ライフサイエンスコーパス: ubiquinone

1 lipid-soluble quinones (e.g. menaquionone or ubiquinone).

2 H(A) and the next electron carrier, Q(A) (a ubiquinone).

3 ial homologs involved in the biosynthesis of ubiquinone.

4 he NqrB subunit in the functional binding of ubiquinone.

5 ion of Na(+)-NQR with its electron acceptor, ubiquinone.

6 e oxidation of succinate to the reduction of ubiquinone.

7 ompletely abolished the electron transfer to ubiquinone.

8 investigate the protein interaction with the ubiquinone.

9 eased by the redox reaction between NADH and ubiquinone.

10 ent electron transport between complex I and ubiquinone.

11 ron-transfer chain and the electron donor to ubiquinone.

12 -1.37 V (vs ferrocene) on par with those of ubiquinone.

13 ot modify the signals corresponding to bound ubiquinone.

14 NADH:ubiquinone-1 activities in the reconstituted membranes w

15 ed by interligand Overhauser effects between ubiquinone-1 and DBMIB or 2-n-heptyl-4-hydroxyquinoline

16 well as quinones with shorter prenyl chains (ubiquinone-1 and ubiquinone-2).

17 h a relatively hydrophilic analogue (such as ubiquinone-1).

18 - 0.37 mol of iron, and 1.99 +/- 0.07 mol of ubiquinone/1 mol of complex I.

19 more, we also identified NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9 (NDUFA9) and in

20 Importantly, the diffusion rate of ubiquinone (10 (-13)-10 (-12) cm (2)/s) was found to be

21 Importantly, the diffusion rate of ubiquinone (10(-13)-10(-12) cm2/s) was found to be order

22 conserves the energy from NADH oxidation by ubiquinone-10 (Q10) in proton transport across a membran

23 tion is not rate determining and deduce that ubiquinone-10 has both the highest binding affinity and

24 Ubiquinone-10 is extremely hydrophobic, but in complex I

25 A) site of RCs from Rhodobacter sphaeroides, ubiquinone-10 is reduced, by a single electron transfer,

26 from Rhodobacter sphaeroides have identical ubiquinone-10 molecules functioning as primary (Q(A)) an

27 e energy from electron transfer from NADH to ubiquinone-10 to drive protons across the energy-transdu

28 secondary (Q(B)) electron acceptors are both ubiquinone-10, but with very different properties and fu

29 Ubiquinone-2, an analog of ubiquinone-10, can also oxidize the reduced mitoNEET [2F

30 the extremely hydrophobic natural substrate, ubiquinone-10, must be substituted with a relatively hyd

31 ubcomplex subunit 8, and NADH dehydrogenase (ubiquinone) 1alpha subcomplex subunit 9 of respiratory c

32 ) iron-sulfur protein 3, NADH dehydrogenase (ubiquinone) 1beta subcomplex subunit 8, and NADH dehydro

33 of the redox-active quinone segment found in ubiquinone, 2,3-dimethoxy-1,4-benzoquinone, coupled to a

34 Compared with oxygen, ubiquinone-2 is more efficient in oxidizing the mitoNEET

35 with shorter prenyl chains (ubiquinone-1 and ubiquinone-2).

36 Ubiquinone-2, an analog of ubiquinone-10, can also oxidi

37 by incubation of the Q-free Ndi1 enzyme with ubiquinone-6.

38 and D75H mutant proteins were prepared with ubiquinone-8 (13)C-labeled selectively at the methyl and

39 NqrA binds ubiquinone-8 as well as quinones with shorter prenyl cha

40 known how plants make the benzenoid ring of ubiquinone, a vital respiratory cofactor.

41 oxidative stress combat players in E. coli, ubiquinone acts as the cell's first line of defense agai

42 trates, and play a pivotal role in bacterial ubiquinone (also known as coenzyme Q) biosynthesis or mi

43 Ubiquinone (also known as coenzyme Q) is a ubiquitous li

44 , only genes involved in the biosynthesis of ubiquinone, an electron carrier in the ETC, are highly r

45 Atovaquone is a ubiquinone analogue, and decreases the OCR by inhibiting

46 Atovaquone, a ubiquinone analogue, targets C. felis cytochrome b (cytb

47 determined the structures of GlpD bound with ubiquinone analogues menadione and 2-n-heptyl-4-hydroxyq

48 the Sdh3p and Sdh4p subunits interacts with ubiquinone and may coordinate a b-type heme.

49 dox potentials of the biologically available ubiquinone and menaquinone aid in driving the chemical r

50 rown in the presence of synthetic analogs of ubiquinone and the known Q biosynthetic precursors demet

51 can and other cell surface structures, while ubiquinones and menaquinones, both containing an essenti

52 the biosynthesis of the redox active lipid, ubiquinone, and human ADCK3 mutations cause a cerebellar

53 ntermediate in the synthesis of cholesterol, ubiquinone, and prenylated proteins; consequently, much

54 pophilicity in lieu of the isoprenyl tail of ubiquinone, and reports on redox changes at the quinone/

55 epts electrons from NADH and donates them to ubiquinone, and the free energy released by this redox r

56 xylic acid cycle and beta-oxidation, reduces ubiquinone, and transports protons across the inner memb

57 d drastic changes in the profile of sterols, ubiquinones, and plastidial isoprenoids.

58 n important precursor of sterols, dolichols, ubiquinones, and prenylated proteins.

59 At the same time, when 1,2-benzoquinone and ubiquinone are adsorbed on the electrode surface, the en

60 Hydrophilic ubiquinones are reduced by an additional, non-energy-tra

61 rotate dehydrogenase, which does not require ubiquinone as an electron acceptor, were completely resi

62 se activity required for the biosynthesis of ubiquinone, as demonstrated by the dramatic (75-80%) red

63 nsterol isoprenoids, such as cholesterol and ubiquinone, as well as other metabolites.

64 Further screens link ubiquinone availability to nitro-drug action, plasma mem

65 Positively charged ubiquinone-based compounds inhibit human leukemic cell g

66 To target this pathway, fifteen ubiquinone-based compounds were designed and synthesized

67 vented the conformational change involved in ubiquinone binding but did not modify the signals corres

68 hese SPROUT-designed inhibitors bound in the ubiquinone binding cavity of the human dihydroorotate de

69 oorotate dehydrogenase, the presumed site of ubiquinone binding during oxidation of dihydroorotate to

70 d that Na(+)-NQR contains a single catalytic ubiquinone binding site and a second site that can bind

71 residues do not participate directly in the ubiquinone binding site but probably control its accessi

72 owed that low concentrations of either SA or ubiquinone binding site inhibitors increased SDH activit

73 kinetic evidence that SA acts at or near the ubiquinone binding site of SDH to stimulate activity and

74 gous inhibitor and blockage of the predicted ubiquinone binding site provide a model for the "deactiv

75 ed by inhibition of complex II at either the ubiquinone-binding site (by atpenin A5) or the flavin (b

76 dicted ancestor, pyruvate oxidase, such as a ubiquinone-binding site and the requirement for FAD as c

77 ggested redundant proton shuttles lining the ubiquinone-binding site or from direct transfer from sol

78 ing a hydrophobic plateau that is likely the ubiquinone-binding site.

79 proposed kinetic scheme at the Qi-site where ubiquinone binds to only the reduced enzyme and ubiquino

80 19010 knockout cannot use para-coumarate for ubiquinone biosynthesis and that the supply of 4-hydroxy

81 the first reaction steps almost identical to ubiquinone biosynthesis in E. coli with conversion of ch

82 8) that is involved in the third step of the ubiquinone biosynthesis pathway and harbors a flavin mon

83 in metabolism (eg, aldehyde dehydrogenase 2, ubiquinone biosynthesis protein CoQ9, lactate dehydrogen

84 ional network of Arabidopsis genes linked to ubiquinone biosynthesis singled out an unsuspected solan

85 para-coumarate, displayed similar defects in ubiquinone biosynthesis to that of the at4g19010 knockou

86 found that a third intermediate involved in ubiquinone biosynthesis, 4-hydroxybenzoate, activates ma

87 hia coli UbiD enzyme, which is implicated in ubiquinone biosynthesis, cannot be isolated in an active

88 even genes have been implicated in bacterial ubiquinone biosynthesis, including ubiX and ubiD, which

89 and demonstrated that it controls folate and ubiquinone biosynthesis.

90 ing COQ5 methyltransferase (BoCOQ5-2) in the ubiquinone biosynthetic pathway was isolated.

91 pathway, outer membrane transport channels, ubiquinone biosynthetic pathways, flagellar movement, an

92 binding site and a second site that can bind ubiquinone but is not active.

93 the FAD is involved in electron transfer to ubiquinone but not in electron transfer from ETF to ETF-

94 demonstrate the NqrA subunit is able to bind ubiquinone but with a low non-catalytically relevant aff

95 imited cytotoxicity was seen with the parent ubiquinone coenzyme Q(10.) Inhibition of cancer cell gro

96 RQ is structurally similar to ubiquinone (coenzyme Q or Q), a polyprenylated benzoquin

97 es implicated in the biosynthetic pathway of ubiquinone (coenzyme Q or UQ).

98 Ubiquinone (coenzyme Q) is the generic name of a class o

99 Ubiquinone (Coenzyme Q) plays an important role in the m

100 rring electrons from DsbA to a tightly bound ubiquinone cofactor, DsbB undergoes an unusual spectral

101 Q) is a synthetically modified, redox-active ubiquinone compound that accumulates predominantly in mi

102 on of At2g34630 gave up to a 40% increase in ubiquinone content compared to wild-type plants.

103 is a mammalian UbiB protein associated with ubiquinone (CoQ) biosynthesis and an ataxia (ARCA2) thro

104 Ubiquinone (CoQ), the physiological oxidant in the react

105 Ubiquinone (CoQ10) deficiency is one of the potentially

106 rmentable carbon sources, the requirement of ubiquinone correlates with oxidative stress.

107 mitoNEET [2Fe-2S] clusters, suggesting that ubiquinone could be an intrinsic electron acceptor of th

108 ction by transferring electrons from NADH to ubiquinone coupled to proton translocation across the me

109 tory chains transfers electrons from NADH to ubiquinone, coupled to the translocation of protons acro

110 ns cause a cerebellar ataxia associated with ubiquinone deficiency, but the biochemical functions of

111 sma membrane electron transport (tPMET) is a ubiquinone-dependent cell survival pathway for maintaini

112 haracterization of a fluorogenic analogue of ubiquinone designed to reversibly report on redox reacti

113 ectable defects in mitochondrial function or ubiquinone distribution.

114 ergy production through the coupling of NADH:ubiquinone electron transfer to proton translocation.

115 NA-encoded subunit of CI (NADH dehydrogenase ubiquinone Fe-S protein 4), typically suffer from Leigh

116 broblasts mutant for the NADH dehydrogenase (ubiquinone) Fe-S protein 1 (NDUFS1) subunit of respirato

117 ry chain subunit Ndufs4 [NADH dehydrogenase (ubiquinone) Fe-S protein 4], delays onset of neurologica

118 Computational docking of ubiquinone followed by mutagenesis instead suggested red

119 tron-transfer flavoprotein (ETF) and reduces ubiquinone from the Q-pool.

120 tron transfer flavoprotein (ETF) and reduces ubiquinone from the ubiquinone pool.

121 In the case that all ubiquinone has been reduced to ubiquinol its reoxidation

122 biosynthetic pathways for sterols, dolichol, ubiquinone, heme, isopentenyl adenine, and prenylated pr

123 e in cytochrome aa(3)-600 in comparison with ubiquinone in cytochrome bo(3).

124 q1 orthologs involved in the biosynthesis of ubiquinone in other eukaryotes.

125 ient electron transfer between complex I and ubiquinone in specific mutants.

126 arate as part of the Krebs cycle and reduces ubiquinone in the electron transport chain.

127 ze the diffusion properties of the ubiquinol/ubiquinone in the tethered membrane system.

128 ze the diffusion properties of the ubiquinol/ubiquinone in the tethered membrane system.

129 pectra associated with unlabeled and labeled ubiquinones in the Q(A) binding site in Rhodobacter spha

130 decreased levels of the NADH dehydrogenase (ubiquinone) iron-sulfur protein 3, NADH dehydrogenase (u

131 ne Ndufs4, which encodes NADH dehydrogenase (ubiquinone) iron-sulfur protein 4, results in compromise

132 Taken together, our results emphasize that ubiquinone is a key antioxidant during LCFA metabolism a

133 o peroxisomes and then to mitochondria where ubiquinone is assembled.

134 In the last step, ubiquinone is bound and reduced, and ubiquinol is releas

135 on to the known electron carrier function of ubiquinone is required to explain its antioxidant role i

136 , we show that this increased requirement of ubiquinone is to mitigate elevated levels of reactive ox

137 Coenzyme Q (Q or ubiquinone) is a redox active lipid composed of a fully

138 Coenzyme Q(1)(0) (CoQ(1)(0); also called ubiquinone) is an antioxidant that has been postulated t

139 ng to the electron transfer between NADH and ubiquinone, is not present in eukaryotes and as such cou

140 , H(2)O(2), lipid hydroperoxides, vitamin K, ubiquinone, juglone, ninhydrin, alloxan, dehydroascorbat

141 In humans, an age-dependent decrease in ubiquinone levels and changes in cholesterol homeostasis

142 5 mutant and by detecting increased cellular ubiquinone levels in the BoCOQ5-2-transformed bacteria.

143 ochondrial regulator similar to benzoquinone-ubiquinones like Ub0.

144 as effective at positioning the redox-active ubiquinone-like function within the lipid bilayer to dis

145 mittently reduced by sulfide and oxidized by ubiquinone, linking H2S oxidation to the electron transf

146 proteins involved in folate, methionine, and ubiquinone metabolism, suggesting that it may play a rol

147 tigated the effects of mitochondria-targeted ubiquinone (MitoQ) (5 and 25 mg/kg/day for 4 weeks) in m

148 agreement cannot be obtained by considering ubiquinone molecules in the gas phase or in solution.

149 ine the kinetics of complex I catalysis with ubiquinones of varying isoprenoid chain length, from 1 t

150 osphate, an intermediate in the synthesis of ubiquinone or coenzyme Q10 (CoQ10).

151 se regulator of biosynthesis of coenzyme Q6 (ubiquinone or CoQ6) and a mitochondrial redox-active lip

152 tial mevalonate-derived metabolites, such as ubiquinone or dolichol.

153 did not affect the dissociation constant of ubiquinone or its analog HQNO (2-n-heptyl-4-hydroxyquino

154 of the Coq proteins involved in coenzyme Q (ubiquinone or Q) biosynthesis are interdependent within

155 Coenzyme Q (ubiquinone or Q) is a crucial mitochondrial lipid requir

156 Coenzyme Q (ubiquinone or Q) is a redox-active lipid found in organi

157 Coenzyme Q (ubiquinone or Q) is an essential lipid component of the

158 hibition of TcuB activity by an inhibitor of ubiquinone oxidation, 2,5-dibromo-3-methyl-6-isoproylben

159 I (reduced nicotinamide adenine dinucleotide-ubiquinone oxido-reductase), we found that human cytomeg

160 rane subunit of the approximately 1 MDa NADH:ubiquinone oxidoreductase (complex 1) involved in oxidat

161 NADH:ubiquinone oxidoreductase (complex I) from bovine heart

162 NADH:ubiquinone oxidoreductase (complex I) is a complicated r

163 NADH:ubiquinone oxidoreductase (complex I) is a complicated r

164 NADH:ubiquinone oxidoreductase (complex I) is the first enzym

165 NADH-ubiquinone oxidoreductase (complex I) is the largest ( a

166 NADH:ubiquinone oxidoreductase (complex I) of the mitochondri

167 NADH:ubiquinone oxidoreductase (complex I) plays a central ro

168 NADH:ubiquinone oxidoreductase (complex I) pumps protons acro

169 The activity of NADH:ubiquinone oxidoreductase (complex I) was inhibited by m

170 (GSH) and the activity of mitochondrial NADH:ubiquinone oxidoreductase (complex I), which is oxidativ

171 NADH-ubiquinone oxidoreductase (Complex I, European Commissio

172 Electron transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO) accepts electrons fro

173 Electron-transfer flavoprotein-ubiquinone oxidoreductase (ETF-QO) is an iron-sulfur fla

174 Na(+)-pumping NADH:ubiquinone oxidoreductase (Na(+)-NQR) is responsible for

175 omparing them with yeast Ndi1, a type 2 NADH:ubiquinone oxidoreductase (NDH-2) regarded as alternativ

176 taken to identify hit compounds against NADH:ubiquinone oxidoreductase (PfNDH2), a dehydrogenase of t

177 taken to identify hit compounds against NADH:ubiquinone oxidoreductase (PfNDH2), a novel enzyme targe

178 action against two respiratory enzymes, NADH:ubiquinone oxidoreductase (Plasmodium falciparum NDH2) a

179 Mitochondrial proton-pumping NADH:ubiquinone oxidoreductase (respiratory complex I) compri

180 the complex II superfamily members succinate:ubiquinone oxidoreductase (SQR) and quinol:fumarate redu

181 tion resulted in a 50% reduction of the NADH:ubiquinone oxidoreductase activity of the complex, which

182 , fructose bisphosphate aldolase C, and NADH-ubiquinone oxidoreductase as proteins whose expressions

183 flavoprotein/electron-transfer flavoprotein:ubiquinone oxidoreductase complex and associated dehydro

184 NDUFAF6 encodes NADH:ubiquinone oxidoreductase complex assembly factor 6, als

185 n NDUFS3, an iron-sulfur subunit of the NADH:ubiquinone oxidoreductase complex I, after Lys56 to inte

186 flavoprotein/electron-transfer flavoprotein:ubiquinone oxidoreductase complex, and (iii) the mitocho

187 tified (cytochrome oxidase 2 (COX2) and NADH:ubiquinone oxidoreductase core subunit 4 (MT-ND4)) are e

188 compared these plants with ndufs4 (for NADH:ubiquinone oxidoreductase Fe-S protein4) mutants possess

189 ce of the catalytic subunit NDUFV1 (for NADH:ubiquinone oxidoreductase flavoprotein1) and compared th

190 NADH:ubiquinone oxidoreductase oxidizes NADH and reduces ubiq

191 s (MTS-AAV) containing the mutant human NADH ubiquinone oxidoreductase subunit 4 (ND4) gene followed

192 e mitochondrial gene encoding the human NADH ubiquinone oxidoreductase subunit 4 (ND4).

193 tion in the mitochondrial gene encoding NADH:ubiquinone oxidoreductase subunit 4 (ND4).

194 chain via the electron transfer flavoprotein/ubiquinone oxidoreductase system.

195 ersed by ectopic expression of yeast NDI1, a ubiquinone oxidoreductase that allows bypass of complex

196 yes, the programmed degradation of succinate-ubiquinone oxidoreductase was inhibited in the central l

197 ysfunctions in mitochondrial complex I (NADH:ubiquinone oxidoreductase) are both genetically and clin

198 Complex I (NADH-ubiquinone oxidoreductase) can form superoxide during fo

199 Respiratory complex II (succinate:ubiquinone oxidoreductase) connects the tricarboxylic ac

200 Mitochondrial complex I (also known as NADH:ubiquinone oxidoreductase) contributes to cellular energ

201 Complex I (NADH:ubiquinone oxidoreductase) in mammalian mitochondria is

202 Complex I (NADH ubiquinone oxidoreductase) in mammalian mitochondria is

203 Complex I (NADH ubiquinone oxidoreductase) in mammalian mitochondria is

204 Complex I (NADH-ubiquinone oxidoreductase) in the respiratory chain of m

205 Complex I (NADH ubiquinone oxidoreductase) is a large multisubunit enzym

206 Complex I (NADH:ubiquinone oxidoreductase) is a multisubunit, membrane-b

207 Mitochondrial complex I (proton-pumping NADH:ubiquinone oxidoreductase) is an essential respiratory e

208 Complex I (NADH:ubiquinone oxidoreductase) is central to cellular NAD(+)

209 Complex I (NADH:ubiquinone oxidoreductase) is crucial for respiration in

210 Complex I (NADH:ubiquinone oxidoreductase) is essential for oxidative ph

211 ergy-transducing respiratory complex I (NADH:ubiquinone oxidoreductase) is one of the largest and mos

212 proton pumping mechanism of complex I (NADH-ubiquinone oxidoreductase) is unknown and continues to b

213 In mitochondria, complex I (NADH:ubiquinone oxidoreductase) uses the redox potential ener

214 Respiratory complex I (NADH:ubiquinone oxidoreductase), one of the largest membrane-

215 Complex I (NADH:ubiquinone oxidoreductase), one of the largest membrane-

216 ubunits of mitochondrial complex I (CI; NADH:ubiquinone oxidoreductase), the first enzyme of the resp

217 ochondrial respiratory complex II (succinate:ubiquinone oxidoreductase).

218 membrane protein X), and nuoN (encoding NADH:ubiquinone oxidoreductase); 2) by investigating co-regul

219 by examining the disappearance of succinate-ubiquinone oxidoreductase, an integral protein of the in

220 Respiratory complex I, NADH:ubiquinone oxidoreductase, is a large and complex integr

221 characterized supernumerary subunits of NADH:ubiquinone oxidoreductase, known as complex I (cI), the

222 Ndufc2, a subunit of the NADH: ubiquinone oxidoreductase, plays a key role in the assem

223 It has been proposed that alternative NADH:ubiquinone oxidoreductases (NADH dehydrogenases) may pro

224 entrations does weak NADH binding limit NADH:ubiquinone oxidoreduction, and at the high nucleotide co

225 This approach has indicated that ubiquinone pathway and the MAPK serine-threonine protein

226 embrane potential and redox potential of the ubiquinone pool could be measured from the redox poise o

227 nates instead from electron flow through the ubiquinone pool into complex II.

228 is kinetically important, and on whether the ubiquinone pool is partitioned between pathways.

229 ed by the dramatic (75-80%) reduction of the ubiquinone pool size in corresponding RNAi lines.

230 ence in redox potentials of cytochrome c and ubiquinone pool using the stochastic model to evaluate t

231 electron flow), leading to a highly reduced ubiquinone pool, displaying the highest ROS production f

232 carbon metabolism to the membrane-associated ubiquinone pool.

233 on, with electrons supplied from the reduced ubiquinone pool.

234 ly with the predicted reduction state of the ubiquinone pool.

235 ld slowing of the rate of reoxidation of the ubiquinone pool.

236 rotein (ETF) and reduces ubiquinone from the ubiquinone pool.

237 potentials of the NADH/NAD(+) and ubiquinol/ubiquinone pools.

238 cket for the octaprenyl tail of the proposed ubiquinone precursor substrate does suggest UbiD might a

239 y a "connecting rod" during the reduction of ubiquinone (Q) can account for two or three of the four

240 , during reverse electron transport from the ubiquinone (Q) pool (NAD(+)-reducing).

241 aminoquinone that is structurally similar to ubiquinone (Q), a polyprenylated benzoquinone used in th

242 intra-mitochondrial synthesis of coenzyme Q (ubiquinone, Q) and Q levels are profoundly decreased, po

243 The ubiquinone reactant is regenerated, so the NADH:Q reacti

244 ples the oxidation and reduction of the NADH/ubiquinone redox couple to proton translocation, the int

245 sition of constraints upon free diffusion of ubiquinone redox species between the RC and cytochrome b

246 The enzyme succinate ubiquinone reductase (SQR or complex II) is one of the m

247 ndrial electron transport chain is succinate ubiquinone reductase (SQR or Complex II).

248 Of note, it decreased NADH-ubiquinone reductase activity but not the activity of NA

249 e determined that LND inhibits the succinate-ubiquinone reductase activity of respiratory complex II

250 ACPM1 from the enzyme complex and paralyzed ubiquinone reductase activity.

251 An exception is Complex II (succinate: ubiquinone reductase), which is composed of four alpha-p

252 lance of reactivity between the two sites of ubiquinone reduction (the energy-transducing site and th

253 f the SQR homologs possess sulfide-dependent ubiquinone reduction activity and are required for growt

254 ved NqrB glycine residues 140 and 141 affect ubiquinone reduction and the proper functioning of the s

255 the implications for mechanistic studies of ubiquinone reduction by complex I are discussed.

256 Studies of ubiquinone reduction by isolated complex I are problemat

257 quinol:fumarate reductase variants show that ubiquinone reduction does not use the same pathway.

258 demonstrating the importance of NADH-related ubiquinone reduction for ROS production under these cond

259 In this paper it is shown that the site of ubiquinone reduction is conformationally coupled to the

260 Here, we show that inhibitor-insensitive ubiquinone reduction occurs by a ping-pong type mechanis

261 trally through the membrane arm connects the ubiquinone reduction site in the hydrophilic arm to four

262 a concerted structural rearrangement at the ubiquinone reduction site, providing support for a two-s

263 lly being defined, but the mechanism linking ubiquinone reduction to proton translocation remains unk

264 s the energy from NADH oxidation, coupled to ubiquinone reduction, as a proton motive force across th

265 s the energy from NADH oxidation, coupled to ubiquinone reduction, as a proton motive force across th

266 r along a chain of iron-sulfur clusters, and ubiquinone reduction.

267 fully understood, and little is known about ubiquinone reduction.

268 just one metabolic function: regeneration of ubiquinone required as the electron acceptor for dihydro

269 Biosynthesis of ubiquinones requires the intramembrane UbiA enzyme, an a

270 Idebenone, an artificial ubiquinone showing promise in the treatment of Friedreic

271 At4g19010 contributes to the biosynthesis of ubiquinone specifically from phenylalanine.

272 The association of a series of ubiquinone substrates with detergent micelles was studie

273 nesyl pyrophosphate, but not cholesterol and ubiquinone, suggests that depletion of intermediates, bu

274 tivity of bc1 complex)-like kinases regulate ubiquinone synthesis, mutations causing severe respirati

275 accounts for electron transfer from NADH to ubiquinone through protein-bound prosthetic groups, whic

276 hrome bc(1) complex requires the presence of ubiquinone to function according to the Q-cycle mechanis

277 I couples electron transfer between NADH and ubiquinone to proton translocation across an energy-tran

278 ergy liberated during oxidation of NADH with ubiquinone to pump sodium ions across the cytoplasmic me

279 pling the transfer of electrons from NADH to ubiquinone to the creation of the proton gradient across

280 nsfer between matrix NADH and inner-membrane ubiquinone to the pumping of protons against a proton mo

281 coupling electron transfer between NADH and ubiquinone to the translocation of four protons across t

282 edox potential energy from NADH oxidation by ubiquinone to transport protons across the inner membran

283 logical conditions and the possible roles of ubiquinone/ubiquinol binding/dissociation in energy conv

284 However, how ubiquinone/ubiquinol exchange occurs on catalytically re

285 atalyze via a single, universally accessible ubiquinone/ubiquinol pool that is not partitioned or cha

286 Here, we focus on the mitochondrial ubiquinone/ubiquinol pool.

287 model the unbinding of neutral ground state ubiquinone (UQ) and its reduced anionic semiquinone (SQ(

288 We identify that both ubiquinone (UQ) and menaquinone (MQ) can form stacking a

289 leased by electron transfer between NADH and ubiquinone (UQ) to pump sodium, producing a gradient tha

290 Ubiquinone (UQ), also referred to as coenzyme Q, is a wi

291 nsient complex consisting of DsbA, DsbB, and ubiquinone (UQ).

292 s of Ndi1 in its substrate-free, NAD(+)- and ubiquinone- (UQ2) complexed states.

293 one oxidoreductase oxidizes NADH and reduces ubiquinone, using the free energy released by this react

294 ng various soluble quinone derivatives (e.g. ubiquinones), we reveal a new path of down-regulation of

295 id benzoquinone conjugates plastoquinone and ubiquinone were not substrates, establishing that the pl

296 biomarkers (lactate, pyruvate, carnitine and ubiquinone) were significantly different between ASD and

297 nking FMN to the terminal electron acceptor, ubiquinone, which is bound in a tunnel in the region of

298 nking FMN to the terminal electron acceptor, ubiquinone, which is bound in the region of the junction

299 It couples electron transfer from NADH to ubiquinone with proton translocation across the energy-t

300 l oxidation by Cox2 is of advantage when all ubiquinone would be completely reduced to ubiquinol, e.g