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-GDH immobilized over polyMG displays the current pla

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

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

13 proteins, yet they instead possess a Ca(2+)-PQQ cofactor.

14 a biomimetic active site that binds Ln(3+), PQQ, and catalyzes benzyl alcohol dehydrogenation.

15 features distinguish enzymes that use Ln(3+)-PQQ cofactors from those that do not.

16 A film with improved properties as well as a PQQ-independent novel enzymatic cascade for the degradat

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

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

19 d molecular dynamics simulations, revealed a PQQ/substrate access channel critically regulated by thi

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

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

22 require a Lewis acidic metal ion to activate PQQ, and the 2011 discovery of lanthanide (Ln(3+))-depen

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

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

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

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

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

28 PABMSA and PQQ act as promoter for enzyme bioelectrocatalysis.

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

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

31 screen a focused library of chimeras between PQQ-glucose dehydrogenase and calmodulin.

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

33 bound PQQ K(142)D-PqqT (but not Ca(2+)-bound PQQ K(142)D-PqqT, or La(3+)-bound PQQ WT-PqqT) produces

34 Addition of benzyl alcohol to La(3+)-bound PQQ K(142)D-PqqT (but not Ca(2+)-bound PQQ K(142)D-PqqT,

35 (2+)-bound PQQ K(142)D-PqqT, or La(3+)-bound PQQ WT-PqqT) produces spectroscopic changes associated w

36 0.2 muM) to La(3+) in the presence of bound PQQ and produces spectral signatures consistent with tho

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

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

39 potential in vivo applications by combining PQQ as a redox probe with EIS measurements.

40 e radical anion concomitant with a companion PQQ radical, as evidenced by an optical absorption at 40

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

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

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

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

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

46 inoline quinone (PQQ)-glucose dehydrogenase (PQQ-GDH) immobilized over electropolymerized methylene g

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

48 glucose monitors PQQ-glucose dehydrogenase (PQQ-GDH).

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

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

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

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

53 Early PQQ supplementation has persistent long-term protective

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

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

56 able and reproducible response for entrapped PQQ.

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

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

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

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

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

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

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

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

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

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

67 1 plays the role of general base catalyst in PQQ reduction rather than Asp297 as previously suggested

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

69 .glucose complex and intermediates formed in PQQ reduction.

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

71 nment of PqqE may be relevant to its role in PQQ biosynthesis within an oxygen-dependent biosynthetic

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

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

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

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

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

77 to produce the quinone moiety of the mature PQQ cofactor.

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

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

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

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

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

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

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

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

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

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

88 the principal component of glucose monitors PQQ-glucose dehydrogenase (PQQ-GDH).

89 Moreover, PQQ protected cells from mitochondrial inhibition by rot

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

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

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

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

94 Following an assessment of PQQ's electrochemical attributes, we conducted a compreh

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

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

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

98 yst for hydride equivalent transfer to C5 of PQQ.

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

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

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

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

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

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

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

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

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

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

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

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

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

112 polymerization of pyrrole in the presence of PQQ.

113 polymerization of pyrrole in the presence of PQQ.

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

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

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

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

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

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

120 While the initial and final steps of PQQ biosynthesis, involving PqqD/E and PqqC, have been e

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

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

123 ased on the artificial allosteric variant of PQQ-glucose dehydrogenase (GDH).

124 ly regulated circular permutated variants of PQQ-GDH that show large (>10-fold) changes in enzymatic

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

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

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

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

129 quely solvent-accessible compared with other PQQ enzymes.

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

131 AM1 also produces a periplasmic PQQ-binding protein, PqqT, which we have now structurall

132 cations, the catalytic current of the polyMG|PQQ-GDH electrode is 700-fold higher than that for the e

133 Thermodynamics of the polyMG|PQQ-GDH electrode is determined by the enzyme-catalyzed

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

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

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

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

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

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

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

141 ox-active coenzyme pyrroloquinoline quinone (PQQ) and is structurally homologous to the Ca(2+)-depend

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

143 is of the cofactor pyrroloquinoline quinone (PQQ) and the PQQ-dependent membrane-bound glucose dehydr

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

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

146 downregulation of pyrroloquinoline quinone (PQQ) biosynthesis genes, and upregulation of fdh4 format

147 thionine enzyme in pyrroloquinoline quinone (PQQ) biosynthesis, contains three iron-sulfur cluster bi

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

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

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

151 actor complex with pyrroloquinoline quinone (PQQ) in bacterial XoxF methanol dehydrogenases (MDHs) an

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

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

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

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

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

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

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

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

160 together with the pyrroloquinoline quinone (PQQ) prosthetic group and the Ca(2+) ion in the catalyti

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

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

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

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

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

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

167 the redox cofactor pyrroloquinoline quinone (PQQ), which is critical for C1 metabolism in many microo

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

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

170 Pyrroloquinoline quinone (PQQ)-binding proteins are found in diverse species and p

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

172 requently involves pyrroloquinoline quinone (PQQ)-dependent enzymes, making it expensive due to the c

173 talytic current of pyrroloquinoline quinone (PQQ)-glucose dehydrogenase (PQQ-GDH) immobilized over el

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

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

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

177 d for synthesis of pyrroloquinoline quinone (PQQ).

178 ecific emphasis on pyrroloquinoline quinone (PQQ).

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

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

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

182 l oxidation without formation of the reduced PQQ ethenediol, a biradical mechanism that allows for po

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

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

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

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

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

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

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

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

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

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

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

194 actor pyrroloquinoline quinone (PQQ) and the PQQ-dependent membrane-bound glucose dehydrogenase nearl

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

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

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

198 enerate a nearly complete description of the PQQ biosynthetic pathway.

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

200 al NAD(+) oxidant in the regeneration of the PQQ cofactor for multiple catalytic turnovers.

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

202 e bound Ca(2+) ion and the O5-C5 bond of the PQQ in the high-resolution X-ray structure.

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

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

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

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

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

208 2+, nucleophilic addition of methanol to the PQQ C-5 carbonyl followed by a retro-ene elimination is

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

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

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

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

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

214 142)A-variants or upon addition of Ca(2+) to PQQ K(142)D-PqqT.

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

216 ure reveals a Lys residue hydrogen-bonded to PQQ at the site analogously occupied by a Lewis acidic c

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

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

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

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

221 and conformational dynamics associated with PQQ and rare earth-dependent enzymes.

222 oduces spectroscopic changes associated with PQQ reduction, and chemical trapping experiments reveal

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

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

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

226 Proline did not react with PQQ.

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

228 tures of XoxF1, one with and another without PQQ, both with La(3+) bound in the active-site region an