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 (AOX)(12), which also oxidizes ubiquinol to ubiquinone.

4 ot modify the signals corresponding to bound ubiquinone.

5 valonate pathway to promote the synthesis of ubiquinone.

6 ial homologs involved in the biosynthesis of ubiquinone.

7 he NqrB subunit in the functional binding of ubiquinone.

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

9 e oxidation of succinate to the reduction of ubiquinone.

10 ompletely abolished the electron transfer to ubiquinone.

11 investigate the protein interaction with the ubiquinone.

12 eased by the redox reaction between NADH and ubiquinone.

13 ent electron transport between complex I and ubiquinone.

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

15 -1.37 V (vs ferrocene) on par with those of ubiquinone.

16 ing point of an electrolyte comprising 50 mM ubiquinone-0 in aqueous buffer such that optimal device

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

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

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

20 - 0.37 mol of iron, and 1.99 +/- 0.07 mol of ubiquinone/1 mol of complex I.

21 l group of M1 of NDUFA1 (NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1) of complex I,

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

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

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

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

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

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

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

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

30 reduces coenzyme Q(10) (CoQ) (also known as ubiquinone-10), which acts as a lipophilic radical-trapp

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

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

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

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

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

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

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

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

39 Ubiquinone 8 (coenzyme Q8 or Q8) mediates electron trans

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

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

42 bfamily-specific Q-loop domain, a structural ubiquinone-8 cofactor, an active-site density interprete

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

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

45 ession of ferroptosis by FSP1 is mediated by ubiquinone (also known as coenzyme Q(10), CoQ(10)): the

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

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

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

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

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

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

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

53 e is a transmembrane protein, which oxidizes ubiquinone and reduces oxygen, while pumping protons.

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

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

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

57 onal genes for reactions involved in biotin, ubiquinone, and pyridoxine biosynthesis in Z. mobilis we

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

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

60 are lesser than that of the more ubiquitous ubiquinone, and the naphthoquinone headgroup of the form

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

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

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

64 mplex III, which highlights the necessity of ubiquinone as an electron acceptor for tumour growth.

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

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

67 2)O(2) is downstream from dehydrogenases and ubiquinone at the level of cytochrome bd-I, which result

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

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

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

71 l membrane fluidity and the mobility of free ubiquinone between complex II and complex III, but not i

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

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

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

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

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

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

78 e-like inhibitor, piericidin A, bound in the ubiquinone-binding active site.

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

80 reperfusion injury) and their effects on the ubiquinone-binding site and a connected cavity in ND1.

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

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

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

84 19010 knockout cannot use para-coumarate for ubiquinone biosynthesis and that the supply of 4-hydroxy

85 of chorismate is folate biosynthesis despite ubiquinone biosynthesis being active and essential in th

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

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

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

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

90 folate biosynthesis), p-hydroxybenzoic acid (ubiquinone biosynthesis), menaquinone, and aromatic amin

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

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

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

94 and demonstrated that it controls folate and ubiquinone biosynthesis.

95 , a coenzyme Q (also called CoQ(10), CoQ, or ubiquinone) biosynthesis pathway enzyme, develop SRNS wi

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

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

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

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

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

101 enzyme plays an important role in bacterial ubiquinone (coenzyme Q) biosynthesis.

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

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

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

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

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

107 Ubiquinone (CoQ10) deficiency is one of the potentially

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

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

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

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

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

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

114 ectable defects in mitochondrial function or ubiquinone distribution.

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

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

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

118 ndrial complex I subunit NADH dehydrogenase (ubiquinone) Fe-S protein 2 (NDUFS2) is regulated in an S

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

120 Computational docking of ubiquinone followed by mutagenesis instead suggested red

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

122 sent work was to expand our knowledge of the ubiquinone head group biosynthesis and its potential met

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

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

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

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

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

128 ins and demonstrated the presence of several ubiquinones in Arabidopsis mitochondria.

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

130 nce suggesting that the benzoquinone ring of ubiquinones in this parasite may be synthesized through

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

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

133 inamide adenine dinucleotide] dehydrogenase [ubiquinone] iron-sulfur protein 1) or other mitochondria

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

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

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

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

138 , the part of CI that transfers electrons to ubiquinone is synthesized but fails to progress in the C

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

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

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

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

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

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

145 ochondrial regulator similar to benzoquinone-ubiquinones like Ub0.

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

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

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

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

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

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

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

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

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

155 sbB, which transfers reducing equivalents to ubiquinone or menaquinone.

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

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

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

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

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 largest ( a

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

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

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

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

169 NADH-ubiquinone oxidoreductase (Complex I, European Commissio

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

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

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

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

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

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

176 e report that MDM2 negatively regulates NADH:ubiquinone oxidoreductase 75 kDa Fe-S protein 1 (NDUFS1)

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

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

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

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

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

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

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

184 ression of the Saccharomyces cerevisiae NADH:ubiquinone oxidoreductase in L6 cells.

185 NADH:ubiquinone oxidoreductase oxidizes NADH and reduces ubiq

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

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

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

189 del of mitochondrial disease that lacks NADH:ubiquinone oxidoreductase subunit S4 (NDUFS4), a subunit

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

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

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

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

194 Respiratory complex I (NADH:ubiquinone oxidoreductase) captures the free energy from

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

210 Complex I (mitochondrial NADH:ubiquinone oxidoreductase), a membrane-bound redox-drive

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

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

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

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

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

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

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

218 gral components and assembly factors of NADH:ubiquinone oxidoreductase, Mtln does not alter its enzym

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

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

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

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

223 a) redox-driven proton pump that reduces the ubiquinone pool and generates proton motive force to pow

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

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

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

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

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

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

230 carbon metabolism to the membrane-associated ubiquinone pool.

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

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

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

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

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

236 Moreover, ubiquinone produced by the mevalonate pathway was essent

237 osynthesis in bacteria and protists requires ubiquinone (Q) as a precursor.

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

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

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

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

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

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

244 tor in clinical trials, as well as succinate ubiquinone reductase (SQR) activity of Complex II, using

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

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

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

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

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

250 We identify a proton-relay pathway for ubiquinone reduction and water molecules that connect me

251 phosphorylation, exploiting the energy from ubiquinone reduction by NADH to drive protons across the

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

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

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

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

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

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

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

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

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

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

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

263 drial complexes I and II donate electrons to ubiquinone, resulting in the generation of ubiquinol and

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

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

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

267 Mutants in ubiquinone synthesis (but not menaquinone and demethylme

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

269 hway via SREBP2 and promote the synthesis of ubiquinone that plays an essential role in reducing oxid

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

271 free energy from oxidising NADH and reducing ubiquinone to drive protons across the mitochondrial inn

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

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

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

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

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

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

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

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

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

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

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

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

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

285 s of quinones: benzoquinones, represented by ubiquinone (UQ) and naphthoquinones, such as menaquinone

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

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

288 In normoxia, they use ubiquinone (UQ), but in anaerobic conditions inside the

289 higher-redox-potential respiratory quinone, ubiquinone (UQ), is believed to be an adaptive response

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

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

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

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

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

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

296 , and complex III oxidizes ubiquinol back to ubiquinone, which also serves as an electron acceptor fo

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