ライフサイエンスコーパス: PQQ

1 PQQ (10, 3, and 1 mg/kg) was given once by intravenous i

2 PQQ at 10 mg/kg infused at the initiation, or 3 h after

3 PQQ did not stimulate mitochondrial biogenesis after sma

4 PQQ exposure stimulated phosphorylation of CREB at serin

5 PQQ is bound in a large cleft in the protein surface and

6 PQQ released from the nanospheres in the presence of 40%

7 PQQ serves as an efficient biocatalyst to mediate the ox

8 PQQ treatment given pre- and postnatally in WD-fed offsp

9 PQQ was incubated with amino acids and condensation prod

10 PQQ-loaded liposomes and the peptide or copolymer are ad

11 om the surface-bound nanospheres (ca. 20,000 PQQ molecules/PMMA particle).

12 ut there is nothing to indicate that it is a PQQ-dependent dehydrogenase.

13 be involved in mouse lysine metabolism, is a PQQ-dependent dehydrogenase.

14 DH is pyrroloquinoline quinone (PQQ), with a PQQ-to-subunit stochiometry of approximately 1:1.

15 lo[2,3-f]quinoline-2,7,9-tricarboxylic acid (PQQ)] is a bacterial vitamin that serves as a cofactor i

16 Notably, these changes persisted even after PQQ withdrawal at weaning.

17 However, DTNB and PQQ had little effect on baseline NMDA-evoked currents i

18 exposed to 4-7 microM bicuculline, DTNB and PQQ reversed the potentiation of evoked epileptiform res

19 NMDA-evoked currents in control medium, and PQQ did not alter NMDAR-dependent long-term potentiation

20 shorter distance between these molecules and PQQ in the enzymatic molecule.

21 PABMSA and PQQ act as promoter for enzyme bioelectrocatalysis.

22 -cycling assay, can be further identified as PQQ based on the profile of inhibition it displays with

23 ropriately label beta-propeller sequences as PQQ-binding motifs.

24 methods we demonstrate the presence of both PQQ and IPQ in human milk in nanomolar to micromolar con

25 iester, and its various isomers, and certain PQQ triester derivatives, to catalyze glycine-fueled red

26 For the CRP assay, neutravidin-coated PQQ-doped PMMA nanospheres are used to bind with a bioti

27 r sequence) alcohol dehydrogenase containing PQQ and heme c as cofactors.

28 biosensor when compared to the conventional PQQ-based counterpart.

29 nsing electrode compared to the conventional PQQ-based one.

30 roloquinoline quinone glucose dehydrogenase (PQQ-GDH) and bilirubin oxidase (BOD) at anode and cathod

31 pyroquinoline quinone glucose dehydrogenase (PQQ-GDH) and laccase functioning as the anodic and catho

32 of the PQQ-dependent glucose dehydrogenase (PQQ-GDH) through the specific binding of its pyrroloquin

33 sfer in PQQ-dependent glucose dehydrogenase (PQQ-sGDH) anodes has been determined.

34 quinone (PQQ)-soluble glucose dehydrogenase (PQQ-sGDH) from Acinetobacter calcoaceticus with osmium-b

35 ne quinone dependent glucose dehydrogenase ((PQQ)GDH) has been immobilized on [poly(3-aminobenzoic ac

36 -AHQQ complex (532-536 nm) and the product E-PQQ complex (346-366 nm), a number of spectral intermedi

37 Early PQQ supplementation has persistent long-term protective

38 lity dependent on the number of encapsulated PQQ species that can be readily released from the surfac

39 reporter DNA-tagged liposomes encapsulating PQQ, the prosthetic group of the apo-enzyme glucose dehy

40 able and reproducible response for entrapped PQQ.

41 The electrochemical properties of entrapped PQQ in the PPy film were influenced by the applied poten

42 cterial soluble glucose dehydrogenase enzyme.PQQ.glucose complex and intermediates formed in PQQ redu

43 In the MD structure of enzyme.PQQ.glucose complex the imidazole of His144 is hydrogen

44 In the structure of the enzyme.PQQ.HOCH(3) complex, the hydrogen bonded Glu171-CO(2)(-)

45 evaluated, and the signal amplification for PQQ detection down to the picomolar levels is well-predi

46 th an unknown function, but is essential for PQQ production.

47 Both mutants form PQQ under aerobic conditions with rate constants of 0.09

48 Furthermore, PQQ has a unique pattern of inhibition induced by a seri

49 of a re-engineered component of glucometers: PQQ-glucose dehydrogenase.

50 s spectroscopic detection of the homogeneous PQQ-GDH reconstitution.

51 1 plays the role of general base catalyst in PQQ reduction rather than Asp297 as previously suggested

52 n in mammals, are not affected by changes in PQQ dietary status.

53 .glucose complex and intermediates formed in PQQ reduction.

54 y that defects in lysine metabolism occur in PQQ-deprived rodents.

55 ion with PqqD, carries out the first step in PQQ biosynthesis: a radical-mediated formation of a new

56 pathway is critical for the initial steps in PQQ biogenesis.

57 E) that plays a role in the initial steps in PQQ formation.

58 ration and mechanism of electron transfer in PQQ-dependent glucose dehydrogenase (PQQ-sGDH) anodes ha

59 olvement of two distinct NAD(+)-independent, PQQ-containing alcohol dehydrogenases, BOH (a quinoprote

60 by quinoprotein methanol dehydrogenase (MDH.PQQ) in combination with methanol (MDH.PQQ.methanol) inv

61 (MDH.PQQ) in combination with methanol (MDH.PQQ.methanol) involves Glu-171--CO2(-) general base remo

62 lations with the neutral >C5=NH imine of MDH.PQQ(NH).methanol structure is similar to the reactive MD

63 ablish that the >C5=NH2(+) derivative of MDH.PQQ(NH2(+).methanol structure is unreactive because of t

64 namics (MD) studies of the structures of MDH.PQQ.methanol in the presence of activator NH3 and inhibi

65 In the MD structure of MDH.PQQ.methanol.NH3, the hydrated NH3 resides at a distance

66 Molecular dynamics (MD) simulations on MDH.PQQ.Wat1 complex in TIP3P water for 5 ns does not result

67 nol structure is similar to the reactive MDH.PQQ.methanol complex.

68 n-bonding to Glu-171CO2(-) such that the MDH.PQQ.methanol.NH4(+) complex is not reactive.

69 osure of mouse Hepa1-6 cells to 10-30 microm PQQ for 24-48 h resulted in increased citrate synthase a

70 Moreover, PQQ protected cells from mitochondrial inhibition by rot

71 nt crystal structure has implicated numerous PQQ-PqqC interactions.

72 ons, the free energy for MeOH reduction of o-PQQ when MeOH is hydrogen bonded to Glu-171-CO(2)(-) and

73 The ability of PQQ to stimulate mitochondrial biogenesis accounts in pa

74 ical change is proportional to the amount of PQQ present, which directly relates to the number of lip

75 tetrahedral configuration of the C-5 atom of PQQ in that study represents the C-5-reduced form of the

76 fication assay was developed on the basis of PQQ's ability to catalyze redox cycling at pH 10 in the

77 onal electron density next to R179 and C5 of PQQ, which can be modeled as O2 or H2O2, indicating a si

78 yst for hydride equivalent transfer to C5 of PQQ.

79 e to the >C5[double bond]O quinone carbon of PQQ.

80 state of the quinone and decarboxylation of PQQ, these methods are invaluable for the rapid detectio

81 Enzyme-bound <C5(H)NH2 derivative of PQQ [PQQ(NH)] and CH(2)O product are formed.

82 should facilitate the specific detection of PQQ in biological samples.

83 tude the direct electrochemical detection of PQQ in solution and by 1 to 2 orders the detection limit

84 lectroanalytical method for determination of PQQ in solution down to subpicomolar concentrations is p

85 investigated whether a supplemental dose of PQQ, provided prenatally in a mouse model of diet-induce

86 lts call into question the identification of PQQ as a new vitamin.

87 densation products formed upon incubation of PQQ with amino acids (IPQ; imidazolopyrroloquinoline and

88 ydrogen bonds to the ortho-quinone moiety of PQQ.

89 hydride equivalent transfer to the >C5=NH of PQQ(NH) by concerted Glu-171CO(2)(-) general-base remova

90 to nutrition, medicine, and pharmacology of PQQ, topa quinone, lysyl topa quinone, tryptophan trytop

91 om methanol and the ortho-quinone portion of PQQ.

92 polymerization of pyrrole in the presence of PQQ.

93 polymerization of pyrrole in the presence of PQQ.

94 Herein, we examine the propensities of PQQ, PQQ triester, and its various isomers, and certain

95 ent reversible electrochemical properties of PQQ, which facilitates optimization of separation and de

96 for the rapid detection of the full range of PQQ adducts in biological matrices.

97 The release of PQQ catalyzes a color change in the presence of apo-GDH,

98 pattern of inhibition induced by a series of PQQ antagonists of different potencies.

99 encoded by pqqC catalyzes the final step of PQQ formation, which involves a ring closure and an over

100 a prototype structure for a new subgroup of PQQ-dependent soluble dehydrogenases that is distinct fr

101 The ubiquity of PQQ in the environment and its steady accessibility in t

102 complexes as well as the x-ray structure of (PQQ)Ca2+ bound at the active site of the methanol dehydr

103 irubin oxidase (BOD) has been immobilized on PQQ-modified electrodes.

104 y TCEP and subsequently decreased by DTNB or PQQ at the same concentrations that modulated epileptifo

105 Originally, PQQ was thought to be a covalently bound cofactor in num

106 quely solvent-accessible compared with other PQQ enzymes.

107 t with activation of the PGC-1alpha pathway, PQQ increased nuclear respiratory factor activation (NRF

108 Enzyme-bound <C5(H)NH2 derivative of PQQ [PQQ(NH)] and CH(2)O product are formed.

109 Herein, we examine the propensities of PQQ, PQQ triester, and its various isomers, and certain PQQ t

110 trode surface with an almost fully preserved PQQ binding properties and catalytic activity.

111 The data indicate that putative PQQ from a biological sample, separated by HPLC and dete

112 The putative PQQ substrate PqqA has not yet been shown to be modified

113 transfer from substrate to the ortho-quinone PQQ to provide a C5-reduced intermediate that subsequent

114 identification of pyrroloquinoline quinone (PQQ) and condensation products formed upon incubation of

115 quinone carbon of pyrroloquinoline quinone (PQQ) and rearrangement to hydroquinone (PQQH2) with rele

116 sahara and Kato of pyrroloquinoline quinone (PQQ) as a 'new' vitamin has received considerable attent

117 ogenase containing pyrroloquinoline quinone (PQQ) as cofactor and in the periplasm (29-residue leader

118 to function in the pyrroloquinoline quinone (PQQ) biosynthetic pathway via catalysis of carbon-carbon

119 fic binding of its pyrroloquinoline quinone (PQQ) cofactor to the apoenzyme anchored on an electrode

120 d diets lacking in pyrroloquinoline quinone (PQQ) have reduced mitochondrial content.

121 Biogenesis of pyrroloquinoline quinone (PQQ) in Klebsiella pneumoniae requires the expression of

122 he ability to bind pyrroloquinoline quinone (PQQ) in the presence of Ca2+ in a manner that is proport

123 on of the coenzyme pyrroloquinoline quinone (PQQ) into a polypyrrole (PPy) film on a glassy carbon el

124 nt of the coenzyme pyrroloquinoline quinone (PQQ) into a polypyrrole (PPy) matrix on a 245-microm gra

125 Pyrroloquinoline quinone (PQQ) is a natural antioxidant found in soil, enriched in

126 Pyrroloquinoline quinone (PQQ) is a naturally occurring redox cofactor that acts a

127 Pyrroloquinoline quinone (PQQ) is a product of a ribosomally synthesized and post-

128 Pyrroloquinoline quinone (PQQ) is a widely distributed redox-active cofactor and e

129 the redox cofactor pyrroloquinoline quinone (PQQ) suppressed low Mg(2+)-induced hippocampal epileptif

130 Pyrroloquinoline quinone (PQQ), a prosthetic group for apoglucose dehydrogenase (a

131 he biosynthesis of pyrroloquinoline quinone (PQQ), a vitamin and redox cofactor of quinoprotein dehyd

132 etic group tracer, pyrroloquinoline quinone (PQQ), and their application to the development of a sand

133 omes encapsulating pyrroloquinoline quinone (PQQ), the prosthetic group of the apoenzyme glucose dehy

134 tamin for mammals, pyrroloquinoline quinone (PQQ), was based on their claim that an enzyme, predicted

135 of the DL-FalDH is pyrroloquinoline quinone (PQQ), with a PQQ-to-subunit stochiometry of approximatel

136 S and conventional pyrroloquinoline quinone (PQQ)-based biosensor were evaluated by dynamic constant

137 n of ethanol using pyrroloquinoline quinone (PQQ)-dependent alcohol and aldehyde dehydrogenase (ADH a

138 made by assembling pyrroloquinoline quinone (PQQ)-soluble glucose dehydrogenase (PQQ-sGDH) from Acine

139 to the O5 atom of pyrroloquinoline quinone (PQQ).

140 p to the cofactor, pyrroloquinoline quinone (PQQ).

141 d for synthesis of pyrroloquinoline quinone (PQQ).

142 of 2,7,9-tricarboxypyrroloquinoline quinone (PQQ), semiquinone (PQQH), and dihydroquinone (PQQH2) hav

143 rrent responses of the surface-reconstituted PQQ-GDH and determination of the PQQ equilibrium binding

144 ons generated are transferred from a reduced PQQ to a redox dye reagent, e.g., 2,6-dichloroindolpheno

145 nase from Corynascus thermophilus or soluble PQQ-dependent glucose dehydrogenase from Acinetobacter c

146 t lysis of the bound fraction by surfactant, PQQ is released and available to activate the apo-enzyme

147 Therefore, we hypothesized that PQQ can induce mitochondrial biogenesis in mouse hepatoc

148 Mass spectra indicate that PQQ forms stable hydrated carbonyls and decarboxylates e

149 These data indicate that PQQ may be a useful neuroprotectant in stroke therapy.

150 e glycine-fueled redox cycling and show that PQQ is the most capable of catalyzing redox cycling.

151 These data suggested that PQQ and DTNB suppressed spontaneous ictal activity by re

152 or action of this compound and suggests that PQQ may be beneficial in diseases associated with mitoch

153 The PQQ/ PPy sensor was utilized for the amperometric detect

154 The PQQ/PPy electrode was also found to be very reproducible

155 The PQQ/PPy-modified electrode was incorporated as an end-co

156 s been determined in the apo-form and as the PQQ-bound active holoenzyme.

157 ntegrity of the liposome is compromised, the PQQ encapsulated in the liposomes is released and availa

158 scores were also significantly better in the PQQ-treated group compared to the vehicle controls when

159 cid, the pH-dependent redox potential of the PQQ catalyst allows tuning of the detection potential to

160 constituted PQQ-GDH and determination of the PQQ equilibrium binding (Kb = 2.4 x 10(10) M(-1)) and as

161 d on the heterogeneous reconstitution of the PQQ-dependent glucose dehydrogenase (PQQ-GDH) through th

162 proposed that the higher performance of the PQQ-sGDH anodes in the presence of 1,2- and 1,4-benzoqui

163 The electrochemical performance of the PQQ-sGDH anodes with and without the mediators was exami

164 less than half the current densities of the PQQ-sGDH electrodes.

165 We have studied the PQQ reduction by molecular dynamic (MD) simulations in a

166 2+, nucleophilic addition of methanol to the PQQ C-5 carbonyl followed by a retro-ene elimination is

167 rom the results obtained here, DET using the PQQ-dependent ADH and AldDH still lacks high current den

168 the MDH oxidation of methanol involving the (PQQ)Ca2+ complex are explored via ab initio computations

169 d compared with ab initio structures of the (PQQ)Ca2+, (PQQH)Ca2+, and (PQQH2)Ca2+ complexes as well

170 -base removal of the methanol proton of the (PQQ)Ca2+O(H)CH3 complex concerted with hydride transfer

171 Thus, PQQ is neuroprotective when given as a single administra

172 hexahydroquinoline-7,9-d icarboxylic-acid to PQQ.

173 Today, PQQ is only found as a noncovalent cofactor in bacterial

174 In vivo, PQQ decreased the duration of chemoconvulsant-induced se

175 Nlrp3, Il6, and Ptgs2), were decreased in WD PQQ-fed mice, concomitant with increased expression of f

176 group compared to the vehicle controls when PQQ was given at 10 and 3 mg/kg, but not at 1 mg/kg.

177 stal structures of PqqC and its complex with PQQ and determine the stoichiometry of H2O2 formation an

178 , Trp, and Tyr form IPQ upon incubation with PQQ.

179 Considering the reaction of methanol with PQQ in the absence of Ca2+, nucleophilic addition of met

180 Proline did not react with PQQ.

181 ur results suggest that supplementation with PQQ, particularly during pregnancy and lactation, protec