ライフサイエンスコーパス: quinol

1 ion by methylamine to form an aminoquinol (N-quinol).

2 ent, it follows a HAT pathway with a pendant quinol.

3 ond cleavage can occur to form a monoanionic quinol.

4 secondary quinone (Q(B)) during reduction to quinol.

5 100-fold on the properties of the substrate quinol.

6 of the oxidized ISP involves H transfer from quinol.

7 ch gates ET from the N-quinol, but not the O-quinol.

8 observable intermediates in the oxidation of quinol.

9 -, 1H-indole-, and benzimidazole-substituted quinols.

10 ate if we assume direct reduction of CymA by quinols.

11 e cyclopentadienones and in situ-generated o-quinols.

12 Furthermore, quinols 1 and 2 inhibited insulin reduction, catalyzed b

13 anner into the final hydrolysis product, the quinol 15.

14 lysis of 1 in aqueous solution generates the quinol 2 as one of several photolysis products.

15 o generate azide adducts 4 at the expense of quinols 3, during hydrolysis reactions in the dark.

16 enyl-2,5-cyclohexadienone, 2a, generates the quinol, 3a.

17 Steady state photolysis of 2b yields the quinol 3b as a major reaction product with a yield of ca

18 Heteroaromatic quinols 4-(benzothiazol-2-yl)-4-hydroxycyclohexa-2,5-die

19 rial evaluation of a number of N-substituted quinol-4(1H)-one-3-carboxamide derivatives 4-6.

20 ation, and anti-inflammatory properties of a quinol-4-one and other A-ring mimetic containing nonster

21 ted ortho metalation (DoM) of N,N-dimethyl O-quinol-7-yl carbamate (2) with LDA followed by oxidation

22 ly, for the ET reactions from O-quinol and N-quinol AADH indicating that transfer of an exchangeable

23 Two model ortho-quinol acetates were easily prepared by iodane-mediated

24 c1 complex in the presence and absence of Qp quinol analog inhibitors implied that a large amplitude

25 dicted covalent irreversible binding between quinol analogues and cysteine residues 32 and 35 of thio

26 The superfamily of quinol and cytochrome c terminal oxidase complexes is re

27 d, respectively, for the ET reactions from O-quinol and N-quinol AADH indicating that transfer of an

28 amic analyses of the ET reactions from the O-quinol and N-quinol forms of TTQ in AADH to the copper o

29 the ET reactions of the dithionite-reduced O-quinol and O-semiquinone forms.

30 and formation of a reaction complex between quinol and oxidized iron sulfur protein.

31 whereas ET reactions from dithionite-reduced quinol and semiquinone forms of MADH are rate-limited by

32 es to small molecules, akin to the substrate quinol and the inhibitor stigmatellin, the Thermus therm

33 rted 2,4,5-trichlorophenol to 2,5-dichloro-p-quinol and then to 5-chlorohydroxyquinol but converted 2

34 his event, the DBU-mediated addition between quinols and ortho-methoxycarbonylaryl isocyanates formed

35 is formed during the deprotonation of the N-quinol, and from which rapid ET to the copper of amicyan

36 in reduction of the high potential chain by quinol, and it is not necessary to invoke such a delay t

37 Under these conditions quinols are known to produce superoxide, and because mit

38 2,4,6-trichlorophenol only to 2,6-dichloro-p-quinol as the final product.

39 rotective antioxidants focusing on steroidal quinols as unique molecular leads.

40 ates reduction of quinone and reoxidation of quinol at sites on opposite sites of the membrane, refer

41 ons producing superoxide during oxidation of quinol at the Q(o) site diverge from the Q-cycle rather

42 pose that this is sufficient for exchange of quinol at the RC Q(B) site.

43 er, influences on the complex (disruption of quinol binding and displacement of the Rieske domain) ar

44 e Q(o) pocket can act as a fully independent quinol binding and oxidation site.

45 pparently favored by the reduced ISP, to the quinol binding site at which the oxidant-induced reducti

46 rome bc1 complex with stigmatellin in the Qo quinol binding site.

47 mal to cytochrome c(1) and to the lumen-side quinol binding site.

48 d as a measure of possible perturbation to a quinol binding site.

49 ubunit II contributes to at least one of the quinol binding sites.

50 F(1)F(o) subunit c (F(o)C), while CyoA (the quinol binding subunit of the cytochrome bo3 quinol oxid

51 s against a structurally obligatory role for quinol binding to Q(D).

52 an acidic residue known to be at or near the quinol-binding site (E257A) also inactivates the enzyme

53 This occurs at a quinol-binding site by sequential one electron steps, re

54 on studies of the E. coli QFR with the known quinol-binding site inhibitors 2-heptyl-4-hydroxyquinoli

55 m an enzyme-substrate complex formed between quinol bound at the Q(o) site and the iron-sulfur protei

56 is involved in ligation of stigmatellin and quinol, but not quinone, and that the carboxylate functi

57 ting reaction step which gates ET from the N-quinol, but not the O-quinol.

58 Analysis of the reaction of the N-quinol by Marcus theory yielded an H(AB) which exceeded

59 r partial reactions involved in oxidation of quinol by the bc(1) complex were independent of pH in th

60 iron porphyrins have indicated that phenols/quinols can react with both ferric superoxide and ferric

61 Using simple models for the quinone/quinol conversion rate, it is shown that the optimal ele

62 proton transfer is linked to the semiquinone/quinol couple.

63 QSR1 (quinol-cytochrome c reductase subunit-requiring) is a hi

64 first synthesis of antifungal sesquiterpene quinol dasyscyphin E was achieved starting from trans-co

65 e that NapG and H form an energy- conserving quinol dehydrogenase functioning as either components of

66 Here, the smallest example of a quinol dehydrogenase in nature, CymA, has been studied.

67 in acting as an electron shuttle between the quinol dehydrogenase membrane complex and CprA.

68 certed in the water chain mutants; and (iii) quinol deprotonation and electron transfer from reduced

69 othiazol-2-yl)-2,5-cyclohexadien-1-one, 1, a quinol derivative that exhibits significant anti-tumor a

70 Bulky peroxyquinols and quinols derived from the A-rings of 17beta-estradiol and

71 enzyme may act as a proton shuttle from the quinol during enzyme turnover.

72 20 mV/pH change for the semiquinone anion to quinol (E2) and none for the quinone to semiquinone (E1)

73 hown through azide trapping studies that the quinol ester 2a and the title compound 3a generate the o

74 Laser flash photolysis of the quinol ester 2b in O2-saturated aqueous phosphate buffer

75 Previously, the quinol esters 2 have been used to generate 1, which were

76 Quinol esters 2b, 2c, and 3b and sulfonamide 4c were inv

77 The reaction of the O-quinol exhibited values of electronic coupling (H(AB)) o

78 for the electron-transfer reaction from the quinol form of methylamine dehydrogenase to amicyanin.

79 te was observed, which is likely the reduced quinol form of TTQ that then is oxidized to the quinone.

80 inct reduced forms of TTQ were studied: an O-quinol form that was generated by reduction by dithionit

81 nerated by reduction by dithionite, and an N-quinol form that was generated by reduction by substrate

82 Regiochemistry of addition shifted from quinol formation to conjugate addition as a function of

83 of the ET reactions from the O-quinol and N-quinol forms of TTQ in AADH to the copper of azurin were

84 uinone and menaquinone into their respective quinol forms.

85 e implications of our data for the export of quinol from the RC, for eventual reduction of the cytoch

86 The quinol-fumarate reductase (QFR) respiratory complex of E

87 Escherichia coli quinol-fumarate reductase operates with both natural qui

88 f two residues, Lys-B228 and Glu-C29, at the quinol-fumarate reductase quinone binding site in reacti

89 bitors against the membrane-embedded protein quinol/fumarate reductase (QFR) from Wolinella succinoge

90 not yet been characterized, either in SQR or quinol:fumarate reductase (QFR) in situ.

91 ntial for catalysis by the diheme-containing quinol:fumarate reductase (QFR) of Wolinella succinogene

92 uccinate:ubiquinone oxidoreductase (SQR) and quinol:fumarate reductase (QFR) participate in aerobic a

93 The Escherichia coli Complex II homolog quinol:fumarate reductase (QFR, FrdABCD) catalyzes the i

94 hereas under microaerophilic conditions, the quinol:fumarate reductase can be utilized.

95 c measurements of site-specific mutations of quinol:fumarate reductase variants show that ubiquinone

96 the capping domain (Thr-A234 to Thr-A244 in quinol:fumarate reductase) begins at the interdomain hin

97 In the complex II homolog quinol:fumarate reductase, it has been demonstrated that

98 sink responsible for the oxidation of excess quinols generated by the TCA cycle.

99 duced forms of TTQ were studied, a quinol (O-quinol) generated by reduction by dithionite and the phy

100 the physiologically relevant aminoquinol (N-quinol) generated by reduction by methylamine.

101 tathion-S-yl)hydroquinone, another cytotoxic quinol-glutathione (GSH) conjugate, cause extensive sing

102 mplex with a ligand containing an oxidizable quinol group serves as a turn-on sensor for H2O2.

103 aring covalently attached pendant phenol and quinol groups is investigated.

104 We, therefore, investigated whether quinol-GSH conjugates have the potential to behave as ge

105 realized, and in vitro, CcmF functions as a quinol:haem oxidoreductase.

106 These transient ortho-quinols have a role in the, as yet uncharacterised, bios

107 x, we suggest that hydrogen bonds to the two quinol hydroxyl groups, from Glu-272 of cytochrome b and

108 One of the quinol hydroxyls is shielded from solvent and thus is no

109 s behavior: 1) The Q(o) site semiquinone (or quinol-imidazolate complex) is unstable and thus occurs

110 more rapidly, suggesting a role of the bound quinol in controlling the redox-linked conformational ch

111 ate the mechanism of bifurcated oxidation of quinol in the cytochrome bc1 complex, Rhodobacter sphaer

112 netics and extent of cytochrome b reduced by quinol in the presence of variable concentrations of ant

113 her 2-benzothiazole derivatives that are not quinols, including ring-substituted derivatives of 2-(4-

114 Little is known about enzymatic quinone-quinol interconversions in the lipid membrane when compa

115 ith a mechanism of action of novel antitumor quinols involving inhibition of the small redox protein

116 The oxidation of quinol is by the low-spin ferri-haem, cytochrome b558.

117 mechanism by which the ET reaction of the N-quinol is gated is also related to mechanisms of other g

118 stabilizing the anionic form of the reduced quinol is important for the reaction mechanism of MADH b

119 f the intermediate in the reactions of the N-quinol is not due to the influence of noncovalently boun

120 bc(1) complexes with menadiol indicates that quinol is not oxidized through center P but is oxidized

121 Therefore, the quinol is singly protonated, and the semiquinone is unpr

122 This quinol is then rapidly converted back to the parent estr

123 oxy-1,2,3,4,6,7,12,12b-octahydroindolo[3,2-h]quinol izin-2-yl]-3-methoxyprop-2-enoic acid methyl este

124 Lewis acid-mediated Diels-Alder reactions of quinol lactone 2 gave regioselectivity opposite to that

125 The quinol-linked cytochrome bd oxidases are terminal oxidas

126 s are similar to those of the ET reaction of quinol MADH and different from those of the gated reacti

127 two sequential one-electron oxidations of N-quinol MADH by its physiologic electron acceptor, amicya

128 mediate but also the subsequent oxidation of quinol MADH during TTQ biosynthesis is a MauG-dependent

129 he complete oxidation of substrate-reduced N-quinol MADH is not the O-semiquinone, but the more slowl

130 the proton transfer-gated ET reaction from N-quinol MADH to amicyanin are also changed by the P52G mu

131 the proton transfer-gated ET reaction from N-quinol MADH to amicyanin is also changed by the M51A mut

132 Electron transfer (ET) from N-quinol MADH to amicyanin is gated by the deprotonation o

133 ET from N-quinol MADH to amicyanin is gated by the transfer of a s

134 true electron transfer (ET) reaction from O-quinol MADH to amicyanin to become a gated ET reaction.

135 true electron transfer (ET) reaction from O-quinol MADH to amicyanin.

136 W199F/K MauGs were able to oxidize quinol MADH to form TTQ, the putative final two-electron

137 Interprotein ET from quinol MADH to the high-valent bis-Fe(IV) form of MauG e

138 e reaction step now also gates the ET from N-quinol MADH, which is normally rate-limited by a proton

139 ferent from those of the gated reaction of N-quinol MADH, whose rate varies considerably with pH and

140 true electron transfer (ET) reactions from O-quinol methylamine dehydrogenase to oxidized native and

141 ce the chemical environment of the bioactive quinol moiety.

142 Paracoccus pantotrophus is catalyzed by the quinol-nitrate oxidoreductase NarGHI.

143 istinct reduced forms of TTQ were studied, a quinol (O-quinol) generated by reduction by dithionite a

144 We have shown that the quinol obtained from a 17beta-estradiol derivative was,

145 pating in intermolecular hydrogen bonds from quinol OH to carbonyl O, but one OH group also interacts

146 "tailed" occupant, either an inhibitor or a quinol or one of their reaction products.

147 ane-localized cytochrome c oxidase (COX) and quinol oxidase (Cyd) and the cytoplasmic membrane-locali

148 cytochrome c oxidase (Cox) and cytochrome bd quinol oxidase (Cyd), are present in the photosynthetic

149 quinol oxidase, and a putative cytochrome bd quinol oxidase (Cyd).

150 Both are members of the diiron carboxylate quinol oxidase (DOX) class of proteins.

151 ligands appear to interact directly with the quinol oxidase (Q(o)) binding pocket.

152 The quinol oxidase (Q(o)) site in this complex oxidizes a hy

153 ions, which bind at a site distant from the quinol oxidase (Q(o)) site, inhibit plastoquinol (PQH2)

154 position of the substrate, ubiquinol, in the quinol oxidase (Q(o)) site.

155 ce to the proton channels of the heme-copper quinol oxidase (QO), cytochrome bo3, E. coli, has been c

156 s containing mammalian complex I, Q10, and a quinol oxidase (the alternative oxidase, AOX) to recycle

157 her of these residues results in the loss of quinol oxidase activity and can result in the loss of th

158 the more conservative D75E substitution has quinol oxidase activity equal to that of the wild-type e

159 The quinol oxidase activity of the W93V mutant is also reduc

160 hrome bd oxidase exhibited cyanide-sensitive quinol oxidase activity.

161 enzymes were found to show very little or no quinol oxidase activity.

162 GSH transport and cytochrome bd quinol oxidase assembly are abolished in the cydD1 mutan

163 mutant of CyoA still assembles as an active quinol oxidase capable of supporting growth of the cells

164 The possibility that a primitive quinol oxidase complex evolved to yield two separate com

165 quinol binding subunit of the cytochrome bo3 quinol oxidase complex) and wild-type procoat are slight

166 plastoquinol oxidation in thylakoids by the quinol oxidase CydAB that occurs without upregulation of

167 The reaction of the quinol oxidase cytochrome bo3 from Escherichia coli with

168 CuB histidines from the cytochrome aa(3)-600 quinol oxidase from Bacillus subtilis.

169 corresponding region of the cytochrome bo(3) quinol oxidase from Escherichia coli (where E89II is the

170 mutagenesis studies of the cytochrome bo(3) quinol oxidase from Escherichia coli implicated an almos

171 Cytochrome bd is a quinol oxidase from Escherichia coli, which is optimally

172 Cu(II) and Cu(I) forms of the cytochrome bo3 quinol oxidase from Escherichia coli.

173 nscribed in the cccA deletion mutant and the quinol oxidase genes (cioAB) were up-regulated.

174 that oxygen consumption by V. fischeri CydAB quinol oxidase is inhibited by NO treatment, whereas oxy

175 The cytochrome bd quinol oxidase is one of two respiratory oxidases in Esc

176 ific enzyme examined is the cytochrome bo(3) quinol oxidase of E. coli.

177 Protein sequence alignments of cytochrome bd quinol oxidase sequences from different microorganisms h

178 the level of a reactive intermediate in the quinol oxidase site of the enzyme, resulting in "bypass

179 on of reactive intermediates produced at the quinol oxidase site of the enzyme.

180 ffinity ubisemiquinone radical, QH*-, of bo3 quinol oxidase to determine its electronic spin distribu

181 that we interpret to be a cytochrome bo-type quinol oxidase, and a putative cytochrome bd quinol oxid

182 The quinol oxidase, cytochrome bd, functions as a terminal o

183 osomes containing complex I, together with a quinol oxidase, to determine the kinetics of complex I c

184 valens expresses a membrane-bound aa(3)-type quinol oxidase, when grown aerobically, that we have stu

185 mbinations of one NADH dehydrogenase and one quinol oxidase.

186 , possibly, in the mitochondrial alternative quinol oxidase.

187 echocystis sp. PCC 6803 encodes a functional quinol oxidase.

188 ctivity but expressing normal levels of aa3 (quinol) oxidase activity.

189 i, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the

190 Cytochrome bd-type quinol oxidases catalyze the reduction of molecular oxyg

191 Cytochrome bd is one of the two quinol oxidases in the respiratory chain of Escherichia

192 uence alignment of subunit II of heme-copper quinol oxidases is used as a guide to select conserved r

193 Speculation that subunit II in the quinol oxidases may also be important as an electron ent

194 and CioB are homologous to the cytochrome bd quinol oxidases of Escherichia coli and Azotobacter vine

195 ain contained reduced levels of the terminal quinol oxidases of the electron transport chain.

196 sibility that there is a family of bacterial quinol oxidases related to the cytochrome bd of E. coli

197 Cytochrome bo3 and other quinol oxidases that are members of the heme-copper oxid

198 Indeed, mutants lacking the respiratory quinol oxidases were sensitive to H2O2, and NO did not h

199 As integral membrane quinol oxidases, cytochrome bd and fumarate reductase re

200 tic activity of classical NO targets such as quinol oxidases.

201 ted in a synergistic decrease in the rate of quinol oxidation (0.7% of the wild type).

202 hoquinone, is a competitive inhibitor of the quinol oxidation (Q(o)) site of the mitochondrial cytoch

203 two electrons in a substrate molecule at the quinol oxidation (Q(o)) site.

204 tes a separated quinone reduction (Q(i)) and quinol oxidation (Q(o)) site.

205 r sphaeroides (Rsbc(1)), stabilized with the quinol oxidation (Q(P)) site inhibitor stigmatellin alon

206 fer of the second proton derived from p-side quinol oxidation and a "dielectric well" for charge bala

207 It couples the redox work of quinol oxidation and cytochrome reduction to the generat

208 Since semiquinone intermediates of quinol oxidation are generally highly reactive, one of t

209 GHI) is a membrane-bound enzyme that couples quinol oxidation at a periplasmically oriented Q-site (Q

210 Quinol oxidation at center P of the cytochrome bc(1) com

211 rane-anchored protein directs electrons from quinol oxidation at the membrane anchor, NarI, to the si

212 itors, we analyze the effects of mutation on quinol oxidation at the Q(o) site of the complex.

213 suggested that the movement is necessary for quinol oxidation at the Q(o) site of the complex.

214 bc(1) complex) suggest that the mechanism of quinol oxidation by the bc(1) complex involves a substan

215 Quinol oxidation by the bc(1) complex of Rhodobacter sph

216 state rate and activation energy (E(a)) for quinol oxidation in purified yeast bc(1) complexes harbo

217 f electron and proton transfer (PCET) during quinol oxidation in respiratory and photosynthetic ET ch

218 The pH dependence of the rate of quinol oxidation in this mutant was also shifted up by a

219 ), which functionally connects the catalytic quinol oxidation Qo site in cytochrome b with cytochrome

220 tion was found to be highly dependent on the quinol oxidation rate.

221 mplex reveal that binding is directed to the quinol oxidation site (Q(o)) of the bc(1) complex.

222 ween O(2) and catalytic intermediates at the quinol oxidation site of cytochrome bc(1) to prevent ROS

223 One location is close enough to the supposed quinol oxidation site to allow reduction of the Fe-S pro

224 en the iron-sulfur protein headgroup and the quinol oxidation site, as judged by the electron paramag

225 wever, when we allowed the rate constant for quinol oxidation to decrease 1000-fold and the rate cons

226 In such fits, quinol oxidation was much slower than literature values

227 on exit to the positive phase resulting from quinol oxidation, are defined in a 2.70-A crystal struct

228 at (1) the initial and rate-limiting step in quinol oxidation, both in the biological and biomimetic

229 l (E(m)) of the ISP and a slowing in rate of quinol oxidation, suggesting that electron transfer from

230 CytcO with O2, and the linked cyt. bc1-CytcO quinol oxidation-oxygen-reduction activities in mitochon

231 s of mutants with altered driving forces for quinol oxidation.

232 cluster may be important in the mechanism of quinol oxidation.

233 y half of the bc(1) complex participating in quinol oxidation.

234 aths for exit of the two protons released in quinol oxidation.

235 the high activation barrier associated with quinol oxidation.

236 allow catalysis of all partial reactions of quinol oxidation.

237 ance of the protonation state of the ISP for quinol oxidation.

238 known to be generated in the b6f complex by quinol oxidation.

239 s both heme groups, it is unable to catalyze quinol oxidation.

240 calculations on model biomimetic systems for quinol oxidation.

241 ng proton transfer to the E-pathway from the quinol-oxidation site via interactions with the heme b(D

242 ependently, at another site connected to the quinol-oxidizing site, possibly the iron-sulfur center.

243 in of Vibrio cholerae contains three bd-type quinol oxygen reductases as well as one cbb(3) oxygen re

244 Phenols and quinols participate in both proton transfer and electron

245 ) catalyzes the conversion of various phytyl quinol pathway intermediates to their corresponding toco

246 The chemical structure of the quinol pharmacophore 4-(hydroxycyclohexa-2,5-dienone) su

247 rate limiting and assuming that the quinone/quinol pool of about 900 molecules acts in a quasi-stati

248 er electrons from the inner membrane quinone/quinol pool through the periplasm to the outer membrane.

249 pB, is assumed to receive electrons from the quinol pool via the membrane-bound cytochrome NapC.

250 er Diels-Alder reactions from pools of ortho-quinol precursors.

251 the semiquinone and the neutral form of the quinol predominate in the pH range studied.

252 essfully developed a method to produce ortho-quinol products with controlled site- and stereoselectiv

253 tionship of the products with well-studied o-quinols provides numerous avenues for synthetic elaborat

254 eduction of a bound quinone molecule Q(B) to quinol Q(B)H(2).

255 ron transfer within cytb(6) f occurs via the quinol (Q) cycle, which catalyses the oxidation of plast

256 obile quinone molecule Q(B) converts it to a quinol, Q(B)H(2).

257 econdary quinone electron acceptor), to form quinol, Q(B)H2.

258 ing models for the two-electron oxidation of quinol (QH2) at the cytochrome bc1 complex and related c

259 mplex recycles one of the two electrons from quinol (QH2) oxidation at center P by reducing quinone (

260 imulations further suggest that formation of quinol (QH2) triggers rapid dissociation of the anionic

261 The pathway of quinol/quinone (Q/QH2) transfer emphasizes the labyrinth

262 and fumarate at one active site with that of quinol/quinone at a second distinct active site over 40

263 o mediate electron transfer between membrane quinols/quinones and soluble periplasmic enzymes.

264 ite in this complex oxidizes a hydroquinone (quinol), reducing two one-electron carriers, a low poten

265 and reports on redox changes at the quinone/quinol segment.

266 Remarkably, the quinol site in complex I (site IQ) and the flavin site i

267 a different maximum capacity (e.g. the outer quinol site in complex III (site IIIQo) has a very high

268 es and the 318 nm intermediate to an initial quinol species.

269 is considered to be analogous to that of the quinol substrate at the moment of electron transfer, the

270 ndow of redox potentials with respect to the quinol substrate to allow normal turnover of the complex

271 le for any enzyme with a hydrophobic quinone/quinol substrate, and could be used to characterize hydr

272 reoscilla phospholipids and energized with a quinol substrate, it translocates Na+, not H+, across th

273 The presence of the quinol suggests that photolysis also leads, in part, to

274 atalyzed cyclization and a series of quinone-quinol tautomerizations that are followed by cycles of O

275 against oxidative stress is also possible by quinols that essentially act as prodrugs for the active

276 tive semiquinone intermediates and producing quinols that promote tolerance of H(2)O(2).

277 sfer reactions resulting in the oxidation of quinol, the reduction of a mobile electron carrier, and

278 gether with the necessary passage of quinone/quinol through the small Q(p) portal in the complex, it

279 onable groups involved in the binding of the quinol to cytochrome bd from Escherichia coli.

280 synthesis; it couples electron transfer from quinol to cytochrome c to proton translocation across th

281 DCCD inhibits the delivery of electrons from quinol to heme c(1).

282 he level of direct one-electron oxidation of quinol to semiquinone by the Rieske protein.

283 n alternative electron transfer pathway from quinol to terminal oxidoreductases independent of CymA o

284 tion, suggesting that electron transfer from quinol to the oxidized ISP controls the overall rate and

285 the Ru and a proton is transferred from the quinol to the pbim(-) ligand.

286 the release of protons from the oxidation of quinol to the periplasm and the uptake of protons used t

287 in which an electron is transferred from the quinol to the Ru and a proton is transferred from the qu

288 n of the extent of cytochrome b reduction by quinol together with a shift of the reduced b(H) heme sp

289 with the true ET reaction from the reduced O-quinol tryptophan tryptophylquinone (TTQ) of MADH to oxi

290 ET from the reduced O-quinol tryptophan tryptophylquinone of MADH to oxidized

291 ht intensity is determined after identifying quinol turnover at the cytochrome bc1 complex (cytbc1) a

292 rains also contain nor, encoding a predicted quinol-type nitric oxide (NO) reductase (saNOR).

293 aa(3) oxidase, which does not contain bound quinol, undergoes a reversible slow conformational chang

294 Estrone quinol was also equipotent with its parent estrogen in r

295 hrome c reductase assays and in reactions of quinol with enzyme in which the inhibitors block pre-ste

296 re of *OH was shown to produce a nonphenolic quinol with no affinity to the estrogen receptors.

297 The rate and E(a) of the slow reaction of quinol with oxygen that are observed after cytochrome b

298 his field is: how does the Q(o) site oxidize quinol without the production of deleterious side reacti

299 erwent 6beta-hydroxylation, but only estrone quinol yielded a second product consistent with hydroxyl

300 Monooxygenation of the 4-hydroxy analogues (quinols) yielded identical cis-epoxyquinols, and both is