ライフサイエンスコーパス: dioxygen

1 nner-sphere reduction of both superoxide and dioxygen.

2 isate, which was subsequently incubated with dioxygen.

3 ted to active oxygen species or to dissolved dioxygen.

4 he enzyme has to catalyze in the presence of dioxygen.

5 ring the reaction of the reduced flavin with dioxygen.

6 Complexes 1 and 2 both react rapidly with dioxygen.

7 neurosporene derivatives in the presence of dioxygen.

8 to dihydrogen and the oxidation of water to dioxygen.

9 such as transferring electrons or activating dioxygen.

10 talyzes the oxidative conversion of water to dioxygen.

11 esence of a regulatory protein (ToMOD), with dioxygen.

12 uene/o-xylene monooxygenase hydroxylase with dioxygen.

13 + (4) (X-ray) along with ca. 0.5 molar equiv dioxygen.

14 ts for the selective oxidation of styrene by dioxygen.

15 ing is unproductive for generating molecular dioxygen.

16 peroxide (O(2)(*-)) to hydrogen peroxide and dioxygen.

17 terminal oxygen atom of the heme iron-bound dioxygen.

18 xylase variants I100Y, L208F, and F205W with dioxygen.

19 hyl groups, which consumes nine molecules of dioxygen.

20 ociated with the terminal oxygen atom of the dioxygen.

21 m the {FeNO}(6) intermediate and reacts with dioxygen.

22 dation of dimethoxyphenol in the presence of dioxygen.

23 removal of OCl(-) by AgNPs in the absence of dioxygen.

24 er enhances the electron acceptor ability of dioxygen.

25 rogen electrode resulted in the formation of dioxygen (84% Faradaic yield) through multiple catalyst

26 analysis suggests two possible pathways for dioxygen access through the alpha-subunit to the diiron

27 The rate constants for dioxygen access to the diiron center were derived from t

28 ional changes will be required to facilitate dioxygen access to the diiron center.

29 uene/o-xylene monooxygenase hydroxylase is a dioxygen-activating enzyme.

30 ritin-like diiron-carboxylate superfamily of dioxygen-activating proteins.

31 threonine residue believed to be involved in dioxygen activation and instead contains an asparagine a

32 The mechanisms of dioxygen activation and methane C-H oxidation in particu

33 ine ligand at Cu(M) is believed to be key to dioxygen activation and the hydroxylation chemistry of t

34 theoretical and biomimetic investigations of dioxygen activation at mononuclear copper centers.

35 Determination of the mechanism of dioxygen activation by flavoenzymes remains one of the m

36 p(2))-H activation has been achieved through dioxygen activation by NHPI.

37 key intermediates in the catalytic cycles of dioxygen activation by non-haem iron enzymes.

38 Dioxygen activation by the reduced T201 variants was exp

39 analogous to Int1 demonstrating that initial dioxygen activation is an inner sphere Pd-based process

40 This activity suggests that dioxygen activation may be reversible.

41 These studies demonstrate that the dioxygen activation mechanism is preserved in all T201 v

42 nooxygenase in methane hydroxylation-through dioxygen activation mechanisms.

43 of a strictly conserved T201 residue during dioxygen activation of the enzyme, T201S, T201G, T201C,

44 e utilized as molecular models to understand dioxygen activation on M(2)O(5)(-) and M(2)O(5) clusters

45 970s-1980s, the current understanding of the dioxygen activation process in flavoenzymes is believed

46 ts suggest a similar role for protons in the dioxygen activation reactions in soluble methane monooxy

47 ntified in a previous study, is a product of dioxygen activation that is formed during aerobic oxidat

48 s, and elucidated chemical steps involved in dioxygen activation through the kinetic studies of T201(

49 A mechanism is postulated for dioxygen activation, and possible structures of oxygenat

50 nated T201(peroxo) and ToMOH(peroxo), during dioxygen activation.

51 evealing that T201 is critically involved in dioxygen activation.

52 on for a proton-coupled electron transfer in dioxygen activation.

53 roxidase-like chemistry with more attractive dioxygen-activation chemistry.

54 closed state that orients the C-As bond for dioxygen addition and cleavage.

55 udies, rR structural characterization of the dioxygen adduct of LPO, commonly called Compound III, ha

56 The protonation-reduction of a dioxygen adduct with [LCu(I)][B(C6F5)4], cupric superoxo

57 o confirm the structural formulations of the dioxygen-adducts, UV-vis and resonance Raman spectroscop

58 uclear copper-containing active site and use dioxygen and a reducing agent to oxidatively cleave glyc

59 Dioxygen and beta-mercaptoethanol are unable to compete

60 late complex, which is capable of activating dioxygen and catalyzing its two-electron reduction to ge

61 es the disproportionation of superoxide into dioxygen and hydrogen peroxide by cycling between Ni(II)

62 idized as it disproportionates superoxide to dioxygen and hydrogen peroxide.

63 e, that the reaction is initiated by triplet dioxygen and its binding to deprotonated substrate and o

64 phyrin intermediates, typically derived from dioxygen and its congeners such as hydrogen peroxide.

65 eins (FDPs) catalyze reductive scavenging of dioxygen and nitric oxide in air-sensitive microorganism

66 tozoa, serving as the terminal components to dioxygen and nitric oxide reductive scavenging pathways

67 Only in the presence of both dioxygen and protons is rapid and clean oxidation to the

68 aldehyde cleavage by the Np AD also requires dioxygen and results in incorporation of (18)O from (18)

69 to involve electron transfer from flavin to dioxygen and subsequent proton transfer to form C4a-hydr

70 prevent the reaction of reductase(TOL) with dioxygen and thus present a solution toward conflicting

71 ion of unactivated C-H bonds using molecular dioxygen and two electrons delivered by the reductase.

72 Dioxygen and water activation on multi-Ru-substituted po

73 the biferrous state would become occupied by dioxygen and Y51 along the O(2) reaction coordinate.

74 faster rate than observed in the presence of dioxygen and/or hydrogen peroxide.

75 substrate during hydroxylation derives from dioxygen, and a late-stage ortho-H(+) transfer to an exo

76 transformation of the small molecules furan, dioxygen, and nitromethane into a more complex and infor

77 The process requires dioxygen, and the transformation rate is first-order in

78 supports a mechanism in which the 2 atoms of dioxygen are inserted into the substrate via a consecuti

79 dihydroxy-3-oxo-5-(methylthio)pent-1-ene and dioxygen) are derived from the same polypeptide chain.

80 a mononuclear non-heme-iron(II) cofactor and dioxygen as cosubstrate to cleave these C-H bonds and di

81 Chlorite is the sole source of dioxygen as determined by oxygen-18 labeling studies.

82 The enzyme uses dioxygen as the terminal oxidant and achieves selectivit

83 The reaction of 4-Me with dioxygen at low temperature produces a species (8-Me) an

84 he [4Fe-4S] clusters in PsaC inaccessible to dioxygen at the onset of oxygenic photosynthesis.

85 ds with near-native structure and reversible dioxygen binding ability equivalent to the haem protein

86 rform a diverse range of reactions including dioxygen binding and transport, electron transfer, and o

87 lar 2/2 hemoglobins suggests that reversible dioxygen binding is not its main activity.

88 of cofactors and defined a novel hydrophobic dioxygen binding pocket adjacent to a bound substrate an

89 The dioxygen binding site is located on the metal face oppos

90 forms a transient ligand interaction at the dioxygen binding site of Fe2.

91 mined structures of S-HPP-HppE, identify the dioxygen binding site on iron and elegantly illustrate h

92 effects of subsequent intramolecular ET and dioxygen binding to the trinuclear copper cluster into t

93 site of the heme-iron is vacant, providing a dioxygen-binding site that would also involve interactio

94 tively, followed by a faster cleavage of the dioxygen bond (4.8 mus), which generates the P intermedi

95 scopic measurements that the cleavage of the dioxygen bond may be mechanistically similar to that in

96 64) may facilitate homolytic cleavage of the dioxygen bond of 9R-HPODE with formation of compound II

97 nclude that homolysis and heterolysis of the dioxygen bond with formation of compound II in AOS and c

98 This unprecedented dioxygen-bonded Cu(III) species with exclusive biologica

99 Cys soaks reveal a complex with Cys, but no dioxygen, bound.

100 the structural properties of the metastable dioxygen-bound complexes of the oxygenase domain of indu

101 lps control the reactivity of the heme-bound dioxygen by "shielding" it from water.

102 Rate enhancements for the reduction of dioxygen by a Mn(II) complex were observed in the presen

103 iiron center, reducing its reactivity toward dioxygen by about 300-fold compared with analogous compl

104 Living organisms have adapted to atmospheric dioxygen by exploiting its oxidizing power while protect

105 We found that the protonation of dioxygen by His396 via a proton-coupled electron transfe

106 ccepted mechanism for catalytic reduction of dioxygen by iron porphyrins, after checking its compatib

107 Protein effects in the activation of dioxygen by methane monooxygenase (MMO) were investigate

108 O-O bond cleaving step in the activation of dioxygen by nonheme iron enzymes and in the first step o

109 the Ca(2+) ion in the oxidation of water to dioxygen by the oxygen-evolving complex.

110 The binding and activation of dioxygen by transition metal complexes is a fundamentall

111 This diiron compound, in the presence of dioxygen, can oxidize external substrates.

112 It has been proposed that DHP evolved from a dioxygen carrier globin protein and therefore possesses

113 Using the electrochemical reduction of dioxygen catalyzed by iron porphyrins in DMF as an examp

114 Here, the reaction of reduced flavin and dioxygen catalyzed by pyranose 2-oxidase (P2O), a flavoe

115 dase trehalose anode and a bilirubin oxidase dioxygen cathode using Os complexes grafted to a polymer

116 riking analogies of copper/sulfur and copper/dioxygen chemistries, with regard to structure type form

117 Herein we describe the dioxygen chemistry of coordinatively unsaturated [Mn(II)

118 The dioxygen chemistry of manganese remains largely unexplor

119 hTDO is determined by the efficiency of the dioxygen chemistry, whereas that in hIDO is controlled b

120 xo to bis-mu-oxo species in transition metal-dioxygen chemistry.

121 eroxide dianion (O(2)(2-)) is a challenge in dioxygen chemistry.

122 the oxidation of the flavonol quercetin with dioxygen, cleaving the central heterocyclic ring and rel

123 Co with O2 gives a rare example of a side-on dioxygen complex of cobalt.

124 The dioxygen complex of the NOS enzyme from a thermophilic b

125 ructure of nNOS-NHA-NO, a close mimic to the dioxygen complex, provides a picture of the potential in

126 ted to the proximal oxygen of the heme-bound dioxygen complex, thus preventing cleavage of the O-O bo

127 yields when it was catalyzed by a palladium-dioxygen complex.

128 f biomimetic high-valent metal-oxo and metal-dioxygen complexes, which can be related to our understa

129 structures, and properties of derived copper-dioxygen complexes.

130 R(TMP) was inversely proportional to dioxygen concentration at [O(2)] > 50 muM, a dependence

131 2))) and apparent H(2)O(2) quantum yields on dioxygen concentration for both untreated and borohydrid

132 2,4,6-trimethylphenol (TMP) loss (R(TMP)) on dioxygen concentration was examined both for a variety o

133 ell as the dependence of RH2O2 on phenol and dioxygen concentrations are consistent with a mechanism

134 With a 1:1 ratio, the dioxygen consumption rate is 1.7 mumol L(-1) s(-1).

135 s, and O2-concentration studies demonstrated dioxygen consumption.

136 peptide bond, and the off-line geometry for dioxygen coordination.

137 Copper-dioxygen (CuO2) adducts are frequently proposed as inter

138 eologically reasonable changes in the global dioxygen cycle, suggesting that this CO2 source should b

139 hts into the reaction of reduced flavin with dioxygen, demonstrating that the positively charged resi

140 ble implication of O-type species in copper-/dioxygen-dependent enzymes such as tyrosinase (Ty) and p

141 oxidase superfamily and is thus crucial for dioxygen-dependent life.

142 roton-triggered reduction of the metal-bound dioxygen-derived fragment is discussed.

143 of a carbon-phosphorus bond using Fe(II) and dioxygen, despite belonging to a large family of hydroly

144 ign chemistries, it is most important to use dioxygen directly in lieu of toxic and/or corrosive stoi

145 Dioxygen displaces the disulfur moiety from 2 to produce

146 the rates deteriorate rapidly on exposure to dioxygen due to the degradation of F(A) and F(B).

147 t with induction of biofilm formation in low-dioxygen environments.

148 ntermediates suggest a detailed mechanism of dioxygen evolution based on changes in oxidization and p

149 ron enzymes that require FeII, alpha-KG, and dioxygen for catalysis with the alpha-KG cosubstrate sup

150 of toluene/o-xylene monooxygenase activates dioxygen for subsequent arene hydroxylation.

151 he substrate and the subsequent mechanism of dioxygen formation are discussed.

152 ion state of the heme environment influences dioxygen formation.

153 s it approaches a configuration conducive to dioxygen formation.

154 imetic diiron cofactor sites that react with dioxygen forming a 520 nm "intermediate" species with an

155 In each reaction the dioxygen fragment is reduced by 1e(-), so generation of

156 in biphasic radical arylation reactions with dioxygen from air as a most simple and readily available

157 ng complex (OEC) of photosystem II generates dioxygen from water using a catalytic Mn(4)CaO(n) cluste

158 ound RH can be reduced and subsequently bind dioxygen, generating oxyferrous DHP, which may represent

159 transition metal complexes that can activate dioxygen has been a challenging goal for the synthetic i

160 Dioxygen has been implicated as the oxidant in this unus

161 e, NO, the diatomic hybrid of dinitrogen and dioxygen, has extensive biochemical, industrial and atmo

162 ral years, intermediates in the reduction of dioxygen have been attributed diverse functional roles r

163 others that catalyse halide oxidation using dioxygen, hydrogen peroxide and hydroperoxides, or that

164 The Mn(II)2SH complex reacts with dioxygen in CH3CN, leading to the formation of a rare mo

165 both the redox state of the mNT cluster and dioxygen in cluster transfer and protein stability.

166 ansfer allows it to serve as an activator of dioxygen in cocatalyzed oxidations, for example, acting

167 is an electrocatalyst for water oxidation to dioxygen in H2PO4(-)/HPO4(2-) buffered aqueous solutions

168 se superoxide generated via the reduction of dioxygen in neutral aqueous solutions at a rotating disk

169 The conversion of water to dioxygen in photosynthesis illustrates one example, in w

170 lso decomposed hydrogen peroxide to liberate dioxygen in the absence of reducing equivalents.

171 d substitution of nitrosyl hydride (HNO) for dioxygen in the activity of Mn-QDO, resulting in the inc

172 t on the concentration of carbon dioxide and dioxygen in the atmosphere requires the fate of petrogen

173 and cyanobacteria has generated most of the dioxygen in the atmosphere.

174 ficiently catalyze the oxidation of water to dioxygen in the presence of a sacrificial oxidant.

175 transfer reagents, were found to react with dioxygen in the presence of B(C6 F5 )3 , a Lewis acid un

176 The reduction of dioxygen in the presence of sodium cations can be tuned

177 of the luminescent triplet state, caused by dioxygen in water and biological fluids, reduces their p

178 that in hIDO is performed by the heme-bound dioxygen; in addition, the stereospecificity of hTDO is

179 on(II) and alpha-ketoglutarate (alphaKG), to dioxygen initiates oxidation in crystallo.

180 At low-temperatures, a dioxygen intermediate, [Mn(S(Me2)N4(6-Me-DPEN))(O2)](+)

181 nzyme to reduce O(2) rapidly, converting the dioxygen into harmless water before it can damage the pr

182 at catalyzes the activation and insertion of dioxygen into L-Trp.

183 where the subsequent sigma bond insertion of dioxygen into the C-Fe bond completes the reaction.

184 enase that incorporates one oxygen atom from dioxygen into the carbon and the other to the arsenic to

185 ds resulting in the insertion of one atom of dioxygen into the organic substrate and the reduction of

186 cifically on the direct insertion pathway of dioxygen into the Pd-H bond and pathways proceeding thro

187 porates both oxygen atoms of its cosubstrate dioxygen into the rubber cleavage product ODTD, and we s

188 simultaneous incorporation of both atoms of dioxygen into the substrate.

189 molecule to the four electrons reduction of dioxygen into water.

190 the MCO family, leading to photoreduction of dioxygen into water.

191 The activation of dioxygen is a key step in CO oxidation catalyzed by gold

192 n of selenocysteine or selenohomocysteine by dioxygen is achieved within a few minutes at neutral pH

193 Dioxygen is formed rapidly with an initial turnover freq

194 uble-laser excitation is introduced in which dioxygen is generated by photolyzing the O(2)-carrier wi

195 nsfer to a generic acceptor protein and that dioxygen is neither required for the cluster transfer re

196 In all three structures, dioxygen is observed bound to the iron in a side-on fash

197 actions, the catalytic oxidation of water to dioxygen is one of the crucial processes that need to be

198 uster composed of the T2 and T3 sites, where dioxygen is reduced to water in two sequential 2e(-) ste

199 After formation of the S4 state, the product dioxygen is released and the cofactor returns to its low

200 ausible reason for the low reactivity toward dioxygen is revealed by the crystal structure of the com

201 s distal mutants suggest that the heme-bound dioxygen is stabilized by H-bonds donated from the Tyr(B

202 (PROS) in the electrocatalytic reduction of dioxygen, is a function of 2 rates: (i) the rate of elec

203 water oxidation, where water is oxidized to dioxygen, is a fundamental chemical reaction that sustai

204 While 1 is stable toward dioxygen, its reaction with dioxygen under NO atmosphere

205 P4 molecules readily react with atmospheric dioxygen, leading this form of the element to spontaneou

206 olecule H-bonded to the distal oxygen of the dioxygen ligand.

207 group of the substrate hydrogen-bonds to the dioxygen ligand.

208 ogenase rapidly decompose in the presence of dioxygen, many free-living diazotrophs are obligate aero

209 These species are composed of metal-dioxygen, metal-superoxo, metal-peroxo, and metal-oxo ad

210 ng/folding, but rather programmed routes for dioxygen migration through the protein matrix.

211 ution; and S-HPP-Fe(II)-HppE in complex with dioxygen mimic NO at 2.9 A resolution.

212 thranilate reaction product, and chloride as dioxygen mimic.

213 Maximum of three dioxygen molecules can bind to the cluster, and they are

214 ion pathway that falls short in dissociating dioxygen molecules.

215 f reducing a variety of substrates including dioxygen, nitric oxide, nitrous oxide, 1-azido adamantan

216 Dioxygen (O(2)) and other gas molecules have a fundament

217 rds the metal-ligand water molecule, where a dioxygen O2 molecule would occupy to initiate the next r

218 reaction of transition-metal complexes with dioxygen (O2 ) is important for understanding oxidation

219 ires superoxide anion (O2(.-) ), rather than dioxygen (O2 ), to access a high-valent Mn2 oxidant.

220 Switching from hydrogen peroxide (H2O2) to dioxygen (O2) as the primary oxidant was achieved by usi

221 the cleavage of non-aromatic double bonds by dioxygen (O2) to form aldehyde or ketone products.

222 hemoglobin (Hb) changes with the binding of dioxygen (O2) to the heme prosthetic groups of the globi

223 II) intermediate formed during reaction with dioxygen of the reduced hydroxylase component of toluene

224 Most of the dioxygen on earth is generated by the oxidation of water

225 minal components for reductive scavenging of dioxygen or nitric oxide to combat oxidative or nitrosat

226 Dioxygen plays an important role in OCl(-)-mediated AgNP

227 ons of triplet quenchers relative to that of dioxygen produced only small decreases (sorbic acid) or

228 vent, and in many instances an atmosphere of dioxygen, promote the oxidative reaction to afford 5,5'-

229 Current interest in copper/dioxygen reactivity includes the influence of thioether

230 es, but not the channel, changed the rate of dioxygen reactivity with the enzyme.

231 (PaPy2Q)(OH)]ClO4 (3), though insensitive to dioxygen, reacts with nitric oxide (NO) to afford the ni

232 s, Schmidt and Sherwood, in the context of a dioxygen-reducing-biocathode, under different flow-rate

233 unactivated C-H bonds, water oxidation, and dioxygen reduction are extremely important reactions in

234 bsorption study, we compared the kinetics of dioxygen reduction by ba(3) cytochrome c oxidase from Th

235 problems remain pending in the catalysis of dioxygen reduction by iron porphyrins in water in terms

236 eport a general kinetics model for catalytic dioxygen reduction on multicopper oxidase (MCO) cathodes

237 provides deep mechanistic insights into the dioxygen reduction process that should serve as useful a

238 Mechanistic investigations of dioxygen reduction revealed that the reaction proceeds t

239 Complex 1 acts as a unique catalyst for dioxygen reduction, whose selectivity can be changed fro

240 yl motif and involving the U(VI/V) couple in dioxygen reduction.

241 n be changed from a preferential 4e(-)/4H(+) dioxygen-reduction (to water) to a 2e(-)/2H(+) process (

242 on of general interest, so that reduction of dioxygen remains a topic of high importance in the conte

243 n of flavin by NADPH and, in the presence of dioxygen, result in the stoichiometric liberation of hyd

244 e after reaction of the reduced protein with dioxygen-saturated buffer was investigated by tryptic di

245 second emission lifetimes that are efficient dioxygen sensors.

246 bonds requires trapping of a triplet radical dioxygen species by a cis-[Re(V)(O)(cat)(2)](-) anion.

247 in Co-BTTri are best described as cobalt(II)-dioxygen species with partial electron transfer, while t

248 The common reactions of dioxygen, superoxide, and hydroperoxides with thiolates

249 High-valent metal-oxo and metal-dioxygen (superoxo, peroxo, and hydroperoxo) cores act a

250 Its reaction with dioxygen takes place rapidly at ambient conditions to gi

251 rminal enzyme of cellular respiration at low dioxygen tensions.

252 which is substantially less reactive toward dioxygen than the reduced reductase in the absence of NA

253 nt turnover number (0.5 s(-1) in atmospheric dioxygen) that is at least 2 orders of magnitude more ra

254 marily through this H-bond, causes the bound dioxygen to adopt a new conformation, which presumably i

255 pen coordination positions on both irons for dioxygen to bridge.

256 dation of AgNPs by OCl(-) in the presence of dioxygen to catalytic removal of OCl(-) by AgNPs in the

257 an unusual mononuclear iron enzyme that uses dioxygen to catalyze the oxidative epoxidation of (S)-2-

258 odinuclear Mn(II)/Fe(II) complex reacts with dioxygen to form a Mn(IV)/Fe(IV) intermediate, which und

259 The reduced cofactor then reacts with dioxygen to form hydrogen peroxide and releases nicotina

260 ue in copper hydroxylating enzymes activates dioxygen to form unknown oxidants, generally assumed as

261 to-5-methylthiopent-1-ene (acireductone) and dioxygen to generate formate and the ketoacid precursor

262 investigations indicated that 2 reacts with dioxygen to give a mixture of (mu-oxo)diiron(III) [Fe(2)

263 OD) catalyzes the spin-forbidden transfer of dioxygen to its N-heteroaromatic substrate in the absenc

264 H), a diiron-containing enzyme, can activate dioxygen to oxidize aromatic substrates.

265 ne and four glutamate residues and activates dioxygen to perform its role in the biosynthetic pathway

266 PmaLAAD does not use dioxygen to re-oxidize reduced FADH2 and thus does not p

267 The ketyl radical then reacts rapidly with dioxygen to regenerate the ketone and form superoxide (O

268 sible pathways for the diffusion of iron and dioxygen to the ferroxidase centers.

269 ordered stepwise binding of ferrous iron and dioxygen to the ferroxidase site in preparation for cata

270 his reaction depends on the concentration of dioxygen to the first order.

271 at the photodissociated CO impedes access of dioxygen to the heme a(3) site in ba(3), making the CO f

272 the peroxide resulting from the addition of dioxygen to the radical.

273 d decay of two species formed by addition of dioxygen to the reduced, diiron(II) state by rapid-freez

274 tion of their structures in the reduction of dioxygen to water by cytochrome c oxidase (CcO) are part

275 in, catalyzes the four-electron reduction of dioxygen to water in a binuclear center comprised of a h

276 t3p catalyzes the four-electron reduction of dioxygen to water, coupled to the one-electron oxidation

277 ogical processes, including the reduction of dioxygen to water, the reduction of CO(2) to formate, an

278 h the concomitant four-electron reduction of dioxygen to water.

279 tic hydrogel that catalyzes the reduction of dioxygen to water.

280 r(eta(2)-C2(SiMe3)2) (1) reacts rapidly with dioxygen to yield chromium(V) dioxo species (i-Pr2Ph)2na

281 f biomimetic Fe/Mn complexes that react with dioxygen to yield such observable metal-oxygen species a

282 They reduce molecular oxygen (dioxygen) to water, avoiding the production of reactive

283 is stable toward dioxygen, its reaction with dioxygen under NO atmosphere forms the {FeNO}(6)(ONO) co

284 This {FeNO}(7) complex reacts with dioxygen upon photoirradiation with visible light in ace

285 x-protective role, approximately half of the dioxygen-using oxidoreductases have Tyr/Trp chain length

286 Dioxygen was detected in yields ranging between 64% and

287 In the water-DEAS system, the evolution of dioxygen was monitored in situ in the aqueous phase by u

288 The dioxygen we breathe is formed by light-induced oxidation

289 y to initiate Fe-S transfer independently of dioxygen, whereas the reduced state is a "dormant form."

290 ydroquinone solution are rapidly oxidized by dioxygen, while the semiquinone radicals generated in SR

291 y produced during the catalytic reduction of dioxygen with 80-84% selectivity, making the Mn(II)2SH c

292 The interaction of dioxygen with a manganese(II) complex (1) of bis[(N'-ter

293 ial low temperature interaction of NH(3) and dioxygen with microporous layers of Co-porphyrins.

294 the dismutation of chlorite to chloride and dioxygen with no other side products.

295 intermolecular C-H activation; reactions of dioxygen with Pt(II) complexes that may be relevant to s

296 e oxygenase (RO), catalyzes the insertion of dioxygen with stereo- and regioselectivity at the 2,3-ca

297 formally spin-forbidden reactions of triplet dioxygen with the closed shell oxorhenium(V) anions.

298 SRFA solution are resistant to oxidation by dioxygen, with the result that steady-state semiquinone

299 first-order each in ionized hydroquinone and dioxygen, yielding hydrogen peroxide stoichiometrically.

300 In the presence of dioxygen, zinc is observed bound to all three sites.