Contreras-Zentella, M E Sosa-Torres, R Arreguín-Espinosa, M Pérez de la Mora, J Membrillo-Hernández, J E Escamilla
Several aldehyde dehydrogenase (ALDH) complexes have been purified from the membranes of acetic acid bacteria. The enzyme structures and the chemical nature of the prosthetic groups associated with these enzymes remain a matter of debate. We report here on the molecular and catalytic properties of the membrane-bound ALDH complex of the diazotrophic bacterium Gluconacetobacter diazotrophicus. The purified ALDH complex is a heterodimer comprising two subunits of 79.7 and 50 kDa, respectively. Reversed-phase high-pressure liquid chromatography (HPLC) and electron paramagnetic resonance spectroscopy led us to demonstrate, for the first time, the unequivocal presence of a pyrroloquinoline quinone prosthetic group associated with an ALDH complex from acetic acid bacteria...
November 2010: Journal of Bacteriology
https://www.readbyqxmd.com/read/18585147/direct-detection-of-formaldehyde-in-air-by-a-novel-nad-and-glutathione-independent-formaldehyde-dehydrogenase-based-biosensor
#7
S Achmann, M Hermann, F Hilbrig, V Jérôme, M Hämmerle, R Freitag, R Moos
An amperometric enzyme-based sensor-system for the direct detection of formaldehyde in air is under investigation. The biosensor is based on a native bacterial NAD(+)- and glutathione-independent formaldehyde dehydrogenase as biorecognition element. The enzyme was isolated from Hyphomicrobium zavarzinii strain ZV 580, grown on methylamine hydrochloride in a fed-batch process. The sensor depends on the enzymatic conversion of the analyte to formic acid. Released electrons are detected in an amperometric measurement at 0...
May 15, 2008: Talanta
https://www.readbyqxmd.com/read/16934215/respiratory-system-of-gluconacetobacter-diazotrophicus-pal5-evidence-for-a-cyanide-sensitive-cytochrome-bb-and-cyanide-resistant-cytochrome-ba-quinol-oxidases
#8
B González, S Martínez, J L Chávez, S Lee, N A Castro, M A Domínguez, S Gómez, M L Contreras, C Kennedy, J E Escamilla
In highly aerobic environments, Gluconacetobacter diazotrophicus uses a respiratory protection mechanism to preserve nitrogenase activity from deleterious oxygen. Here, the respiratory system was examined in order to ascertain the nature of the respiratory components, mainly of the cyanide sensitive and resistant pathways. The membranes of G. diazotrophicus contain Q(10), Q(9) and PQQ in a 13:1:6.6 molar ratios. UV(360 nm) photoinactivation indicated that ubiquinone is the electron acceptor for the dehydrogenases of the outer and inner faces of the membrane...
December 2006: Biochimica et Biophysica Acta
https://www.readbyqxmd.com/read/12804890/electrochemical-behavior-of-pyrroloquinoline-quinone-immobilized-on-silica-gel-modified-with-zirconium-oxide
#9
Miyuki Yamashita, Christiana A Pessôa, Lauro T Kubota
Pyrroloquinoline quinone (PQQ) was immobilized on the silica gel surface modified with zirconium oxide, designated as Si:Zr, by the carboxylic groups of the PQQ molecule and the zirconium oxide on the silica surface. The electrochemistry of PQQ immobilized on the Si:Zr matrix, incorporated in a carbon paste electrode, was evaluated using the cyclic voltammetry technique. The Si:Zr:PQQ-modified electrode showed a redox couple at E(m)=(E(pa1)+E(pc))/2=-0.150 V vs SCE at pH 7, close to that observed in aqueous solution, and another oxidation peak, E(pa2)=-0...
July 1, 2003: Journal of Colloid and Interface Science
https://www.readbyqxmd.com/read/11999403/l-erythrulose-production-by-oxidative-fermentation-is-catalyzed-by-pqq-containing-membrane-bound-dehydrogenase
#10
Duangtip Moonmangmee, Osao Adachi, Emiko Shinagawa, Hirohide Toyama, Gunjana Theeragool, Napha Lotong, Kazunobu Matsushita
Thermotolerant Gluconobacter frateurii CHM 43 was selected for L-erythrulose production from mesoerythritol at higher temperatures. Growing cells and the membrane fraction of the strain rapidly oxidized mesoerythritol to L-erythrulose irreversibly with almost 100% of recovery at 37 degrees C. L-Erythrulose was also produced efficiently by the resting cells at 37 degrees C with 85% recovery. The enzyme responsible for mesoerythritol oxidation was found to be located in the cytoplasmic membrane of the organism...
February 2002: Bioscience, Biotechnology, and Biochemistry
https://www.readbyqxmd.com/read/11213228/an-integrated-nad-dependent-enzyme-functionalized-field-effect-transistor-enfet-system-development-of-a-lactate-biosensor
#11
M Zayats, A B Kharitonov, E Katz, A F Bückmann, I Willner
An integrated NAD+-dependent enzyme field-effect transistor (ENFET) device for the biosensing of lactate is described. The aminosiloxane-functionalized gate interface is modified with pyrroloquinoline quinone (PQQ) that acts as a catalyst for the oxidation of NADH. Synthetic amino-derivative of NAD+ is covalently linked to the PQQ monolayer. An affinity complex formed between the NAD+/PQQ-assembly and the NAD+-cofactor-dependent lactate dehydrogenase (LDH) is crosslinked and yields an integrated biosensor ENFET-device for the analysis of lactate...
2000: Biosensors & Bioelectronics
https://www.readbyqxmd.com/read/10753442/nadh-regulated-metabolic-model-for-growth-of-methylosinus-trichosporium-ob3b-model-presentation-parameter-estimation-and-model-validation
#12
E M Sipkema, W de Koning, K J Ganzeveld, D B Janssen, A A Beenackers
A biochemical model is presented that describes growth of Methylosinus trichosporium OB3b on methane. The model, which was developed to compare strategies to alleviate NADH limitation resulting from cometabolic contaminant conversion, includes (1) catabolism of methane via methanol, formaldehyde, and formate to carbon dioxide; (2) growth as formaldehyde assimilation; and (3) storage material (poly-beta-hydroxybutyric acid, PHB) metabolism. To integrate the three processes, the cofactor NADH is used as central intermediate and controlling factor-instead of the commonly applied energy carrier ATP...
March 2000: Biotechnology Progress
https://www.readbyqxmd.com/read/9828368/fully-integrated-biocatalytic-electrodes-based-on-bioaffinity-interactions
#13
E Katz, V Heleg-Shabtai, A Bardea, I Willner, H K Rau, W Haehnel
Integrated bioelectrocatalytically active electrodes are assembled by the deposition of enzymes onto respective electrically contacted affinity matrices and further cross-linking of the enzyme monolayers. A catalyst-NAD(+)-dyad for the binding of the NAD(+)-dependent enzymes and cytochrome-like molecules for the binding of the heme-protein-dependent enzymes are used to construct integrated electrically contacted biocatalytic systems. NAD(+)-dependent lactate dehydrogenase (LDH) is assembled onto a pyrroloquinoline quinone-NAD+ monolayer...
October 1, 1998: Biosensors & Bioelectronics
https://www.readbyqxmd.com/read/9451793/assembling-and-evaluation-of-new-dehydrogenase-enzyme-electrode-probes-obtained-by-electropolymerization-of-aminobenzine-isomers-and-pqq-on-gold-platinum-and-carbon-electrodes
#14
A Curulli, I Carelli, O Trischitta, G Palleschi
Pt, Au and graphite electrodes have been coated by electropolymerization of 1,2-, 1,3-, 1,4-diaminobenzene (DAB) and 4-aminobiphenyl in the presence of PQQ using cyclic voltammetry. The activity of the modified electrodes for the oxidation of paracetamol, ascorbic and uric acid was reduced by approximately 90% as compared to the bare electrodes. Polymerization in the presence 4,5-dihydro-4,5-dioxo-1H-pyrrolo(2,3-f)quinoline-2,7,9-tricarboxilic+ ++ acid, pyrroloquinolinequinone (PQQ) led, after optimization, to electrodes capable of catalysing the electrooxidation of beta-nicotinamide adenine dinucleotide, reduced form (NADH), in the range 10(-4)-10(-2) mol/l with a detection limit of 5 x 10(-5) mol/l...
1997: Biosensors & Bioelectronics
https://www.readbyqxmd.com/read/8814312/nadh-mediated-dna-damage-induced-by-a-new-coenzyme-pyrroloquinoline-quinone-in-the-presence-of-copper-ii-ion
#15
Y Hiraku, S Kawanishi
Pyrroloquinoline quinone (PQQ) plays a role as a vitamin or growth factor. Low concentrations of PQQ induced DNA cleavage sites frequently at thymine and cytosine residues in the presence of NADH and Cu(II). Catalase and bathocuproine inhibited DNA damage, whereas free hydroxyl radical scavengers did not. Electron spin resonance and UV-visible spectrometries showed generation of semiquinone radical and superoxide during the reaction of PQQ with NADH. These results suggest that NADH-dependent PQQ redox cycle generated superoxide and hydrogen peroxide to mediate copper-dependent DNA damage...
September 16, 1996: FEBS Letters
https://www.readbyqxmd.com/read/8389151/pyrroloquinoline-quinone-acts-with-flavin-reductase-to-reduce-ferryl-myoglobin-in-vitro-and-protects-isolated-heart-from-re-oxygenation-injury
#16
F Xu, C P Mack, K S Quandt, M Shlafer, V Massey, D E Hultquist
Pyrroloquinoline quinone has been isolated from bacteria and recently has been detected in mammalian tissues and fluids. We report in vitro studies which show that pyrroloquinoline quinone serves as a high-affinity substrate for an erythrocyte "flavin reductase" and that the pyrroloquinoline quinol generated by this catalysis reacts rapidly with ferryl myoglobin radical. Western blot analysis of rat and rabbit heart homogenates detects a cross-reactive protein which has a molecular weight identical to the erythrocyte reductase from the same species...
May 28, 1993: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/8139798/is-pqq-a-significant-nutrient-in-addition-to-its-role-as-a-therapeutic-agent-in-the-higher-animal
#17
REVIEW
H N Christensen
The controversy as to the nutritional status of pyroloquinoline (PQQ) has now been broadened to include various animal tissues by evidence of its vitamin status in mice, a mammalian PQQ reductase, and evidence that this enzyme participates in mechanisms protecting tissues against oxidative stress.
January 1994: Nutrition Reviews
https://www.readbyqxmd.com/read/7836380/dt-diaphorase-redox-potential-steady-state-and-rapid-reaction-studies
#18
G Tedeschi, S Chen, V Massey
NAD(P)H:quinone oxidoreductase (DT-diaphorse) appears to be a 2-electron transfer flavoprotein, which catalyzes the conversion of quinones into hydroquinones. Upon photoreduction in the presence of dimethylformamide, the enzyme forms a red semiquinone. In the absence of dimethylformamide, only 10% of the radical form is thermodynamically stabilized. This indicates a redox potential of the enzyme-bound semiquinone/reduced flavin couple that is higher than the midpoint potential for the oxidized flavin/semiquinone couple...
January 20, 1995: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/6373362/nad-dependent-pqq-containing-methanol-dehydrogenase-a-bacterial-dehydrogenase-in-a-multienzyme-complex
#19
J A Duine, J Frank, M P Berkhout
Cell-free extracts of methanol-grown Nocardia sp. 239 only show significant dye-linked methanol-oxidizing activity when NAD+ is added to the assay mixture. This activity resides in a multienzyme complex which could be resolved into 3 components, namely the methanol dehydrogenase, NAD-dependent aldehyde dehydrogenase and NADH dehydrogenase. In its dissociated form, the methanol dehydrogenase no longer shows dye reduction and although rises in the absorbance values around 340 nm are seen on addition of methanol plus NAD+ to the enzyme, this is not due to NADH production...
March 26, 1984: FEBS Letters
https://www.readbyqxmd.com/read/2829975/properties-of-a-coenzyme-pyrroloquinoline-quinone-generation-of-an-active-oxygen-species-during-a-reduction-oxidation-cycle-in-the-presence-of-nad-p-h-and-o2
#20
K Sugioka, M Nakano, I Naito, S Tero-Kubota, Y Ikegami
The oxidation of NAD(P)H by pyrroloquinoline quinone (PQQ) was non-enzymatically carried out at physiological pH in the presence of O2. The PQQ-NAD(P)H system requires about 1 mol of O2 for the oxidation of 1 mol of NAD(P)H. The oxidation of NAD(P)H occurred at a pseudo-first-order rate with respect to NAD(P)H and was of zero order with respect to PQQ concentration in in the presence of O2: k0[PQQ] [NAD(P)H] = k1 [NAD(P)H], where k0[PQQ] = k1, in which [PQQ] represents the initial concentration of PQQ. k0 values for NADH and NADPH were 3...
February 17, 1988: Biochimica et Biophysica Acta
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