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PQQ AND LDH

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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/18760973/isolation-and-purification-of-pqq-dependent-lactate-dehydrogenase-from-gluconobacter-and-use-for-direct-electron-transfer-at-carbon-and-gold-electrodes
#2
Becky L Treu, Shelley D Minteer
This research details the isolation and purification of a new type of lactate dehydrogenase that is dependent upon the coenzyme pyrroloquinoline quinone (PQQ). PQQ-dependent enzymes have been of interest in the literature over the last decade due to the fact that many of them can undergo direct electron transfer (DET) at electrode surfaces which is of interest for biosensor and biofuel cell applications. In the paper, we detail the isolation of PQQ-dependent lactate dehydrogenase (PQQ-LDH) from two sources of Gluconobacter (Gluconobacter sp...
November 2008: Bioelectrochemistry
https://www.readbyqxmd.com/read/15771535/magnetic-field-effects-on-bioelectrocatalytic-reactions-of-surface-confined-enzyme-systems-enhanced-performance-of-biofuel-cells
#3
Eugenii Katz, Oleg Lioubashevski, Itamar Willner
The effect of a constant magnetic field on bioelectrocatalytic transformations of three different enzyme assemblies linked to electrodes is examined and correlated with a theoretical magnetohydrodynamic model. The systems consist of surface-reconstituted glucose oxidase (GOx), an integrated lactate dehydrogenase/nicotinamide/pyrroloquinoline quinone assembly (LDH/NAD+ -PQQ), and a cytochrome c/cytochrome oxidase system (Cyt c/COx) linked to the electrodes. Pronounced effects of a constant magnetic field applied parallel to the electrode surface are observed for the bioelectrocatalyzed oxidation of glucose and lactate by the GOx-electrode and LDH/NAD+ -PQQ-electrode, respectively...
March 23, 2005: Journal of the American Chemical Society
https://www.readbyqxmd.com/read/12465985/electrical-contacting-of-flavoenzymes-and-nad-p-dependent-enzymes-by-reconstitution-and-affinity-interactions-on-phenylboronic-acid-monolayers-associated-with-au-electrodes
#4
Maya Zayats, Eugenii Katz, Itamar Willner
The preparation of integrated, electrically contacted, flavoenzyme and NAD(P)(+)-dependent enzyme-electrodes is described. The reconstitution of apo-glucose oxidase, apo-GOx, on a FAD cofactor linked to a pyrroloquinoline quinone (PQQ) phenylboronic acid monolayer yields an electrically contacted enzyme monolayer (surface coverage 2.1 x 10(-)(12) mol cm(-)(2)) exhibiting a turnover rate of 700 s(-)(1) (at 22 +/- 2 degrees C). The system is characterized by microgravimetric quartz-crystal microbalance analyses, Faradaic impedance spectroscopy, rotating disk electrode experiments, and cyclic voltammetry...
December 11, 2002: Journal of the American Chemical Society
https://www.readbyqxmd.com/read/12298004/magneto-switchable-electrocatalytic-and-bioelectrocatalytic-transformations
#5
Eugenii Katz, Laila Sheeney-Haj-Ichia, Itamar Willner
Magnetic switching of redox reactions and bioelectrocatalytic transformations is accomplished in the presence of relay-functionalized magnetite particles (Fe(3)O(4)). The electrochemistry of a naphthoquinone (1), pyrroloquinoline quinone (2; PQQ), microperoxidase-11 (3), a ferrocene derivative (4) and a bipyridinium derivative (5), functionalized magnetic particles, is switched "ON" and "OFF" by an external magnet upon the attraction of the magnetic particles to an electrode or their retraction from the electrode, respectively...
September 16, 2002: Chemistry: a European Journal
https://www.readbyqxmd.com/read/11213228/an-integrated-nad-dependent-enzyme-functionalized-field-effect-transistor-enfet-system-development-of-a-lactate-biosensor
#6
M Zayats, A B Kharitonov, E Katz, A F B├╝ckmann, 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/9828368/fully-integrated-biocatalytic-electrodes-based-on-bioaffinity-interactions
#7
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
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