ライフサイエンスコーパス: dioxygen

1 e major electron carrier in the reduction of dioxygen.

2 the basis of the slow reaction of PHD2 with dioxygen.

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

4 er enhances the electron acceptor ability of dioxygen.

5 t work to ameliorate the effects of limiting dioxygen.

6 isate, which was subsequently incubated with dioxygen.

7 ted to active oxygen species or to dissolved dioxygen.

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

9 ring the reaction of the reduced flavin with dioxygen.

10 Complexes 1 and 2 both react rapidly with dioxygen.

11 neurosporene derivatives in the presence of dioxygen.

12 to dihydrogen and the oxidation of water to dioxygen.

13 such as transferring electrons or activating dioxygen.

14 talyzes the oxidative conversion of water to dioxygen.

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

16 lizes the selective and tunable reduction of dioxygen.

17 active towards external substrates including dioxygen.

18 nner-sphere reduction of both superoxide and dioxygen.

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

20 dation of dimethoxyphenol in the presence of dioxygen.

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

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

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

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

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

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

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

28 This work provides a rare example of dioxygen activation at a mononuclear nonheme iron(II) co

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

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

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

32 Dioxygen activation by the reduced T201 variants was exp

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

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

35 nooxygenase in methane hydroxylation-through dioxygen activation mechanisms.

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

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

38 970s-1980s, the current understanding of the dioxygen activation process in flavoenzymes is believed

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

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

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

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

43 TIM-barrel-fold enzymes for metal-dependent dioxygen activation, with the majority predicted to act

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

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

46 evealing that T201 is critically involved in dioxygen activation.

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

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

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

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

51 can determine for an initially formed metal-dioxygen adduct, whether it exists as a superoxide or a

52 e2))((tBu2)APH)], gives rise to two distinct dioxygen adducts at reduced temperatures.

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

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

55 Dioxygen and beta-mercaptoethanol are unable to compete

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

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

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

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

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

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

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

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

64 s of the PHDs, in particular a high K(m) for dioxygen and slow reaction with dioxygen, are proposed t

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

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

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

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

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

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

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

72 igh K(m) for dioxygen and slow reaction with dioxygen, are proposed to enable their hypoxia-sensing r

73 scope, mild reaction conditions, and use of dioxygen as an oxidant both for catalyst regeneration an

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

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

76 wed by a catalytic cycle through a molecular-dioxygen-assisted pathway.

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

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

79 a reaction enabling adaptation to different dioxygen availability.

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

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

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

83 Dioxygen binding is shown to be reversible with complexe

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

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

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

87 omplex in ADO, suggesting the possibility of dioxygen binding to the iron ion in a side-on mode.

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

89 influence the kinetics and thermodynamics of dioxygen binding versus release from structurally analog

90 provide evidence for a catalytic cycle where dioxygen binds prior to NO to generate an active iron(II

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

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

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

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

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

96 ibrium between dioxygen in bulk solution and dioxygen bound to the PHD2.Fe.2OG.HIF-alpha substrate co

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

98 lectrodes for reduction of carbon dioxide or dioxygen, but determining how strain affects the hydroge

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

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

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

102 The activation of dioxygen by Fe(II)(Me(3)TACN)(S(2)SiMe(2)) (1) is report

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

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

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

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

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

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

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

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

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

112 The dioxygen chemistry of manganese remains largely unexplor

113 The reaction landscape for the dioxygen chemistry of the more electron-rich complexes i

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

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

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

117 the mechanism for conversion of the ferrous-dioxygen complex into the reactive ferryl intermediate.

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

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

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

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

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

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

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

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

126 2,4,6-trimethylphenol (TMP) loss (R(TMP)) on dioxygen concentration was examined both for a variety o

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

128 llular studies, TgPhyA is more active at low dioxygen concentrations than DdPhyA.

129 ls was used to monitor in situ variations of dioxygen consumed by all mitochondria captured in the de

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

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

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

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

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

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

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

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

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

139 bined with QM/MM trajectories to investigate dioxygen diffusion to, and binding at, the active site i

140 actor, an active-site density interpreted as dioxygen, distinct water-filled proton channels, and an

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

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

143 Water oxidation and concomitant dioxygen formation by the manganese-calcium cluster of o

144 s it approaches a configuration conducive to dioxygen formation.

145 ion state of the heme environment influences dioxygen formation.

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

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

148 etermining step of the OER as the release of dioxygen from the superoxide intermediate.

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

150 trained by the side activity of Rubisco with dioxygen, generating 2-phosphoglycolate.

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

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

153 Dioxygen has been implicated as the oxidant in this unus

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

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

156 nce of stoichiometric triethyl phosphite and dioxygen in air as the terminal redox reagents (redox de

157 e a manifestation of the equilibrium between dioxygen in bulk solution and dioxygen bound to the PHD2

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

180 They imply that the reversible binding of dioxygen is central to the hypoxia-sensing capacity of t

181 An understanding of how dioxygen is delivered to, and binds at, the active site

182 Dioxygen is formed rapidly with an initial turnover freq

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

184 eavage of the indole ring of tryptophan with dioxygen is mediated by two heme enzymes, tryptophan 2,3

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

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

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

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

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

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

191 obtained from photosensitization of triplet dioxygen is shown to react with an alkene surfactant (8-

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

193 nly trigger their degradation, peroxide, and dioxygen, is orders of magnitude slower in comparison.

194 s Communication demonstrates that water, not dioxygen, is the main source of the oxygen present in th

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

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

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

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

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

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

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

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

203 thranilate reaction product, and chloride as dioxygen mimic.

204 ing the EBFCs in the presence of glucose and dioxygen, model drug compounds incorporated in the CP la

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

206 ion pathway that falls short in dissociating dioxygen molecules.

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

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

209 enging due to the necessity of a microscopic dioxygen (O(2)) concentration gradient, which reconciles

210 oluble methane monooxygenase enzymes (sMMO), dioxygen (O(2)) is activated at a diiron(II) center to f

211 The selective electrocatalytic reduction of dioxygen (O(2)) to hydrogen peroxide (H(2)O(2)) could be

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

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

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

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

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

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

218 For example, the cleavage of dioxygen often produces an iron(IV)-oxo that has been ch

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

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

221 s that define a diffusion-reaction model for dioxygen:PHD2 interactions; in combination with reported

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

223 tanding of (bio)chemical processes involving dioxygen processing.

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

225 at the reaction of the diferrous enzyme with dioxygen produces stoichiometric product per cluster.

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

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

228 Herein, we examine the dioxygen reactivity of a new Mn(II) complex containing a

229 The dioxygen reactivity of a series of TMPA-based copper(I)

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

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

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

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

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

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

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

237 D) for direct electron transfer (DET) in the dioxygen reduction reaction (ORR) at neutral pH.

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 substrate combinations might have different dioxygen sensitivity profiles.

244 second emission lifetimes that are efficient dioxygen sensors.

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

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

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

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

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

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

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

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

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

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

255 iolate-ligated iron complex that reacts with dioxygen to form an unprecedented example of an iron sup

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

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

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

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

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

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

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

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

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

265 The transport of dioxygen to the active site is described; dioxygen trans

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

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

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

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

270 Cytochrome c oxidase (CcO) reduces dioxygen to water and harnesses the chemical energy to d

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

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

273 e c oxidase (CcO) catalyzes the reduction of dioxygen to water utilizing a heterobinuclear active sit

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

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

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

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

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

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

280 of dioxygen to the active site is described; dioxygen transport follows a single well-defined hydroph

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

282 esigned a binding site with accessibility to dioxygen units in the open coordination site of the Mn c

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

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

285 Dioxygen was detected in yields ranging between 64% and

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

287 rresponding to a diatomic molecule (probably dioxygen) was sandwiched between the heme iron atom and

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 adsorbents capable of selectively capturing dioxygen with a high reversible capacity is a crucial go

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

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

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

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

297 involved in the activation and reduction of dioxygen, with only few exceptions known.

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.