PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 164901-2 1975 Water relaxation studies at 8, 24, 100, and 220 MHz indicate two classes of bound Co(II). Water 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 82-88 164901-7 1975 This distance decreases to 6.9 A when NADH is bound, and a Co(II) to methyne proton distance of 6.6 A is determined indicating a conformation change leading to the formation of a second sphere enzyme-Co(II)-isobutyramide complex in which a hydroxyl or water ligand intervenes between the metal and the substrate analog. Water 252-257 mitochondrially encoded cytochrome c oxidase II Homo sapiens 59-64 164901-7 1975 This distance decreases to 6.9 A when NADH is bound, and a Co(II) to methyne proton distance of 6.6 A is determined indicating a conformation change leading to the formation of a second sphere enzyme-Co(II)-isobutyramide complex in which a hydroxyl or water ligand intervenes between the metal and the substrate analog. Water 252-257 mitochondrially encoded cytochrome c oxidase II Homo sapiens 59-65 164901-10 1975 The role of the catalytic Co(II) thus appears to be the activation of a hydroxyl or water ligand which polarizes the aldehyde carbonyl group by hydrogen bonding. Water 84-89 mitochondrially encoded cytochrome c oxidase II Homo sapiens 26-32 33904544-7 2021 The UV-vis absorbance of CoII further corroborates TX-100-assisted water pool formation within TBAC-DA via the appearance of the band that is assigned to the response of the probe in water. Water 67-72 mitochondrially encoded cytochrome c oxidase II Homo sapiens 25-29 33980833-5 2021 In this study, we determine that the magnetic anisotropy of a Co(II) complex can be effectively controlled by the slight rotation of coordinating water ligands, which is achieved by a two-step structural phase transition. Water 146-151 mitochondrially encoded cytochrome c oxidase II Homo sapiens 62-68 33904544-7 2021 The UV-vis absorbance of CoII further corroborates TX-100-assisted water pool formation within TBAC-DA via the appearance of the band that is assigned to the response of the probe in water. Water 183-188 mitochondrially encoded cytochrome c oxidase II Homo sapiens 25-29 33300509-0 2021 Accessing water processable cyanido bridged chiral heterobimetallic Co(II)-Fe(III) one dimensional network. Water 10-15 mitochondrially encoded cytochrome c oxidase II Homo sapiens 68-74 33823482-1 2021 The reaction between Co(II) and PMS is an appealing advanced oxidation process (AOP), where multiple reactive oxidizing species (ROS) including high-valent cobalt-oxo [Co(IV)], sulfate radical (SO4 -), and hydroxy radical ( OH) are intertwined together for degrading pollutants. Water 206-221 mitochondrially encoded cytochrome c oxidase II Homo sapiens 21-27 33851772-0 2021 Water-assisted concerted proton-electron transfer at Co(II)-aquo sites in polyoxotungstates with photogenerated RuIII(bpy)33+ oxidant. Water 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 53-59 33851772-2 2021 Mechanistic evidence has been acquired indicating that: (i) the one-electron oxidation of Co6 involves Co(II) aquo or Co(II) hydroxo groups (abbreviated as Co6(II)-OH2 and Co6(II)-OH, respectively, whose speciation in aqueous solution is associated to a pKa of 7.6), and generates a Co(III)-OH moiety (Co6(III)-OH), as proven by transient absorption spectroscopy; (ii) at pH > pKa, the Co6(II)-OH RuIII(bpy)33+ ET occurs via bimolecular kinetics, with a rate constant k close to the diffusion limit and dependent on the ionic strength of the medium, consistent with reaction between charged species; (iii) at pH < pKa, the process involves Co6(II)-OH2 Co6(III)-OH transformation and proceeds via a multiple-site, concerted proton electron transfer (CPET) where water assists the transfer of the proton, as proven by the absence of effect of buffer base concentrations on the rate of the ET and by a H/D kinetic isotope in a range of 1.2 - 1.4. Water 765-770 mitochondrially encoded cytochrome c oxidase II Homo sapiens 103-109 33851772-3 2021 The reactivity of water is ascribed to its organization on the surface of the polyanionic scaffold through hydrogen bond networking involving the Co(II)-OH2 group. Water 18-23 mitochondrially encoded cytochrome c oxidase II Homo sapiens 146-152 33595555-10 2021 The sensor showed high selectivity and efficiency for simultaneous determination of Cu(ii), Co(ii), Ni(ii), Hg(ii), and Mn(ii) in drinking, tap, and pond water samples on a single device and detection with the naked eye. Water 154-159 mitochondrially encoded cytochrome c oxidase II Homo sapiens 87-89 33504835-9 2021 The proposed method was successfully applied for the analysis of the As(III), Cd(II), Cr(III), Co(II), Ni(II), and Pb(II) ions in different environmental water samples. Water 154-159 mitochondrially encoded cytochrome c oxidase II Homo sapiens 95-101 33045697-2 2021 These water-durable frameworks exhibit varied hydrogen production rates of 361.2, 271.3, and 327.5 mumol g-1 h-1 in 12 hour due to their slightly different donor environments of the octahedral CdII and CoII ions. Water 6-11 mitochondrially encoded cytochrome c oxidase II Homo sapiens 202-206 33300509-1 2021 A water processable cyanido bridged extended chiral heterobimetallic Co(ii)-Fe(iii) network is assembled. Water 2-7 mitochondrially encoded cytochrome c oxidase II Homo sapiens 69-75 32652152-0 2020 Biologically active Co (II), Cu (II), Zn (II) centered water soluble novel isoniazid grafted O-carboxymethyl chitosan Schiff base ligand metal complexes: Synthesis, spectral characterisation and DNA nuclease activity. Water 55-60 mitochondrially encoded cytochrome c oxidase II Homo sapiens 20-27 33100004-0 2020 Versatility of Amide-Functionalized Co(II) and Ni(II) Coordination Polymers: From Thermochromic-Triggered Structural Transformations to Supercapacitors and Electrocatalysts for Water Splitting. Water 177-182 mitochondrially encoded cytochrome c oxidase II Homo sapiens 36-42 33520284-9 2021 The title compound is isotypic with its CoII and MnII analogues: the three K2 M 3(OH)2(SO4)3(H2O)2 (M = Mg, Co, Mn) structures are qu-anti-tatively compared. Water 93-96 mitochondrially encoded cytochrome c oxidase II Homo sapiens 40-44 33179662-0 2020 Water soluble ionic Co(II), Cu(II) and Zn(II) diimine-glycinate complexes targeted to tRNA: structural description, in vitro comparative binding, cleavage and cytotoxic studies towards chemoresistant prostate cancer cells. Water 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 20-26 33179662-0 2020 Water soluble ionic Co(II), Cu(II) and Zn(II) diimine-glycinate complexes targeted to tRNA: structural description, in vitro comparative binding, cleavage and cytotoxic studies towards chemoresistant prostate cancer cells. Water 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 23-25 33179662-1 2020 Four new water soluble Co(ii), Cu(ii) and Zn(ii) ionic metal complexes (1-4) [Cu(diimine)(H2O)2(glycinate)]+[glycinate]-, [Co(diimine)(H2O)4]+[glycinate]- and [Zn(diimine) (H2O)4]+[glycinate]-, where diimine = 2,2"-bipyridine (1-3) and 1,10-phenanthroline (4) were synthesized and thoroughly characterized by spectroscopic and single X-ray crystallographic studies. Water 9-14 mitochondrially encoded cytochrome c oxidase II Homo sapiens 23-29 33179662-1 2020 Four new water soluble Co(ii), Cu(ii) and Zn(ii) ionic metal complexes (1-4) [Cu(diimine)(H2O)2(glycinate)]+[glycinate]-, [Co(diimine)(H2O)4]+[glycinate]- and [Zn(diimine) (H2O)4]+[glycinate]-, where diimine = 2,2"-bipyridine (1-3) and 1,10-phenanthroline (4) were synthesized and thoroughly characterized by spectroscopic and single X-ray crystallographic studies. Water 9-14 mitochondrially encoded cytochrome c oxidase II Homo sapiens 26-28 33179662-1 2020 Four new water soluble Co(ii), Cu(ii) and Zn(ii) ionic metal complexes (1-4) [Cu(diimine)(H2O)2(glycinate)]+[glycinate]-, [Co(diimine)(H2O)4]+[glycinate]- and [Zn(diimine) (H2O)4]+[glycinate]-, where diimine = 2,2"-bipyridine (1-3) and 1,10-phenanthroline (4) were synthesized and thoroughly characterized by spectroscopic and single X-ray crystallographic studies. Water 90-93 mitochondrially encoded cytochrome c oxidase II Homo sapiens 23-29 32652152-1 2020 In this study, the new N, N, O tridentate donor water soluble isoniazid based biopolymer Schiff base ligand and their Co (II), Cu (II), Zn (II) metal complexes were prepared. Water 48-53 mitochondrially encoded cytochrome c oxidase II Homo sapiens 118-125 32659957-1 2020 The present work introduces both synthesis of silica nanoparticles doped with CoII ions by means of differently modified microemulsion water-in-oil (w/o) and Stober techniques and characterization of the hybrid nanoparticles (CoII@SiO2) by TEM, DLS, XRD, ICP-EOS, SAXS, UV-Vis, and UV-Vis/DR spectroscopy and electrochemical methods. Water 135-140 mitochondrially encoded cytochrome c oxidase II Homo sapiens 78-82 33076661-3 2020 [CuII(H2O)8/3]3/2[FeII(CN)5(NH3)] showed higher catalytic activity than [CoII(H2O)8/3]3/2[FeII(CN)5(NH3)] and [GaIII(H2O)][FeII(CN)5(NH3)], although N-bound CuII species has been reported as less active than CoII and GaIII species in conventional PBAs. Water 6-9 mitochondrially encoded cytochrome c oxidase II Homo sapiens 73-77 33076661-3 2020 [CuII(H2O)8/3]3/2[FeII(CN)5(NH3)] showed higher catalytic activity than [CoII(H2O)8/3]3/2[FeII(CN)5(NH3)] and [GaIII(H2O)][FeII(CN)5(NH3)], although N-bound CuII species has been reported as less active than CoII and GaIII species in conventional PBAs. Water 6-9 mitochondrially encoded cytochrome c oxidase II Homo sapiens 208-212 33076661-3 2020 [CuII(H2O)8/3]3/2[FeII(CN)5(NH3)] showed higher catalytic activity than [CoII(H2O)8/3]3/2[FeII(CN)5(NH3)] and [GaIII(H2O)][FeII(CN)5(NH3)], although N-bound CuII species has been reported as less active than CoII and GaIII species in conventional PBAs. Water 78-81 mitochondrially encoded cytochrome c oxidase II Homo sapiens 73-77 33076661-3 2020 [CuII(H2O)8/3]3/2[FeII(CN)5(NH3)] showed higher catalytic activity than [CoII(H2O)8/3]3/2[FeII(CN)5(NH3)] and [GaIII(H2O)][FeII(CN)5(NH3)], although N-bound CuII species has been reported as less active than CoII and GaIII species in conventional PBAs. Water 78-81 mitochondrially encoded cytochrome c oxidase II Homo sapiens 208-212 33076661-3 2020 [CuII(H2O)8/3]3/2[FeII(CN)5(NH3)] showed higher catalytic activity than [CoII(H2O)8/3]3/2[FeII(CN)5(NH3)] and [GaIII(H2O)][FeII(CN)5(NH3)], although N-bound CuII species has been reported as less active than CoII and GaIII species in conventional PBAs. Water 78-81 mitochondrially encoded cytochrome c oxidase II Homo sapiens 73-77 33076661-3 2020 [CuII(H2O)8/3]3/2[FeII(CN)5(NH3)] showed higher catalytic activity than [CoII(H2O)8/3]3/2[FeII(CN)5(NH3)] and [GaIII(H2O)][FeII(CN)5(NH3)], although N-bound CuII species has been reported as less active than CoII and GaIII species in conventional PBAs. Water 78-81 mitochondrially encoded cytochrome c oxidase II Homo sapiens 208-212 33076661-4 2020 IR measurements of a series of the CN-deficient PBAs after the catalytic reactions clarified that a part of the NH3 ligands remained on [CoII(H2O)8/3]3/2[FeII(CN)5(NH3)] and that hydrogen phosphate formed as a product strongly adsorbed on the FeII ions of [GaIII(H2O)][FeII(CN)5(NH3)]. Water 142-145 mitochondrially encoded cytochrome c oxidase II Homo sapiens 137-141 33076661-4 2020 IR measurements of a series of the CN-deficient PBAs after the catalytic reactions clarified that a part of the NH3 ligands remained on [CoII(H2O)8/3]3/2[FeII(CN)5(NH3)] and that hydrogen phosphate formed as a product strongly adsorbed on the FeII ions of [GaIII(H2O)][FeII(CN)5(NH3)]. Water 263-266 mitochondrially encoded cytochrome c oxidase II Homo sapiens 137-141 33209348-7 2020 The asymmetric unit of the complex is comprised of half the pyridine ring and water mol-ecule with the CoII atom at the center of the pincer situated about a twofold axis. Water 78-83 mitochondrially encoded cytochrome c oxidase II Homo sapiens 103-107 32969214-4 2020 This study provides the first account of how CoII imine based supramolecules can be employed as H2O oxidation catalysts. Water 96-99 mitochondrially encoded cytochrome c oxidase II Homo sapiens 45-49 32945437-8 2020 The results revealed that Nitrodi spring water promoted cell migration and cell viability, and downregulated protein S-nitrosylation, probably also the nitrosylated active form of the cyclooxygenase (COX)-2 protein. Water 41-46 mitochondrially encoded cytochrome c oxidase II Homo sapiens 184-206 32840539-3 2020 The notable differences are (a) the binding mode of the tridentate part of polypyridyl ligands to the Co(ii) center is facial in 1a, 3a and 4a but meridional in 2a, (b) the Co(ii) centers in 1a-3a are hexacoordinated (with a coordinated water in 1a and 3a) but are pentacoordinated in 4a, and (c) the binding mode of tdc linker is bis(monodentate) in 1a, 3a and 4a but chelated in one end and monodentate in the other end in 2a. Water 237-242 mitochondrially encoded cytochrome c oxidase II Homo sapiens 102-108 32361496-0 2020 Efficient removal of triclosan via peroxymonosulfate activated by a ppb level dosage of Co(II) in water: Reaction kinetics, mechanisms and detoxification. Water 98-103 mitochondrially encoded cytochrome c oxidase II Homo sapiens 88-94 32510942-1 2020 Reaction of the metalloligand IrIII(ppy-COOH)3 and the anisotropic paramagnetic CoII ion under solvothermal conditions resulted in a metal-metalloligand coordination polymer, [CoII3(mu3-O)(mu-OH2){IrIII(ppy-COO)2(ppy-COOH)}2(H2O)4] 2DMF xH2O (I). Water 225-228 mitochondrially encoded cytochrome c oxidase II Homo sapiens 80-84 31497810-0 2019 Water-mediated proton conduction in Ni(ii) and Co(ii) benzenetriphosphonates. Water 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 39-41 32420829-1 2021 The results of experimental study on effectiveness of gas phase total oxidation of toluene towards carbon dioxide and water with the aid of ozone over Co(II)/ SiO2 catalyst are presented in this work. Water 118-123 mitochondrially encoded cytochrome c oxidase II Homo sapiens 151-157 32391690-1 2020 Three mononuclear octahedral Co(II) complexes are reported, [Co(py)4(SCN)2] (1), [Co(py)4(Cl)2] H2O (2), and [Co(py)4(Br)2] (3), that exhibit different distortions with compression (1) or elongation (2 and 3) of the axial positions. Water 96-99 mitochondrially encoded cytochrome c oxidase II Homo sapiens 29-35 32250753-0 2020 Nano-manganese oxide-functionalized-oleyl amine as a simple and low cost nanosorbent for remediation of ZnII/CoII and their radioactive nuclides 65Zn and 60Co from water. Water 164-169 mitochondrially encoded cytochrome c oxidase II Homo sapiens 109-113 31832938-0 2020 Facile fabrication of magnetic phosphorylated chitosan for the removal of Co(II) in water treatment: separation properties and adsorption mechanisms. Water 84-89 mitochondrially encoded cytochrome c oxidase II Homo sapiens 74-80 31698185-1 2020 A "scorpionate" type precursor [bdtbpza = bis(3,5-di-t-butylpyrazol-1-yl)acetate] has been employed to synthesize two mononuclear ZnII and CoII derivatives, namely [Zn(bdtbpza)2 (H2O)2] 2.5CH3OH 2[(CH3)3C-C3H2N2-C(CH3)3] (1) and [Co(bdtbpza)2(CH3OH)4] (2) in good yield. Water 179-182 mitochondrially encoded cytochrome c oxidase II Homo sapiens 139-143 32189464-2 2020 A neutral cobalt(II) complex, [Co II (COO-terpy) 2 ] 4H 2 O ( 1 4H 2 O ), stably formed cavities generated via pi-pi stacking motifs and hydrogen bond networks, resulted in the accommodation of four water molecules. Water 199-204 mitochondrially encoded cytochrome c oxidase II Homo sapiens 31-36 32432869-1 2020 The homodinuclear CoII helicate complex [CoII(DQPD)]2 (1) was prepared by treating [Co(H2O)6](ClO4)2 with the deprotonated form of the ligand N2,N6-bis(quinolin-8-yl)pyridine-2,6-dicarboxamide (DQPDH2). Water 87-90 mitochondrially encoded cytochrome c oxidase II Homo sapiens 18-22 32432869-1 2020 The homodinuclear CoII helicate complex [CoII(DQPD)]2 (1) was prepared by treating [Co(H2O)6](ClO4)2 with the deprotonated form of the ligand N2,N6-bis(quinolin-8-yl)pyridine-2,6-dicarboxamide (DQPDH2). Water 87-90 mitochondrially encoded cytochrome c oxidase II Homo sapiens 41-45 31497810-0 2019 Water-mediated proton conduction in Ni(ii) and Co(ii) benzenetriphosphonates. Water 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 47-53 31041973-1 2019 A coordination compound with the composition [CoLCl2] H2O (L = bis-condensation product of diacetyl and 2-hydrazinyl-4,6-dimethylpyrimidine) was synthesized, in which the Co(ii) ion was hexacoordinated. Water 54-57 mitochondrially encoded cytochrome c oxidase II Homo sapiens 171-177 31201908-7 2019 Experimentally, P(DADMAC-AAm)CMC/Fe2O3 and P(DADMAC-SA)CMC/Fe2O3 show high sorption capacity of Co(II), i.e. 69.67 mg g-1 and 75.17 mg g-1, respectively, which makes them potential sorbents for Co(II) removal from water/wastewater. Water 214-219 mitochondrially encoded cytochrome c oxidase II Homo sapiens 96-102 31247845-0 2019 Exploring Inner-Sphere Water Interactions of Fe(II) and Co(II) Complexes of 12-Membered Macrocycles To Develop CEST MRI Probes. Water 23-28 mitochondrially encoded cytochrome c oxidase II Homo sapiens 56-62 31247845-1 2019 Several paramagnetic Co(II) and Fe(II) macrocyclic complexes were prepared with the goal of introducing a bound water ligand to produce paramagnetically shifted water 1H resonances and for paramagnetic chemical exchange saturation transfer (paraCEST) applications. Water 112-117 mitochondrially encoded cytochrome c oxidase II Homo sapiens 21-27 31247845-1 2019 Several paramagnetic Co(II) and Fe(II) macrocyclic complexes were prepared with the goal of introducing a bound water ligand to produce paramagnetically shifted water 1H resonances and for paramagnetic chemical exchange saturation transfer (paraCEST) applications. Water 161-166 mitochondrially encoded cytochrome c oxidase II Homo sapiens 21-27 31247845-8 2019 Variable-temperature 17O NMR spectra of Co(II) and Fe(II) NODA complexes were consistent with rapid exchange of the water ligand with bulk water. Water 116-121 mitochondrially encoded cytochrome c oxidase II Homo sapiens 40-46 31247845-8 2019 Variable-temperature 17O NMR spectra of Co(II) and Fe(II) NODA complexes were consistent with rapid exchange of the water ligand with bulk water. Water 139-144 mitochondrially encoded cytochrome c oxidase II Homo sapiens 40-46 31247845-9 2019 Notably, the Co(II) and Fe(II) complexes presented here produced substantial paramagnetic shifts of bulk water 1H resonances, independent of having an inner-sphere water. Water 105-110 mitochondrially encoded cytochrome c oxidase II Homo sapiens 13-19 31247845-9 2019 Notably, the Co(II) and Fe(II) complexes presented here produced substantial paramagnetic shifts of bulk water 1H resonances, independent of having an inner-sphere water. Water 164-169 mitochondrially encoded cytochrome c oxidase II Homo sapiens 13-19 30580142-4 2019 Capturing cobalt (Co(II)) from filtered river water doped with competing metals (Cu, As, Ag, Cd, Hg, Tl, and Pb) was most effective from pH 5-8 with binding affinity ranged from IDAA > DE4A > ED3A > Ac-Phos > SH on SAMMS. Water 46-51 mitochondrially encoded cytochrome c oxidase II Homo sapiens 18-24 30888790-0 2019 Mixed-Ligand-Architected 2D Co(II)-MOF Expressing a Novel Topology for an Efficient Photoanode for Water Oxidation Using Visible Light. Water 99-104 mitochondrially encoded cytochrome c oxidase II Homo sapiens 28-34 31458193-3 2018 However, two isostructural monomeric complexes are formed {[M(HCPCA)2(H2O)2], M = Co(II), (2) and Mn(II) (3)} when reactions were carried out in the absence of dmphen. Water 70-73 mitochondrially encoded cytochrome c oxidase II Homo sapiens 82-88 30398331-7 2018 Thus, the study demonstrates both facile O-O bond cleavage and formation in the stoichiometric reduction of O2 to H2O with 2 equiv of Co(II) and suggests a new pathway for selective reduction of O2 to water via Co(III)-O-O-Co(III) peroxo intermediates. Water 114-117 mitochondrially encoded cytochrome c oxidase II Homo sapiens 134-140 30398331-7 2018 Thus, the study demonstrates both facile O-O bond cleavage and formation in the stoichiometric reduction of O2 to H2O with 2 equiv of Co(II) and suggests a new pathway for selective reduction of O2 to water via Co(III)-O-O-Co(III) peroxo intermediates. Water 201-206 mitochondrially encoded cytochrome c oxidase II Homo sapiens 134-140 30668108-14 2019 Further reflecting the role of the ligand in tuning reactivity, the trimetallic trihydride cluster compounds, [M3(mu-H)3]3+ (M = FeII, CoII, ZnII), demonstrate substrate specificity for CO2 over various other unsaturated molecules and surprising stability toward water. Water 263-268 mitochondrially encoded cytochrome c oxidase II Homo sapiens 135-139 30881630-6 2019 Architectures that disassembled when CoII, ZnII and CdII templates were employed could be directly prepared from NiSO4 in water. Water 122-127 mitochondrially encoded cytochrome c oxidase II Homo sapiens 37-41 30295298-5 2018 No polymeric structures were obtained in the CoII and NiII complexes due to the higher affinity of these metals for water than that for the m-carboranylphosphinate and accordingly, these complexes generate supramolecular hydrophobic/hydrophilic structures. Water 116-121 mitochondrially encoded cytochrome c oxidase II Homo sapiens 45-49 30009517-5 2018 In the resting state, the catalyst returns to the original six-coordinate high-spin CoII state with a pentapyridyl and one water molecule coordinating to the metal center. Water 123-128 mitochondrially encoded cytochrome c oxidase II Homo sapiens 84-88 30226522-2 2018 Herein, two hydroxy-rich hydrazone-based COFs are synthesized in pure water and postsynthetically incorporated with CoII, exhibiting Lewis acid catalytic activity towards cyanosilylation of various aldehydes with size selectivity. Water 70-75 mitochondrially encoded cytochrome c oxidase II Homo sapiens 116-120 30152699-0 2018 Co(II)/Ag(I) Synergistically Catalyzed Monoinsertion Reaction of Isocyanide to Terminal Alkynes with H2O: Synthesis of Alkynamide Derivatives. Water 101-104 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-6 30152699-1 2018 A Co(II)/Ag(I) synergistically catalyzed three-component reaction of isocyanide with terminal alkyne and water to afford alkynamide derivatives is reported. Water 105-110 mitochondrially encoded cytochrome c oxidase II Homo sapiens 2-8 29697966-1 2018 In this work we present a systematic computational study of the structural and magnetic properties of a layered family of Co(II) hydroxichlorides, obeying to the general formula Co(OH)2- xCl x(H2O) y. Water 193-196 mitochondrially encoded cytochrome c oxidase II Homo sapiens 122-128 29653357-1 2018 The Co(II)/peroxymonosulfate (Co(II)/PMS) process, producing sulfate radicals (SO4 -), effectively removes organic pollutants in water, while producing a significant amount of bromate (BrO3-) in the presence of bromide (Br-). Water 129-134 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-28 29653357-1 2018 The Co(II)/peroxymonosulfate (Co(II)/PMS) process, producing sulfate radicals (SO4 -), effectively removes organic pollutants in water, while producing a significant amount of bromate (BrO3-) in the presence of bromide (Br-). Water 129-134 mitochondrially encoded cytochrome c oxidase II Homo sapiens 30-40 29799201-0 2018 Rational Design of Co(II) Dominant and Oxygen Vacancy Defective CuCo2O4@CQDs Hollow Spheres for Enhanced Overall Water Splitting and Supercapacitor Performance. Water 113-118 mitochondrially encoded cytochrome c oxidase II Homo sapiens 19-25 29697966-6 2018 Moreover, our results suggest that the presence of interlayer water stabilizes the material and at the same time strongly modifies the electronic environment of tetrahedral Co(II), leading to a further drop of the band gap. Water 62-67 mitochondrially encoded cytochrome c oxidase II Homo sapiens 173-179 29214722-3 2018 The best water oxidation activity is obtained with cobalt hydroxide carbonate templated t-CoII -CoIII with an overpotential as low as 240 mV to reach a current density of 10 mA cm-2 . Water 9-14 mitochondrially encoded cytochrome c oxidase II Homo sapiens 90-94 29451291-1 2018 In this work, we demonstrate the synthesis and application of a novel CoII-based metal-organic framework {[Co2(Dcpp)(Bpe)0.5 (H2O)(mu2-H2O)] (Bpe)0.5}n (CoII-MOF, H4Dcpp = 4,5-bis(4"-carboxylphenyl)-phthalic acid, Bpe = 1,2-bis(4-pyridyl)ethane) as an electrochemical sensor for glucose detection. Water 126-129 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-74 29412653-7 2018 Amide pendents deprotonate at high pH (>8), and the water ligands of the Co(II) complexes are not deprotonated at neutral pH. Water 55-60 mitochondrially encoded cytochrome c oxidase II Homo sapiens 76-82 29553723-2 2018 Upon heating/cooling, the water molecules which are coordinated to a pair of crystallographically symmetric Co(II) ions are removed/recovered discretely in two steps, giving [Co3(pimda)2(H2O)4] (2) and [Co3(pimda)2(H2O)3] (3), which is evidenced by the reversible single-crystal-to-single-crystal (SCSC) structural transformations. Water 26-31 mitochondrially encoded cytochrome c oxidase II Homo sapiens 108-114 29553723-2 2018 Upon heating/cooling, the water molecules which are coordinated to a pair of crystallographically symmetric Co(II) ions are removed/recovered discretely in two steps, giving [Co3(pimda)2(H2O)4] (2) and [Co3(pimda)2(H2O)3] (3), which is evidenced by the reversible single-crystal-to-single-crystal (SCSC) structural transformations. Water 187-190 mitochondrially encoded cytochrome c oxidase II Homo sapiens 108-114 29412653-0 2018 Inner-Sphere and Outer-Sphere Water Interactions in Co(II) paraCEST Agents. Water 30-35 mitochondrially encoded cytochrome c oxidase II Homo sapiens 52-57 29412653-2 2018 The first examples of Co(II) paraCEST agents with bound water ligands are presented here. Water 56-61 mitochondrially encoded cytochrome c oxidase II Homo sapiens 22-27 29381136-2 2018 The conserved mitochondrial-encoded COX1- and COX2-subunits are the heme- and copper-center containing core subunits that catalyze water formation. Water 131-136 mitochondrially encoded cytochrome c oxidase II Homo sapiens 46-50 29303495-3 2018 It consists of a mononuclear unit with the CoII ion on an inversion centre coordinated by two 2,6-diamino-7H-purin-1-ium cations, two 4,4"-oxydibenzoate anions (in a nonbridging kappaO-monodentate coordination mode, which is less common for the anion in its CoII complexes) and two water molecules, defining an octahedral environment around the metal atom. Water 282-287 mitochondrially encoded cytochrome c oxidase II Homo sapiens 43-47 28862848-0 2017 Enantioselective Aldol Reactions in Water by a Proline-Derived Cryptand and Fixation of CO2 by Its Exocyclic Co(II) Complex. Water 36-41 mitochondrially encoded cytochrome c oxidase II Homo sapiens 109-115 29052412-0 2017 Co(II)-Doped Cd-MOF as an Efficient Water Oxidation Catalyst: Doubly Interpenetrated Boron Nitride Network with the Encapsulation of Free Ligand Containing Pyridine Moieties. Water 36-41 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-6 28766939-5 2017 Here, we present magnetic resonance imaging (MRI) as an accessible and powerful technique to monitor bioreduction by treating the cobalt complex as an MRI contrast agent and monitoring the change in water signal induced by reduction from diamagnetic Co(III) to paramagnetic Co(II). Water 199-204 mitochondrially encoded cytochrome c oxidase II Homo sapiens 274-280 28573307-1 2017 We report a combined experimental characterization and theoretical modeling of the hexa-coordinated high-spin Co(ii) complex cis-[Co(hfac)2(H2O)2] (I). Water 140-143 mitochondrially encoded cytochrome c oxidase II Homo sapiens 113-115 28613850-0 2017 A Highly Selective and Robust Co(II)-Based Homogeneous Catalyst for Reduction of CO2 to CO in CH3CN/H2O Solution Driven by Visible Light. Water 100-103 mitochondrially encoded cytochrome c oxidase II Homo sapiens 30-35 28613850-3 2017 Herein, we report a Co(II)-based homogeneous catalyst, [Co(NTB)CH3CN](ClO4)2 (1, NTB = tris(benzimidazolyl-2-methyl)amine), which shows high selectivity and stability for the catalytic reduction of CO2 to CO in a water-containing system driven by visible light, with turnover number (TON) and turnover frequency (TOF) values of 1179 and 0.032 s-1, respectively, and selectivity to CO of 97%. Water 213-218 mitochondrially encoded cytochrome c oxidase II Homo sapiens 20-25 28534627-0 2017 Highly Stable and Regenerative Metal-Organic Framework Designed by Multiwalled Divider Installation Strategy for Detection of Co(II) Ions and Organic Aromatics in Water. Water 163-168 mitochondrially encoded cytochrome c oxidase II Homo sapiens 126-132 28529781-3 2017 The CoII atom is coordinated by two TMB anions and two water mol-ecules in the basal plane, while another water mol-ecule bridges the CoII atoms in the axial directions, forming polymeric chains running along [001]. Water 55-60 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-8 27301436-5 2016 X-ray analysis of and revealed that presents a dinuclear structure whereas is trinuclear; in both cases a six-coordinated Co(II) compound with water molecules bridging each of the two Co(II) centres has been observed. Water 143-148 mitochondrially encoded cytochrome c oxidase II Homo sapiens 122-128 28254043-0 2017 Adsorption of Co(II) from aqueous solutions by water treatment residuals. Water 47-52 mitochondrially encoded cytochrome c oxidase II Homo sapiens 14-20 28254043-1 2017 A study on the removal of Co(II) from aqueous solutions by water treatment residuals (WTR) was conducted in batch conditions. Water 59-64 mitochondrially encoded cytochrome c oxidase II Homo sapiens 26-32 27774535-1 2016 Partial reductive hydrolysis of a penta-CoII/III cluster [Co(H2O)2(CoIIIW9O34)(PW9O34)]12- (1) leads to the formation of [Co2{Co3(H2O)(Co(OH)2W7O26)(PW9O34)}2]22- (2). Water 61-64 mitochondrially encoded cytochrome c oxidase II Homo sapiens 40-44 27500422-3 2016 In both structures, the Co(II) centers adopt octahedral {CoN2O4} geometries filled by pairs of mutually trans terminal 3,5-dnb, py, and water ligands. Water 136-141 mitochondrially encoded cytochrome c oxidase II Homo sapiens 24-30 28225613-3 2017 To further investigate this issue and inspired by research in water oxidation, we calculate in the present study the dehydrogenation free energy of aqueous Co2+, which is the free energy change associated with the first step of the water oxidation reaction mechanism of recently investigated model Co(II)-aqua catalysts. Water 62-67 mitochondrially encoded cytochrome c oxidase II Homo sapiens 298-303 28225613-3 2017 To further investigate this issue and inspired by research in water oxidation, we calculate in the present study the dehydrogenation free energy of aqueous Co2+, which is the free energy change associated with the first step of the water oxidation reaction mechanism of recently investigated model Co(II)-aqua catalysts. Water 232-237 mitochondrially encoded cytochrome c oxidase II Homo sapiens 298-303 27433926-2 2016 The addition of 1 % H2 O significantly improved the performance of the Co(II) catalyst. Water 20-24 mitochondrially encoded cytochrome c oxidase II Homo sapiens 71-77 27301436-5 2016 X-ray analysis of and revealed that presents a dinuclear structure whereas is trinuclear; in both cases a six-coordinated Co(II) compound with water molecules bridging each of the two Co(II) centres has been observed. Water 143-148 mitochondrially encoded cytochrome c oxidase II Homo sapiens 184-190 27301436-6 2016 The magnetic properties of and show a weak antiferromagnetic behaviour, respectively, between the Co(II) centres mediated by two carboxylate ligands and a molecule of water. Water 167-172 mitochondrially encoded cytochrome c oxidase II Homo sapiens 98-104 26757444-0 2016 A Mononuclear Co(II) Coordination Complex Locked in a Confined Space and Acting as an Electrochemical Water-Oxidation Catalyst: A "Ship-in-a-Bottle" Approach. Water 102-107 mitochondrially encoded cytochrome c oxidase II Homo sapiens 14-19 26777227-2 2016 In this study, we describe the successful demonstration of the water- and temperature-triggered reversible structural transformation between cubane- and planar-type tetranuclear Co(II) cores sandwiched by polyoxometalates. Water 63-68 mitochondrially encoded cytochrome c oxidase II Homo sapiens 178-184 27167594-1 2016 Under H2 pressure, Co(II)(dmgBF2)2L2 (L = H2O, THF) generates a low concentration of an H donor. Water 42-45 mitochondrially encoded cytochrome c oxidase II Homo sapiens 19-36 26846498-8 2016 The Co(II) cations are bridged by BDC(2-) ligands and are octahedrally coordinated by three carboxylate O atoms from three BDC(2-) ligands, one water O atom and two pyridine N atoms. Water 144-149 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 25611163-4 2015 On the other hand, in linear trinuclear complex , in addition to the mu2-phenoxido and mu1,1-azido bridges with terminal octahedral Co(III) centres, the central Co(II) is bonded with two mutually trans-oxygen atoms of water molecules. Water 218-223 mitochondrially encoded cytochrome c oxidase II Homo sapiens 161-167 26467233-1 2015 A heterometallic phenylsilsesquioxane [(PhSiO1,5)22(CoO)3(NaO0.5)6] (EtOH)6 (H2O) 1 cage architecture of Co(II) ions in a triangular topology exhibits a slow dynamic behavior in its magnetization, induced by the freezing of the spins of individual molecules. Water 77-80 mitochondrially encoded cytochrome c oxidase II Homo sapiens 105-111 26870577-2 2016 The Co(II) atom is octa-hedrally coordinated by the O atom of a water mol-ecule, by one terminally bound carboxyl-ate O atom of an HMal(-) anion and by two O atoms of a chelating HMal(-) anion, as well as by two Cl(-) anions. Water 64-69 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 27293584-4 2015 Herein we describe the stepwise optimisation of reaction parameters (pH, reagent concentrations and reaction time) for the room temperature, water-based synthesis of several members of the CPO-27/MOF-74-M series of MOFs, including ones made from Mg(II), Ni(II), Co(II) and Zn(II) ions. Water 141-146 mitochondrially encoded cytochrome c oxidase II Homo sapiens 262-268 25700155-1 2015 The self-assembly between a water-soluble bis-bidentate ligand L(18w) and Co(II) salts in water affords three high-spin Co(II) products: a dinuclear meso-helicate [Co2(L(18w))3]X4; a tetrahedral cage [Co4(L(18w))6]X8; and a dodecanuclear truncated-tetrahedral cage [Co12(L(18w))18]X24 (X = BF4 or ClO4). Water 28-33 mitochondrially encoded cytochrome c oxidase II Homo sapiens 74-80 25700155-1 2015 The self-assembly between a water-soluble bis-bidentate ligand L(18w) and Co(II) salts in water affords three high-spin Co(II) products: a dinuclear meso-helicate [Co2(L(18w))3]X4; a tetrahedral cage [Co4(L(18w))6]X8; and a dodecanuclear truncated-tetrahedral cage [Co12(L(18w))18]X24 (X = BF4 or ClO4). Water 28-33 mitochondrially encoded cytochrome c oxidase II Homo sapiens 120-126 25700155-1 2015 The self-assembly between a water-soluble bis-bidentate ligand L(18w) and Co(II) salts in water affords three high-spin Co(II) products: a dinuclear meso-helicate [Co2(L(18w))3]X4; a tetrahedral cage [Co4(L(18w))6]X8; and a dodecanuclear truncated-tetrahedral cage [Co12(L(18w))18]X24 (X = BF4 or ClO4). Water 90-95 mitochondrially encoded cytochrome c oxidase II Homo sapiens 74-80 25700155-1 2015 The self-assembly between a water-soluble bis-bidentate ligand L(18w) and Co(II) salts in water affords three high-spin Co(II) products: a dinuclear meso-helicate [Co2(L(18w))3]X4; a tetrahedral cage [Co4(L(18w))6]X8; and a dodecanuclear truncated-tetrahedral cage [Co12(L(18w))18]X24 (X = BF4 or ClO4). Water 90-95 mitochondrially encoded cytochrome c oxidase II Homo sapiens 120-126 25494642-1 2015 We report the synthesis of a perylene derivative (perylene tetracarboxylic di(propyl imidazole), abbreviated as PDI) that is coordinated with Co(II) ions to form a coordination polymer [PDI-Co(Cl)2(H2O)2]n (abbreviated as PDI-Co). Water 198-201 mitochondrially encoded cytochrome c oxidase II Homo sapiens 142-148 25533319-2 2015 An initial Co(II) amine complex 1 is prone to aerial oxidation yielding a Co(III) imine complex 2 that is further converted into an amide complex 4 in presence of adventitious water. Water 176-181 mitochondrially encoded cytochrome c oxidase II Homo sapiens 11-16 25533319-4 2015 Both the Co(III) 4 and Co(II) 5 show electrocatalytic H2 generation in weakly acidic media as well as in water. Water 105-110 mitochondrially encoded cytochrome c oxidase II Homo sapiens 9-14 25459625-3 2015 The metal complexes were found to have The structural formula ML H2O and the metal ions Mn(II), Co(II), Ni(II)) and Zn(II) were found to form tetrahedral complexes with the ligand whereas Cu(II) formed a square planar one. Water 65-68 mitochondrially encoded cytochrome c oxidase II Homo sapiens 96-102 24664104-0 2014 A Co(II)-Ru(II) dyad relevant to light-driven water oxidation catalysis. Water 46-51 mitochondrially encoded cytochrome c oxidase II Homo sapiens 2-8 24960108-2 2014 Two n-propanol molecules and one water molecule coordinate to three Co(II) ions and four mu-phenoxo oxygen atoms from two [CoL(CH3CH2CH2OH)] units also coordinating to Co(II) ion. Water 33-38 mitochondrially encoded cytochrome c oxidase II Homo sapiens 68-74 24960108-2 2014 Two n-propanol molecules and one water molecule coordinate to three Co(II) ions and four mu-phenoxo oxygen atoms from two [CoL(CH3CH2CH2OH)] units also coordinating to Co(II) ion. Water 33-38 mitochondrially encoded cytochrome c oxidase II Homo sapiens 168-174 25248683-0 2014 Enhanced water-soluble derivative of PC407 as a novel potential COX-2 inhibitor injectable formulation. Water 9-14 mitochondrially encoded cytochrome c oxidase II Homo sapiens 64-69 25248683-4 2014 This derivative represents the profiles of prodrug and potential candidate of PC407 for the development of injectable COX-2 inhibitor due to extraordinary water solubility, low toxicity, and impressive analgesic activity. Water 155-160 mitochondrially encoded cytochrome c oxidase II Homo sapiens 118-123 25407218-0 2014 Water oxidation catalysis by Co(II) impurities in Co(III)4O4 cubanes. Water 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 29-35 25407218-1 2014 The observed water oxidation activity of the compound class Co4O4(OAc)4(Py-X)4 emanates from a Co(II) impurity. Water 13-18 mitochondrially encoded cytochrome c oxidase II Homo sapiens 95-101 25407218-3 2014 We present results from electron paramagnetic resonance spectroscopy, nuclear magnetic resonance line broadening analysis, and electrochemical titrations to establish the existence of the Co(II) impurity as the major source of water oxidation activity that has been reported for Co4O4 molecular cubanes. Water 227-232 mitochondrially encoded cytochrome c oxidase II Homo sapiens 188-194 25423999-7 2014 Interestingly, the nanofibers exhibit a reversible transformation of the coordination geometry of the Co(II) ions between octahedral and pseudotetrahedral with a concomitant color change between pink and blue, which involves the loss and reuptake of unusual weakly coordinated water molecules without destroying the structure. Water 277-282 mitochondrially encoded cytochrome c oxidase II Homo sapiens 102-108 25484680-1 2014 In the title complex, [Co(C15H6ClO4)2(H2O)4] 2H2O, the Co(II) ion is bound by two carboxylate O atoms of two 5-chloro-9,10-anthra-quinone-1-carboxyl-ate anions and four water O atoms in a trans conformation, forming an irregular octa-hedral coordination geometry. Water 169-174 mitochondrially encoded cytochrome c oxidase II Homo sapiens 55-61 24819564-1 2014 A homogeneous solution of Co(II) in acetate buffer at pH 7 is found to be an efficient water oxidation catalyst (WOC) showing significantly greater current density than Co(II) in phosphate buffer (Co-Pi) under identical conditions owing to the higher solubility of the former. Water 87-92 mitochondrially encoded cytochrome c oxidase II Homo sapiens 26-32 24797689-0 2014 An unusual water-bridged homospin Co(II) single-chain magnet. Water 11-16 mitochondrially encoded cytochrome c oxidase II Homo sapiens 34-40 24888451-1 2014 Reaction of Co(II) with the nitrogen-rich ligand N,N-bis(1H-tetrazole-5-yl)-amine (H2bta) leads to a mixed-valence, 3D, porous, metal-organic framework (MOF)-based, energetic material with the nitrogen content of 51.78%, [Co9(bta)10(Hbta)2(H2O)10]n (22 H2O)n (1). Water 240-243 mitochondrially encoded cytochrome c oxidase II Homo sapiens 12-18 24888451-1 2014 Reaction of Co(II) with the nitrogen-rich ligand N,N-bis(1H-tetrazole-5-yl)-amine (H2bta) leads to a mixed-valence, 3D, porous, metal-organic framework (MOF)-based, energetic material with the nitrogen content of 51.78%, [Co9(bta)10(Hbta)2(H2O)10]n (22 H2O)n (1). Water 253-256 mitochondrially encoded cytochrome c oxidase II Homo sapiens 12-18 24797689-1 2014 An unusual water-bridged homospin Co(II) coordination polymer has been successfully assembled, which exhibits slow relaxation of the magnetization at low temperature. Water 11-16 mitochondrially encoded cytochrome c oxidase II Homo sapiens 34-40 24425867-4 2014 These structures reveal that the oxicams bind to the active site of COX-2 using a binding pose not seen with other NSAIDs through two highly coordinated water molecules. Water 153-158 mitochondrially encoded cytochrome c oxidase II Homo sapiens 68-73 24562186-0 2014 Outer Co(II) ions in Co-ZIF-67 reversibly adsorb oxygen from both gas phase and liquid water. Water 87-92 mitochondrially encoded cytochrome c oxidase II Homo sapiens 6-12 24562186-1 2014 Outer Co(II) species in Co-ZIF-67 coordinate molecular oxygen both from the gas phase and liquid water, through an adsorption process (presumably yielding in both cases surface superoxo species), respectively weak and reversible (gas phase), and strong and irreversible (liquid); in the latter case desorption is however brought about by illumination with solar light comprising the UV component. Water 97-102 mitochondrially encoded cytochrome c oxidase II Homo sapiens 6-12 24635104-2 2014 The ligand readily accommodates Co(II) bearing two axial chlorides, and the resulting complex is reasonably soluble in water. Water 119-124 mitochondrially encoded cytochrome c oxidase II Homo sapiens 32-38 24578654-4 2014 In the title complex, the Co(II) ion is six-coordinated by two pyridine N atoms and two carboxyl O atoms from two 2-picolinic acid anions, and two O atoms from two H2O molecules, and forming a slightly distorted octahedral geometry. Water 164-167 mitochondrially encoded cytochrome c oxidase II Homo sapiens 26-32 31986579-1 2014 By using a rigid multicarboxylate ligand, 4,5-di(4"-carboxylphenyl)phthalic acid (H4 L), two CoII complexes formulated as [Co4 L2 (4,4"-bpy)(H2 O)6 ] 3.5 H2 O (4,4"-bpy=4,4"-bipyridine) (1) and [Co2 L(azene)(H2 O)3 ] DMF (azene=(E)-1,2-di(pyridin-4-yl)diazene, DMF=dimethylformamide) (2) have been synthesized and structurally characterized by single-crystal X-ray diffraction. Water 141-145 mitochondrially encoded cytochrome c oxidase II Homo sapiens 93-97 31986579-1 2014 By using a rigid multicarboxylate ligand, 4,5-di(4"-carboxylphenyl)phthalic acid (H4 L), two CoII complexes formulated as [Co4 L2 (4,4"-bpy)(H2 O)6 ] 3.5 H2 O (4,4"-bpy=4,4"-bipyridine) (1) and [Co2 L(azene)(H2 O)3 ] DMF (azene=(E)-1,2-di(pyridin-4-yl)diazene, DMF=dimethylformamide) (2) have been synthesized and structurally characterized by single-crystal X-ray diffraction. Water 195-214 mitochondrially encoded cytochrome c oxidase II Homo sapiens 93-97 24402189-1 2014 Efficient photocatalytic hydrogen evolution is obtained from 1 M phosphate buffer at pH 7 in the presence of a Ru(bpy)3(2+) sensitizer, an ascorbic acid sacrificial donor, and a water-soluble Co(II) porphyrin catalyst. Water 178-183 mitochondrially encoded cytochrome c oxidase II Homo sapiens 192-198 25421594-0 2014 Water-extracted Ampelopsis brevipedunculata downregulates IL-1beta,CCL5, and COX-2 expression via inhibition of PKC-mediated JNK/NF-kappaB signaling pathways in human monocytic cells. Water 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 77-82 24558308-0 2014 Korean Red Ginseng water extract inhibits COX-2 expression by suppressing p38 in acrolein-treated human endothelial cells. Water 19-24 mitochondrially encoded cytochrome c oxidase II Homo sapiens 42-47 25421594-8 2014 Collectively, our data showed that water-extracted A.bre inhibited the protein kinase C-JNKs/NF-kappaB signaling pathways, resulting in the suppression of IL-1beta, CCL-5, and COX-2 expression. Water 35-40 mitochondrially encoded cytochrome c oxidase II Homo sapiens 176-181 24231744-0 2014 Highly stable water dispersible calix[4]pyrrole octa-hydrazide protected gold nanoparticles as colorimetric and fluorometric chemosensors for selective signaling of Co(II) ions. Water 14-19 mitochondrially encoded cytochrome c oxidase II Homo sapiens 165-171 23939252-0 2013 Voltammetric and spectroscopic characterization of early intermediates in the Co(II)-polypyridyl-catalyzed reduction of water. Water 120-125 mitochondrially encoded cytochrome c oxidase II Homo sapiens 78-84 24279370-1 2013 We introduce the novel Co4O4 complex [Co(II)4(hmp)4(mu-OAc)2(mu2-OAc)2(H2O)2] (1) (hmp = 2-(hydroxymethyl)pyridine) as the first Co(II)-based cubane water oxidation catalyst. Water 149-154 mitochondrially encoded cytochrome c oxidase II Homo sapiens 38-44 24279370-4 2013 The Co(II) core combines robustness and stability with flexibility through a new type of water-oxidation mechanism via mobile ligands. Water 89-94 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 23842534-0 2013 Two novel Co(II) coordination polymers based on 1,4-bis(3-pyridylaminomethyl)benzene as electrocatalysts for oxygen evolution from water. Water 131-136 mitochondrially encoded cytochrome c oxidase II Homo sapiens 10-16 23764826-7 2013 The analysis of existing crystallographic data for the reactivation conformation of MetH enzyme (1K7Y (@3.0 A); 1K98 (@3.8 A) and 3IVA (@2.7 A)) indicates that the Y1139 residue and the beta-axial H2O ligand in the MetH-bound Co(II)Cbx complex are equidistant from the Co(II) ion (Y1139Co(II)=3.97 A; H2OCo(II)=3.96 A). Water 197-200 mitochondrially encoded cytochrome c oxidase II Homo sapiens 269-275 23806103-11 2013 Films containing Co(II) reached current densities of 6.0 mA/cm(2) at +1.8 V vs NHE in H2O. Water 86-89 mitochondrially encoded cytochrome c oxidase II Homo sapiens 17-23 23637886-4 2013 And H(H2O)m significantly prevented UV-induced MMP-1, COX-2, IL-6 and IL-1beta mRNA expressions in human skin in vivo. Water 6-9 mitochondrially encoded cytochrome c oxidase II Homo sapiens 54-59 24109269-1 2013 In the title salt, [Co(C7H9NO)2(H2O)2]Cl2, the Co(II) cation, located on an inversion center, is N,O-chelated by two hy-droxy-ethyl-pyridine ligands and coordinated by two water mol-ecules in a distorted O4N2 octa-hedral geometry. Water 172-177 mitochondrially encoded cytochrome c oxidase II Homo sapiens 47-53 23692429-1 2013 Electrocatalytic water oxidation occurs at fluoride-doped tin oxide (FTO) electrodes that have been surface-modified by addition of Co(II). Water 17-22 mitochondrially encoded cytochrome c oxidase II Homo sapiens 132-138 23692429-3 2013 On the basis of cyclic voltammetry measurements, surface-bound Co(II) undergoes a pH-dependent 1e(-)/1H(+) oxidation to Co(III), which is followed by pH-dependent catalytic water oxidation. Water 173-178 mitochondrially encoded cytochrome c oxidase II Homo sapiens 63-69 23462930-6 2013 The crystal structures of all the studied hetero-trinuclear species highlight that such systems are formed thanks to the synergy between the different stereochemical requirement of the transition metal (Cu(II) or Co(II)) and the different donor atoms set of the ligands which preorganize the maltol units for the binding of the hard M(III) metal, otherwise difficult to bind in water, through L/M(II)/M(III) self-assembling. Water 378-383 mitochondrially encoded cytochrome c oxidase II Homo sapiens 213-219 23637886-5 2013 We found that H(H2O)m prevented UV-induced ROS generation and inhibited UV-induced MMP-1, COX-2 and IL-6 expressions, and UV-induced JNK and c-Jun phosphorylation in HaCaT cells. Water 16-19 mitochondrially encoded cytochrome c oxidase II Homo sapiens 90-95 22998407-5 2012 Water binds to [Co(II)MST](-) to form the five-coordinate [Co(II)MST(OH(2))](-) complex that was used to prepare the Co(II)/Ca(II) complex [Co(II)MST(mu-OH(2))Ca(II) 15-crown-5(OH(2))](+) ([Co(II)(mu-OH(2))Ca(II)OH(2)](+)). Water 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 59-65 23557586-1 2013 The reaction of the multisite coordination ligand (LH4) with CoX2 nH2O in the presence of tetrabutylammonium hydroxide affords a series of homometallic dinuclear mixed-valence complexes, [Co(III)Co(II)(LH2)2(X)(H2O)](H2O)m (1, X = Cl and m = 4; 2, X = Br and m = 4; 3, X = NO3 and m = 3). Water 211-215 mitochondrially encoded cytochrome c oxidase II Homo sapiens 61-65 23557586-1 2013 The reaction of the multisite coordination ligand (LH4) with CoX2 nH2O in the presence of tetrabutylammonium hydroxide affords a series of homometallic dinuclear mixed-valence complexes, [Co(III)Co(II)(LH2)2(X)(H2O)](H2O)m (1, X = Cl and m = 4; 2, X = Br and m = 4; 3, X = NO3 and m = 3). Water 67-70 mitochondrially encoded cytochrome c oxidase II Homo sapiens 61-65 23517550-3 2013 Recent theoretical calculations raised a new proposal that the Co(salen)(H2O)(SbF6) complex contains appreciable contribution from a Co(II)(salen( +)) electronic structure (Kochem, A.; Kanso, H.; Baptiste, B.; Arora, H.; Philouze, C.; Jarjayes, O.; Vezin, H.; Luneau, D.; Orio, M.; Thomas, F. Inorg. Water 73-77 mitochondrially encoded cytochrome c oxidase II Homo sapiens 133-139 23344965-1 2013 Subtle differences in metal-ligand bond lengths between a series of [M(4)L(6)](4-) tetrahedral cages, where M = Fe(II), Co(II), or Ni(II), were observed to result in substantial differences in affinity for hydrophobic guests in water. Water 228-233 mitochondrially encoded cytochrome c oxidase II Homo sapiens 120-126 22998407-5 2012 Water binds to [Co(II)MST](-) to form the five-coordinate [Co(II)MST(OH(2))](-) complex that was used to prepare the Co(II)/Ca(II) complex [Co(II)MST(mu-OH(2))Ca(II) 15-crown-5(OH(2))](+) ([Co(II)(mu-OH(2))Ca(II)OH(2)](+)). Water 153-159 mitochondrially encoded cytochrome c oxidase II Homo sapiens 59-65 22998407-5 2012 Water binds to [Co(II)MST](-) to form the five-coordinate [Co(II)MST(OH(2))](-) complex that was used to prepare the Co(II)/Ca(II) complex [Co(II)MST(mu-OH(2))Ca(II) 15-crown-5(OH(2))](+) ([Co(II)(mu-OH(2))Ca(II)OH(2)](+)). Water 153-159 mitochondrially encoded cytochrome c oxidase II Homo sapiens 59-65 23634005-1 2013 In the title compound, [Co(C7H4ClO2)2(C5H5N)2(H2O)], the Co(II) atom is six-coordinated by three O atoms from a bidentate and a monodentate 4-chloro-benzoate ligand, two N atoms from two pyridine ligands and a water O atom, giving a distorted octa-hedral geometry. Water 210-215 mitochondrially encoded cytochrome c oxidase II Homo sapiens 57-63 22998407-5 2012 Water binds to [Co(II)MST](-) to form the five-coordinate [Co(II)MST(OH(2))](-) complex that was used to prepare the Co(II)/Ca(II) complex [Co(II)MST(mu-OH(2))Ca(II) 15-crown-5(OH(2))](+) ([Co(II)(mu-OH(2))Ca(II)OH(2)](+)). Water 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 59-65 22998407-5 2012 Water binds to [Co(II)MST](-) to form the five-coordinate [Co(II)MST(OH(2))](-) complex that was used to prepare the Co(II)/Ca(II) complex [Co(II)MST(mu-OH(2))Ca(II) 15-crown-5(OH(2))](+) ([Co(II)(mu-OH(2))Ca(II)OH(2)](+)). Water 69-75 mitochondrially encoded cytochrome c oxidase II Homo sapiens 59-65 22998407-5 2012 Water binds to [Co(II)MST](-) to form the five-coordinate [Co(II)MST(OH(2))](-) complex that was used to prepare the Co(II)/Ca(II) complex [Co(II)MST(mu-OH(2))Ca(II) 15-crown-5(OH(2))](+) ([Co(II)(mu-OH(2))Ca(II)OH(2)](+)). Water 69-75 mitochondrially encoded cytochrome c oxidase II Homo sapiens 59-65 22887038-1 2012 Crystal clear: An end-on (EO) azide-bridged Co(II) layer (see scheme; 1) with coordinated water molecules, long spacer p-XBP4 ligands, and unbound azide anions was evacuated to generate a dehydrated sample of 2. Water 91-96 mitochondrially encoded cytochrome c oxidase II Homo sapiens 44-50 22354161-2 2012 Single crystal X-ray diffraction studies revealed that the Co(II) complex, {[Co(H(2)L)(H(2)O)(2)](NO(3))(2) 3H(2)O}(n) has a slightly distorted octahedral geometry around the central Co(II) ion; the ligand is coordinated through the ONO donor atoms to one Co(II) metal center and bridged through the pyridine nitrogen atom to another similar Co(II) center so as to form a one-dimensional polymeric unit. Water 87-93 mitochondrially encoded cytochrome c oxidase II Homo sapiens 183-189 22913479-1 2012 A novel, highly efficient, and stable water oxidation catalyst was prepared by a pH-controlled adsorption of Co(II) on ~10 nm diameter silica nanoparticles. Water 38-43 mitochondrially encoded cytochrome c oxidase II Homo sapiens 109-115 22354161-2 2012 Single crystal X-ray diffraction studies revealed that the Co(II) complex, {[Co(H(2)L)(H(2)O)(2)](NO(3))(2) 3H(2)O}(n) has a slightly distorted octahedral geometry around the central Co(II) ion; the ligand is coordinated through the ONO donor atoms to one Co(II) metal center and bridged through the pyridine nitrogen atom to another similar Co(II) center so as to form a one-dimensional polymeric unit. Water 87-93 mitochondrially encoded cytochrome c oxidase II Homo sapiens 59-65 22354161-2 2012 Single crystal X-ray diffraction studies revealed that the Co(II) complex, {[Co(H(2)L)(H(2)O)(2)](NO(3))(2) 3H(2)O}(n) has a slightly distorted octahedral geometry around the central Co(II) ion; the ligand is coordinated through the ONO donor atoms to one Co(II) metal center and bridged through the pyridine nitrogen atom to another similar Co(II) center so as to form a one-dimensional polymeric unit. Water 87-93 mitochondrially encoded cytochrome c oxidase II Homo sapiens 183-189 22354161-2 2012 Single crystal X-ray diffraction studies revealed that the Co(II) complex, {[Co(H(2)L)(H(2)O)(2)](NO(3))(2) 3H(2)O}(n) has a slightly distorted octahedral geometry around the central Co(II) ion; the ligand is coordinated through the ONO donor atoms to one Co(II) metal center and bridged through the pyridine nitrogen atom to another similar Co(II) center so as to form a one-dimensional polymeric unit. Water 87-93 mitochondrially encoded cytochrome c oxidase II Homo sapiens 183-189 22346896-2 2012 The coordination geometry of the Co(II) ion is a distorted octa-hedron with two O atoms from two coordinated water mol-ecules occupying cis positions in the equatorial plane and four O atoms from two hydrogen tartrate ions occupying the remaining positions. Water 109-114 mitochondrially encoded cytochrome c oxidase II Homo sapiens 33-39 22240735-1 2012 Examination of the aqueous electrochemistry of a Co(II) complex bearing a pentadentate ligand suggests that the catalytic current corresponding to water oxidation is molecular in origin, and does not emanate exclusively from Co-oxide phases formed in situ. Water 147-152 mitochondrially encoded cytochrome c oxidase II Homo sapiens 49-55 22346827-2 2012 The Co(II) ion is six-coordinated in a distorted octa-hedral environment, binding to two water O atoms, to the ether O atom of the bicyclo-heptane unit, to two carboxyl-ate O atoms from two different carboxyl-ate groups of the same anion and to one carboxyl-ate O atom from a symmetry-related anion. Water 89-94 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 21754320-3 2011 The Co(II) atom is in an almost octa-hedral environment formed by four carboxyl-ate O atoms from two malonate ligands and two water O atoms. Water 126-131 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 22259365-1 2012 In the title compound, [Co(C(5)H(4)NO(3))(2)(H(2)O)(2)] 2H(2)O, the coordination polyhedron around the six-coordinate Co(II) ion is formed by two equatorial 5-methyl-isoxazole-3-carboxyl-ate ligands in an N,O(3)-bidentate fashion through the isoxazole N atom and a carboxyl-ate O atom, and by two axial water ligands. Water 303-308 mitochondrially encoded cytochrome c oxidase II Homo sapiens 118-124 22199511-2 2011 The Co(II) atom is located on an inversion centre and displays a distorted octa-hedral coordination geometry defined by four O atoms of two 3-aza-niumyl-1-hy-droxy-propyl-idene-1,1-bis-phospho-nato ligands in the equatorial plane and two water mol-ecules located in axial positions. Water 238-243 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 22199572-1 2011 In the title compound, [CoNa(2)(C(7)H(3)NO(4))(2)(H(2)O)(2)](n), the Co(II) atom is coordinated by two pyridine N atoms and four carboxyl-ate O atoms from two doubly deprotonated pyridine-2,6-dicarboxyl-ate ligands in a distorted octa-hedral geometry. Water 50-56 mitochondrially encoded cytochrome c oxidase II Homo sapiens 69-75 21889841-1 2011 New nano hybrid material (ZrO(2)/B(2)O(3)) was synthesized and applied as a sorbent for the separation and/or preconcentration of Co(II), Cu(II) and Cd(II) in water and tea leaves prior to their determination by flame atomic absorption spectrometry. Water 159-164 mitochondrially encoded cytochrome c oxidase II Homo sapiens 130-136 22090887-2 2011 In the mol-ecule, the Co(II) atom is six-coordinated in a distorted octa-hedral environment, binding to the bridging O atom of the bicyclo-heptane unit, to two O atoms from monodentate carboxyl-ate groups and to three water O atoms. Water 218-223 mitochondrially encoded cytochrome c oxidase II Homo sapiens 22-28 23232244-2 2012 The ATPS-MSFA method was applied for the determination of cobalt, based on the reaction between Co(II) and KSCN, which produces a metallic complex that spontaneously partitions to the top phase of the ATPS composed of poly(ethylene oxide), ammonium sulfate and water. Water 261-266 mitochondrially encoded cytochrome c oxidase II Homo sapiens 96-111 22219767-1 2011 The Co(II) atom in the title salt, [Co(H(2)O)(6)](C(13)H(10)NO(3))(2) 2H(2)O, lies on a center of inversion in an octa-hedron of water mol-ecules. Water 39-45 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 22219767-1 2011 The Co(II) atom in the title salt, [Co(H(2)O)(6)](C(13)H(10)NO(3))(2) 2H(2)O, lies on a center of inversion in an octa-hedron of water mol-ecules. Water 129-134 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 21359324-1 2011 The pH-dependent electrochemical behavior for a Co(II) complex, [Co(Py5)(OH(2))](ClO(4))(2) (1; Py5 = 2,6-(bis(bis-2-pyridyl)methoxymethane)pyridine), indicates consecutive (proton-coupled) oxidation steps furnish a Co(IV) species that catalyzes the oxidation of water in basic media. Water 263-268 mitochondrially encoded cytochrome c oxidase II Homo sapiens 48-54 21416515-3 2011 Here we report the exchange rates of water ligated to Co(II) atoms in two polyoxotungstate sandwich molecules using the (17)O-NMR-based Swift-Connick method. Water 37-42 mitochondrially encoded cytochrome c oxidase II Homo sapiens 54-60 21522293-1 2011 In the title diaqua-cobalt complex, [Co(C(8)H(11)NO(5)PS)(2)(H(2)O)(2)], the Co(II) atom is surrounded by six O atoms belonging to the phosphoryl and sulfonyl groups of two deprotonated chelate ligands and two additional O atoms from water mol-ecules which are in cis positions with respect to one another. Water 61-66 mitochondrially encoded cytochrome c oxidase II Homo sapiens 77-83 21247694-11 2011 This promising result can provide a basis for applying the studied materials to the treatment of water effluents containing Co(II) chelated by EDTA by a simple one-step adsorption process. Water 97-102 mitochondrially encoded cytochrome c oxidase II Homo sapiens 124-130 21522869-1 2011 In the title complex, [Co(NCS)(2)(C(13)H(19)N(3)O)(H(2)O)], the Co(II) ion is six-coordinated by the N,N",N""-tridentate Schiff base, the N atoms of two thio-cyanate ligands and one water mol-ecule in a distorted octa-hedral geometry. Water 182-187 mitochondrially encoded cytochrome c oxidase II Homo sapiens 64-70 21522824-1 2011 In the title coordination polymer, [Co(C(14)H(16)O(6))(H(2)O)(2)](n), the Co(II) ion, situated on a twofold rotation axis, is coordinated by four O atoms from two 4,4"-[1,4-phenyl-enebis(-oxy)]dibutano-ate (L) ligands and two water mol-ecules in a highly distorted octa-hedral geometry. Water 226-231 mitochondrially encoded cytochrome c oxidase II Homo sapiens 74-80 21578138-1 2009 In the salt, (NH(4))(2)[Co(CH(4)O(6)P(2))(2)(H(2)O)(2)], the methyl-ene-diphospho-nate acts as a bidentate ligand and the Co(II) ion (site symmetry ) assumes an octa-hedral CoO(6) coordination geometry. Water 45-51 mitochondrially encoded cytochrome c oxidase II Homo sapiens 122-128 20976340-1 2010 Two new azido-Co(II) complexes with pyrazine carboxylato ligands, [Co(N(3))(L) H(2)O](n) (L = pyrazine-2-carboxylato) (1) and [CoNa(N(3))(2)(L)](n) (2), have been obtained by carefully tuning the Co(II):N(3)(-) ratio. Water 79-84 mitochondrially encoded cytochrome c oxidase II Homo sapiens 14-20 20976340-1 2010 Two new azido-Co(II) complexes with pyrazine carboxylato ligands, [Co(N(3))(L) H(2)O](n) (L = pyrazine-2-carboxylato) (1) and [CoNa(N(3))(2)(L)](n) (2), have been obtained by carefully tuning the Co(II):N(3)(-) ratio. Water 79-84 mitochondrially encoded cytochrome c oxidase II Homo sapiens 14-19 20433197-3 2010 As the deposition voltage is increased into the region where water oxidation prevails, the population of Co(IV) rises and the population of Co(II) decreases. Water 61-66 mitochondrially encoded cytochrome c oxidase II Homo sapiens 140-146 20396815-3 2010 In the N6 octahedral 4 : 1-type complex [Co(II)(L10)4](ClO4)2 H2O (25) both axially coordinating N1 unidentate and equatorially bound N2,N(pyr) bidentate ligands L10 are observed. Water 62-65 mitochondrially encoded cytochrome c oxidase II Homo sapiens 41-47 19632777-0 2009 Removal of Co(II) and Ni(II) ions from contaminated water using silica gel functionalized with EDTA and/or DTPA as chelating agents. Water 52-57 mitochondrially encoded cytochrome c oxidase II Homo sapiens 11-17 19632777-1 2009 In this study, the removal of Co(II) and Ni(II) ions from contaminated water was investigated using silica gel materials functionalized with both ethylenediaminetetraacetic acid (EDTA) and diethylenetriaminepentaacetic acid (DTPA). Water 71-76 mitochondrially encoded cytochrome c oxidase II Homo sapiens 30-36 20023872-4 2009 The absence of acetate in reaction mixtures containing Co(II) and Mn(II) led to mononuclear complexes, with water ligands completing the coordination spheres of the metal ions, even in the presence of large excess of the metal ions. Water 108-113 mitochondrially encoded cytochrome c oxidase II Homo sapiens 55-61 19846791-6 2009 The structure supports earlier suggestions that the enzyme acts to lower the reduction potential of the Co(II)/Co(I) couple by elongating the bond between the cobalt and its upper axial water ligand, effectively making the cobalt 4-coordinate, and illuminates the role of Tyr-1139 in the stabilization of this 4-coordinate state. Water 186-191 mitochondrially encoded cytochrome c oxidase II Homo sapiens 104-110 19658385-7 2009 The lattices in 1-3 reveal the presence of mononuclear Co(II) units bound exclusively to quinate (1 and 2) or quinate and water ligands (3), thus projecting the unique chemical reactivity in each investigated system and suggesting that 3 is an intermediate in the synthetic pathway leading to 1 and 2. Water 122-127 mitochondrially encoded cytochrome c oxidase II Homo sapiens 55-61 19406573-2 2009 The resin was used for selective separation, preconcentration and determination of Cu(II), Ni(II), Co(II), Cd(II), Pb(II), Mn(II) and Fe(III) ions in water samples by flame atomic absorption spectrometry. Water 150-155 mitochondrially encoded cytochrome c oxidase II Homo sapiens 99-104 19190378-3 2009 In (I), two independent Co(II) ions are six-coordinated through N(3)O(3) donor sets in slightly distorted octahedral geometries provided by two carboxylate and three pyridine ligands, and one water molecule. Water 192-197 mitochondrially encoded cytochrome c oxidase II Homo sapiens 24-30 19652294-2 2009 The Co(II) ions have local 4/m symmetry, with the equatorial water molecules in the mirror plane, while the V and apical O atom of the vanadyl group are located on the fourfold rotation axis and the P atoms reside on 4 sites. Water 61-66 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 21583812-2 2009 The Co(II) atom is located on an inversion center and is coordinated by six O atoms from two water mol-ecules and four mu(2)-carboxyl-ate groups of 4-fluoro-benzoate anions, forming a distorted CoO(6) octa-hedron, with Co-O bond lengths in the range 2.071 (2)-2.130 (2) A. Water 93-98 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 18482860-4 2008 The Co(II) cations present a slightly distorted CoN2O4 octahedral environment, with equatorially coordinated water molecules and axially pyridine N-bound ethylisonicotinate ligands. Water 109-114 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 21581161-1 2008 In the title complex, [Co(C(5)H(5)NO(4)P)(2)(H(2)O)(2)], the Co(II) ion, which lies on a crystallographic inversion center, is coordin-ated by four O atoms from two bidentate 2-phospho-nato-pyridine N-oxide ligands and two O atoms from two water ligands in a slightly distorted octa-hedral environment. Water 45-50 mitochondrially encoded cytochrome c oxidase II Homo sapiens 61-67 18975935-3 2008 Ni[(C(6)H(5)PO(3))(H(2)O)] crystallizes in the orthorhombic space group Pmn2(1) and is isostructural with the Mn(II), Fe(II), and Co(II) analogues. Water 19-25 mitochondrially encoded cytochrome c oxidase II Homo sapiens 130-136 19057066-1 2008 The title compound, [Co(C(18)H(23)N(10))](BF(4))(2) x H(2)O, is the result of complexing a Co cation (initially in a Co(II) state) with tris[2-(1H-imidazol-2-ylmethyleneamino)ethyl]amine (L), obtained by a condensation process involving imidazole-2-carbaldehyde and tris(2-aminoethyl)amine. Water 54-59 mitochondrially encoded cytochrome c oxidase II Homo sapiens 117-123 21581161-1 2008 In the title complex, [Co(C(5)H(5)NO(4)P)(2)(H(2)O)(2)], the Co(II) ion, which lies on a crystallographic inversion center, is coordin-ated by four O atoms from two bidentate 2-phospho-nato-pyridine N-oxide ligands and two O atoms from two water ligands in a slightly distorted octa-hedral environment. Water 240-245 mitochondrially encoded cytochrome c oxidase II Homo sapiens 61-67 18386923-3 2008 X-ray diffraction studies on the crystalline complex salt of formula [CoII(1)...H2O]Cl(PF6)(4).2MeCN have shown that a water molecule is included in the cavity and the water oxygen atom receives six H-bonds from the C-H fragments of the three imidazolium subunits and of the three proximate pyridine rings, according to a slightly distorted trigonal prismatic geometry. Water 119-124 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-74 21200991-1 2008 In the title complex, [Co(C(7)H(4)BrO(2))(2)(H(2)O)(2)], the Co(II) ion, which lies on a crystallographic inversion center, is coordin-ated by four O atoms from two bidentate 4-bromo-2-formyl-phenolate ligands and two O atoms from two water ligands in a slightly distorted octa-hedral environment. Water 45-51 mitochondrially encoded cytochrome c oxidase II Homo sapiens 61-67 21200991-1 2008 In the title complex, [Co(C(7)H(4)BrO(2))(2)(H(2)O)(2)], the Co(II) ion, which lies on a crystallographic inversion center, is coordin-ated by four O atoms from two bidentate 4-bromo-2-formyl-phenolate ligands and two O atoms from two water ligands in a slightly distorted octa-hedral environment. Water 235-240 mitochondrially encoded cytochrome c oxidase II Homo sapiens 61-67 18642438-0 2008 Retraction notice to "Determination of Co(II) in water and soil samples using spectrophotometry coupled with preconcentration on 4-amino methyl pyridine anchored silica gel column" [J. Water 49-54 mitochondrially encoded cytochrome c oxidase II Homo sapiens 39-45 18700754-4 2008 The computed values of the exchange coupling between the Co(II) ions across anti-syn carboxylate (1) and syn-syn carboxylate/water (2) bridges are J = -0.060 (1) and -1.90 (2) cm(-1) (with the Hamiltonian being defined as H = -Jsigma(i,j)S(i) x S(j)). Water 125-130 mitochondrially encoded cytochrome c oxidase II Homo sapiens 57-63 18781025-10 2008 The method was applied to the determination of Co(II) in water, biological and standard samples. Water 57-62 mitochondrially encoded cytochrome c oxidase II Homo sapiens 47-53 18386923-3 2008 X-ray diffraction studies on the crystalline complex salt of formula [CoII(1)...H2O]Cl(PF6)(4).2MeCN have shown that a water molecule is included in the cavity and the water oxygen atom receives six H-bonds from the C-H fragments of the three imidazolium subunits and of the three proximate pyridine rings, according to a slightly distorted trigonal prismatic geometry. Water 168-173 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-74 18520053-3 2008 We previously reported that intact fecal water samples from human volunteers significantly decreased prostaglandin production and COX-2 protein expression in colonic cells. Water 41-46 mitochondrially encoded cytochrome c oxidase II Homo sapiens 130-135 21202222-1 2008 In the mol-ecule of the title compound, [Co(C(6)H(4)NO(2))(2)(H(2)O)(2)], the coordination environment around the Co(II) atom is distorted octahedral; two N and two O atoms of the pyridine-2-carboxylate ligands lie in the equatorial plane and the two water O atoms in the axial positions. Water 62-67 mitochondrially encoded cytochrome c oxidase II Homo sapiens 114-120 17388586-1 2007 A new carboxylato-bridged CoII network of formula {Co((kappa1-kappa1)-(kappa1-mu2)-mu4-TDC)(mu2-H2O)0.5(H2O)}n (H2TDC=2,5-thiophenedicarboxylic acid) has been hydrothermally synthesized and characterized by single-crystal X-ray diffraction, thermogravimetric analysis, and IR and UV-visible spectroscopies. Water 96-99 mitochondrially encoded cytochrome c oxidase II Homo sapiens 26-30 17574332-0 2008 Wet oxidative method for removal of 2,4,6-trichlorophenol in water using Fe(III), Co(II), Ni(II) supported MCM41 catalysts. Water 61-66 mitochondrially encoded cytochrome c oxidase II Homo sapiens 82-88 17574332-2 2008 In the present work, Fe(III), Co(II) and Ni(II) incorporated MCM41 mesoporous solids were used as catalysts for oxidation of 2,4,6-trichlorophenol in water with or without the oxidant, H(2)O(2). Water 150-155 mitochondrially encoded cytochrome c oxidase II Homo sapiens 30-36 17574332-6 2008 The conversion achieved with Fe(III), Co(II) and Ni(II) incorporated MCM41 in 5h is respectively 59.4, 50.0 and 65.6% with 2,4,6-TCP:H(2)O(2) molar ratio of 1:1, and 60.2, 60.9 and 68.8% in absence of H(2)O(2). Water 133-138 mitochondrially encoded cytochrome c oxidase II Homo sapiens 38-44 18057610-1 2007 The title compound, [Co(C7H6NO2)2(H2O)4] x 4 H2O, contains a Co(II) ion lying on a crystallographic inversion centre. Water 34-37 mitochondrially encoded cytochrome c oxidase II Homo sapiens 61-67 18057610-2 2007 The Co(II) ion is octahedrally coordinated by two 6-methylpyridine-3-carboxylate ligands in axial positions [Co-O = 2.0621 (9) A] and by four water molecules in the equatorial plane [Co-O = 2.1169 (9) and 2.1223 (11) A]. Water 142-147 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 17222507-0 2007 Determination of Co(II) in water and soil samples using spectrophotometry coupled with preconcentration on 4-amino methyl pyridine anchored silica gel column. Water 27-32 mitochondrially encoded cytochrome c oxidase II Homo sapiens 17-23 17222507-7 2007 The present method was successfully applied for the determination of Co(II) in various water and soil samples. Water 87-92 mitochondrially encoded cytochrome c oxidase II Homo sapiens 69-75 17388586-1 2007 A new carboxylato-bridged CoII network of formula {Co((kappa1-kappa1)-(kappa1-mu2)-mu4-TDC)(mu2-H2O)0.5(H2O)}n (H2TDC=2,5-thiophenedicarboxylic acid) has been hydrothermally synthesized and characterized by single-crystal X-ray diffraction, thermogravimetric analysis, and IR and UV-visible spectroscopies. Water 104-107 mitochondrially encoded cytochrome c oxidase II Homo sapiens 26-30 17386766-0 2007 A quantitative method for determination of Co(II) based on the inner filter effect of reagents on the Raman scattering signals of water. Water 130-135 mitochondrially encoded cytochrome c oxidase II Homo sapiens 43-49 17822232-0 2007 Determination of cobalt at ng ml(-1) level in water using the electrophilic substiution complexation between co(II) and chlorophosphonazo-p-CL-Cu(II) complex. Water 46-51 mitochondrially encoded cytochrome c oxidase II Homo sapiens 109-115 17822232-5 2007 The proposed method has been applied to the direct detection of Co(II) in surface water and wastewater with good percent of recovery. Water 82-87 mitochondrially encoded cytochrome c oxidase II Homo sapiens 64-70 17309209-9 2007 In the Co(TPMCP) Langmuir films formed on the water subphases, Co(II) was complexed by aromatic but not cyclic heteroaliphatic ligands, while, in these films formed on the NaCl subphase solutions, the metalloporphyrin was also complexed by DABCO. Water 46-51 mitochondrially encoded cytochrome c oxidase II Homo sapiens 63-69 19071321-3 2007 Co(II) was rapidly and quantitatively back-extracted with deionised water. Water 68-73 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-6 17723766-5 2006 The chemosensor has been used for determination of Co(II) in water samples. Water 61-66 mitochondrially encoded cytochrome c oxidase II Homo sapiens 51-57 17117223-6 2006 In addition to the added electrocatalysis a significant percentage of O2 reduced at the oxidized Co(II)/Pt(II) EPG electrode is converted to H2O as determined by rotating disk electrode measurements. Water 141-144 mitochondrially encoded cytochrome c oxidase II Homo sapiens 97-103 17723778-5 2006 The proposed procedure was applied for Ni(II) and Co(II) determination in water certified reference materials. Water 74-79 mitochondrially encoded cytochrome c oxidase II Homo sapiens 50-56 16097814-0 2005 Novel self-assembled chain of water molecules in a metal-organic framework structure of Co(II) with tartrate acid. Water 30-35 mitochondrially encoded cytochrome c oxidase II Homo sapiens 88-93 16455289-6 2006 The proposed method offers the potential advantages of high sensitivity, simplicity and rapidity for Co(II) and Cr(III) determination, and was successfully applied to the simultaneous determination of both analytes in real water sample. Water 223-228 mitochondrially encoded cytochrome c oxidase II Homo sapiens 101-107 16462098-1 2006 Meloxicam (MLX), a non-steroidal anti-inflammatory drug (NSAID) and a selective COX-2 inhibitor is a water insoluble drug (about 12 microg/ml). Water 101-106 mitochondrially encoded cytochrome c oxidase II Homo sapiens 80-85 17017983-11 2006 In contrast lornoxicam and meloxicam, which demonstrated activity against COX-2, have revealed smaller partition capacity in liposomes/water systems together with a higher ability to change the membrane fluidity and surface potential. Water 135-140 mitochondrially encoded cytochrome c oxidase II Homo sapiens 74-79 16633692-6 2006 In particular, we investigated the dissociation path of one water molecule from the first hydration shell of Co(II) with CPMD. Water 60-65 mitochondrially encoded cytochrome c oxidase II Homo sapiens 109-115 16582994-0 2006 A new Co(II) coordination solid with mixed oxygen, carboxylate, pyridine and thiolate donors exhibiting canted antiferromagnetism with T(C) approximately 68 K. Reaction of Co(II) chloride with the sodium salt of 2-mercaptonicotinic acid in water at 200 degrees C results in the formation of Co4(2-mna)4(H2O), which orders as a canted antiferromagnet at 68 K. Water 303-306 mitochondrially encoded cytochrome c oxidase II Homo sapiens 6-12 16582994-0 2006 A new Co(II) coordination solid with mixed oxygen, carboxylate, pyridine and thiolate donors exhibiting canted antiferromagnetism with T(C) approximately 68 K. Reaction of Co(II) chloride with the sodium salt of 2-mercaptonicotinic acid in water at 200 degrees C results in the formation of Co4(2-mna)4(H2O), which orders as a canted antiferromagnet at 68 K. Water 303-306 mitochondrially encoded cytochrome c oxidase II Homo sapiens 6-11 16363471-6 2005 The results showed that the technique is satisfactory to determine Co(II) at trace level in water samples with a detection limit of 2.3 ng/ml. Water 92-97 mitochondrially encoded cytochrome c oxidase II Homo sapiens 67-73 18969902-6 2005 The validation of the method is performed by the analyses of certified reference materials and comparing the result of Co(II) determination in river water sample by the proposed method with those obtained by ET AAS. Water 149-154 mitochondrially encoded cytochrome c oxidase II Homo sapiens 119-125 15840770-0 2005 COX-2 inhibition prevents downregulation of key renal water and sodium transport proteins in response to bilateral ureteral obstruction. Water 54-59 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-5 15837305-0 2005 Novel approach to pro-drugs of lactones: water soluble imidate and ortho-ester derivatives of a furanone-based COX-2 selective inhibitor. Water 41-46 mitochondrially encoded cytochrome c oxidase II Homo sapiens 111-116 15837305-1 2005 Interest in water soluble COX-2 inhibitors that can be administered intravenously led to the development of novel pro-drugs of a furanone based COX-2 inhibitor 2. Water 12-17 mitochondrially encoded cytochrome c oxidase II Homo sapiens 26-31 15837305-1 2005 Interest in water soluble COX-2 inhibitors that can be administered intravenously led to the development of novel pro-drugs of a furanone based COX-2 inhibitor 2. Water 12-17 mitochondrially encoded cytochrome c oxidase II Homo sapiens 144-149 15870622-13 2005 CONCLUSION: This study has confirmed that selective and nonselective COX inhibition can induce significant inhibition of free water clearance, indicating that these acute changes are regulated predominantly via COX-2. Water 126-131 mitochondrially encoded cytochrome c oxidase II Homo sapiens 211-216 15813652-6 2005 The adverse reaction profile of the COX-2 inhibitors has confirmed the role of the COX-2 enzyme in renal function, salt and water homeostasis and the vascular endothelium. Water 124-129 mitochondrially encoded cytochrome c oxidase II Homo sapiens 36-41 15813652-6 2005 The adverse reaction profile of the COX-2 inhibitors has confirmed the role of the COX-2 enzyme in renal function, salt and water homeostasis and the vascular endothelium. Water 124-129 mitochondrially encoded cytochrome c oxidase II Homo sapiens 83-88 15350923-1 2004 A series of new metal complexes of Co(II), Ce(III) and UO(2)(VI), with the Schiff base ligand, H2L, bis-salicylatothiosemicarbazide have been prepared in presence of different molar ratios of LiOH.H2O as a deprotonating agent. Water 197-200 mitochondrially encoded cytochrome c oxidase II Homo sapiens 35-41 15692221-1 2005 BACKGROUND/AIMS: Water diuresis usually increases medullary oxygenation as a result of increased medullary synthesis of prostaglandins, but it is not clear whether this involves activation of cyclooxygenase-1 (COX-1) or cyclooxygenase-2 (COX-2). Water 17-22 mitochondrially encoded cytochrome c oxidase II Homo sapiens 238-243 15692221-8 2005 CONCLUSION: Renal medullary oxygenation is improved by water diuresis in normal young women in a way that is blocked by a selective inhibitor of COX-2 as well as non-selective cyclooxygenase inhibitors. Water 55-60 mitochondrially encoded cytochrome c oxidase II Homo sapiens 145-150 15106969-2 2004 However, Co(III) can bind water far more strongly than Co(II) as a sixth ligand, so that the competition between water and NO complexation strongly favors water for Co(III) in the gas phase. Water 113-118 mitochondrially encoded cytochrome c oxidase II Homo sapiens 55-61 15328060-10 2004 The exact local structure of the inner sphere Co(II) surface complexes, formed by exchanging the H(2)O ligands with surface oxygens, has been already approached but only for the surface planes of the alpha-Al(2)O(3) and rutile monocrystals. Water 97-102 mitochondrially encoded cytochrome c oxidase II Homo sapiens 46-52 15106969-2 2004 However, Co(III) can bind water far more strongly than Co(II) as a sixth ligand, so that the competition between water and NO complexation strongly favors water for Co(III) in the gas phase. Water 113-118 mitochondrially encoded cytochrome c oxidase II Homo sapiens 55-61 15106969-3 2004 Although the Co(II) oxidation state is found to bind water slightly more strongly than NO in the gas phase, the inclusion of solvation effects via the polarizeable continuum model makes NO binding more favorable. Water 53-58 mitochondrially encoded cytochrome c oxidase II Homo sapiens 13-19 14577772-5 2003 Its eight cyanide groups are coordinated to Co(II) ions which have two coordinated water molecules in trans position. Water 83-88 mitochondrially encoded cytochrome c oxidase II Homo sapiens 44-50 15134917-2 2004 In 10% methanol/water, the one-electron reduction of quinones L1 and L2 to the corresponding semiquinones is shifted to more positive potentials upon addition of one equivalent of Zn(II), Ni(II), Co(II) or Cd(II) and is consistent with formation of a 1:1 complex involving the quinone(N) and adjacent quinone(O). Water 16-21 mitochondrially encoded cytochrome c oxidase II Homo sapiens 196-202 14670476-2 2004 The ligand and its metal complexes (Co(II)-PAN and Ni(II)-PAN) were made water-soluble by the neutral surfactant Triton X-100, and therefore, no extraction with organic solvents was required. Water 73-78 mitochondrially encoded cytochrome c oxidase II Homo sapiens 36-42 15110946-7 2004 The aqua Co(II) complex must be the reactive catalytic species in the catalyzed dehydration reaction and the rate-determining step is the substitution of the labile water molecule by HCO3-. Water 165-170 mitochondrially encoded cytochrome c oxidase II Homo sapiens 9-15 12513074-6 2003 The octahedral environment around each Co(II) is complemented by another singly bonded citrate belonging to the adjacent Co(II) unit and two water molecules. Water 141-146 mitochondrially encoded cytochrome c oxidase II Homo sapiens 39-45 12889922-1 2003 A new type of cyano-bridged Co-W bimetallic assembly, CsI[{CoII(3-cyanopyridine)2}{WV(CN)8}].H2O was synthesized. Water 93-96 mitochondrially encoded cytochrome c oxidase II Homo sapiens 59-63 12484230-0 2002 Colonic luminal contents (faecal water) induce COX-2. Water 33-38 mitochondrially encoded cytochrome c oxidase II Homo sapiens 47-52 12196951-2 2002 The synthesis of a verdazyl radical with a carboxylate substituent renders the radical highly soluble in water, thereby permitting the aqueous synthesis of Ni(II) and Co(II) verdazyl complexes which have been structurally and magnetically characterized. Water 105-110 mitochondrially encoded cytochrome c oxidase II Homo sapiens 167-173 12079454-8 2002 In it, there exist mononuclear octahedral sites of Co(II) surrounded by oxygens, belonging to terminal phosphonates and bound water molecules. Water 126-131 mitochondrially encoded cytochrome c oxidase II Homo sapiens 51-57 12007092-2 2002 Accurate single-crystal diffraction data were measured on a suitable crystal with Mo(K alpha) radiation at 125 K. The CoII ion is coordinated in a square bipyramidal fashion with four imino nitrogen atoms at the equatorial plane and two water molecules at the axial positions. Water 237-242 mitochondrially encoded cytochrome c oxidase II Homo sapiens 118-122 12487621-14 2003 However, trials with the new COX-2 inhibitors offer the chance to address these open questions of highly selective COX-2 inhibition; that is, thrombogenic risk, sodium and water retention, and interference with tissue repair, in particular, healing of mucosal damage. Water 172-177 mitochondrially encoded cytochrome c oxidase II Homo sapiens 29-34 12044078-0 2002 Kinetics of adsorption of Co(II) removal from water and wastewater by ion exchange resins. Water 46-51 mitochondrially encoded cytochrome c oxidase II Homo sapiens 26-32 11118975-1 2000 The Co(II) ion lies on an inversion centre and is octahedrally coordinated to two trimesate anions and four water molecules. Water 108-113 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 11414818-1 2001 Catalysis of (18)O exchange between CO(2) and water catalyzed by a Co(II)-substituted mutant of human carbonic anhydrase II is analyzed to show the rate of release of H(2)(18)O from the active site. Water 46-51 mitochondrially encoded cytochrome c oxidase II Homo sapiens 67-72 11330996-9 2001 Considering only the high-affinity site, there is a diminution in the enthalpy of binding through the series Co(II) --> Zn(II) --> Cu(II) that mirrors the enthalpy of hydration; this observation reinforces the notion that the thermodynamics of solute association with water is at least as important as the thermodynamics of solute-solute interaction and that these effects must be considered when interpreting association in aqueous solution. Water 274-279 mitochondrially encoded cytochrome c oxidase II Homo sapiens 109-115 11300810-1 2001 (1/2)H2O and in the spin crossover complexes [Co(II)(terpy)2]X2.nH2O (X = Cl and ClO4): a Mossbauer emission spectroscopic study. Water 5-8 mitochondrially encoded cytochrome c oxidase II Homo sapiens 46-51 11195058-6 2001 Whereas COX1 expression does not exhibit dynamic regulation, COX2 expression is subject to regulation by several environmental conditions, including salt intake, water intake, medullary tonicity, growth factors, cytokines, and adrenal steroids. Water 162-167 mitochondrially encoded cytochrome c oxidase II Homo sapiens 61-65 18966220-4 1995 The polymer used in this study was Polymin Water-Free and its complexation with Hg(II), Cd(II), Pb(II), Co(II) and Ni(II) was successfully modelled. Water 43-48 mitochondrially encoded cytochrome c oxidase II Homo sapiens 104-110 10469539-4 1999 Based on EXAFS results and bond valence analysis, plausible surface complexation reactions for Co(II) sorption on these two surfaces can be written as represent surface water molecules, hydroxyl groups, and oxygens bonded to one, two, and three Al cations, respectively. Water 169-174 mitochondrially encoded cytochrome c oxidase II Homo sapiens 95-101 10101953-0 1999 Selective COX-2 inhibitors: is the water becoming muddy? Water 35-40 mitochondrially encoded cytochrome c oxidase II Homo sapiens 10-15 9524553-4 1998 In MeCN/H2O electrochemical reduction is irreversible, indicating rapid substitution of H2O into the coordination sphere of the Co(II) intermediate. Water 8-11 mitochondrially encoded cytochrome c oxidase II Homo sapiens 128-134 9524553-4 1998 In MeCN/H2O electrochemical reduction is irreversible, indicating rapid substitution of H2O into the coordination sphere of the Co(II) intermediate. Water 88-91 mitochondrially encoded cytochrome c oxidase II Homo sapiens 128-134 18967999-6 2000 The developed method was applied to Co(II) determination in potable water. Water 68-73 mitochondrially encoded cytochrome c oxidase II Homo sapiens 36-42 9720310-6 1998 UV and O2 consumption measurements showed that the reaction of Co with water consumed molecular oxygen and generated Co(II). Water 71-76 mitochondrially encoded cytochrome c oxidase II Homo sapiens 117-123 8371984-8 1993 Model building of Co(II) binding to guanine N7 in B-DNA indicates that the coordinated waters in the axial positions would have a van der Waals clash with the neighboring base on the 5" side. Water 87-93 mitochondrially encoded cytochrome c oxidase II Homo sapiens 18-24 34549505-6 2021 And the amorphous Co(II) component accelerates the water dissociation. Water 51-56 mitochondrially encoded cytochrome c oxidase II Homo sapiens 18-24 18965533-1 1992 Single-phase solutions (1.72 x 10(-2)M in TTA) of water/ethanol/MIBK, when added to an excess of water, break down into two immiscible liquid layers and TTA complexes of Fe(III), Co(II), Ni(II), Cu(II) and PB(II) are extracted into the organic layer. Water 50-55 mitochondrially encoded cytochrome c oxidase II Homo sapiens 179-185 1316186-10 1992 An experiment using 17O-enriched water revealed that the Co(II)-ethylenediamine complex caused the DMPO to react with solvent water to form the DMPO/.OH adduct. Water 33-38 mitochondrially encoded cytochrome c oxidase II Homo sapiens 57-63 1316186-10 1992 An experiment using 17O-enriched water revealed that the Co(II)-ethylenediamine complex caused the DMPO to react with solvent water to form the DMPO/.OH adduct. Water 126-131 mitochondrially encoded cytochrome c oxidase II Homo sapiens 57-63 34702033-2 2021 Herein, the electric active CoII ion is selected to coordinate with redox-active S-rich tetrathiafulvalene (TTF) derivatives to create two TTF-Co-MOFs, formulated as (Co2(py-TTF-py)2(BDC)2) 2DMF H2O (TTF-Co-MOF 1) and (Co2(py-TTF-py)2(BPDC)2) 3DMF 3H2O (TTF-Co-MOF 2), where py-TTF-py = 2,6-bis(4"-pyridyl)tetrathiafulvalene, H2BDC = terephthalic acid, H2BPDC = biphenyl-4,4"-dicarboxylic acid, and DMF = N,N-dimethylformamide. Water 195-198 mitochondrially encoded cytochrome c oxidase II Homo sapiens 28-32 34726676-1 2021 Herein a 1D Co(II) coordination polymer of formula (Co(eta1-L1)(eta2-L1)(py)2(H2O))n (CoCP) has been synthesised using the rigid H2L1 proligand, containing a long spacer bearing two triple bonds. Water 78-81 mitochondrially encoded cytochrome c oxidase II Homo sapiens 12-18 34248399-1 2021 In this current experiment, by applying the mixed-ligand synthesis method, two coordination polymers (CPs) containing Co(II) were created triumphantly with reaction between 1,3-bis(1-imidazoly)benzene (mbib) and Co(II) salts with the aid of diverse carboxylic ligands, and their chemical formulae are (Co3(opda)3(mbib)4(H2O)4) 2H2O (1, H2opda is 1,2-phenylenediacetic acid) and (Co(mpda)(mbib)) H2O (2, H2mpda is 1,3-phenylenediacetic acid). Water 320-323 mitochondrially encoded cytochrome c oxidase II Homo sapiens 118-124 34586126-2 2021 Treatment of the PtII2PdII2 tetranuclear complex (Pd2{Pt(NH3)2(D-pen)2}2) ((1); D-H2pen = D-penicillamine) with CoX2 (X = Cl, Br) provided (PtII2PdII2CoII2)n coordination polymers (Co2(H2O)6(1))X4 ((2)X4), in which the PtII2PdII2 units of (1) are linked by (Co2(mu-H2O)(H2O)5)4+ moieties in a 3D network structure. Water 185-188 mitochondrially encoded cytochrome c oxidase II Homo sapiens 112-116 34586126-2 2021 Treatment of the PtII2PdII2 tetranuclear complex (Pd2{Pt(NH3)2(D-pen)2}2) ((1); D-H2pen = D-penicillamine) with CoX2 (X = Cl, Br) provided (PtII2PdII2CoII2)n coordination polymers (Co2(H2O)6(1))X4 ((2)X4), in which the PtII2PdII2 units of (1) are linked by (Co2(mu-H2O)(H2O)5)4+ moieties in a 3D network structure. Water 265-268 mitochondrially encoded cytochrome c oxidase II Homo sapiens 112-116 34586126-2 2021 Treatment of the PtII2PdII2 tetranuclear complex (Pd2{Pt(NH3)2(D-pen)2}2) ((1); D-H2pen = D-penicillamine) with CoX2 (X = Cl, Br) provided (PtII2PdII2CoII2)n coordination polymers (Co2(H2O)6(1))X4 ((2)X4), in which the PtII2PdII2 units of (1) are linked by (Co2(mu-H2O)(H2O)5)4+ moieties in a 3D network structure. Water 270-273 mitochondrially encoded cytochrome c oxidase II Homo sapiens 112-116 34586126-3 2021 (2)X4 showed a colour change from orange to dark green upon dehydration, reflecting the geometrical conversion of the CoII centres in (Co2(mu-H2O)(H2O)5)4+ from an octahedron to a tetrahedron by the removal of aqua ligands. Water 142-145 mitochondrially encoded cytochrome c oxidase II Homo sapiens 118-122 34586126-3 2021 (2)X4 showed a colour change from orange to dark green upon dehydration, reflecting the geometrical conversion of the CoII centres in (Co2(mu-H2O)(H2O)5)4+ from an octahedron to a tetrahedron by the removal of aqua ligands. Water 147-150 mitochondrially encoded cytochrome c oxidase II Homo sapiens 118-122 34586126-4 2021 While both (2)Cl4 and (2)Br4 electrochemically catalysed water reduction to H2 in the solid state due to the presence of PdII active centres, water oxidation to O2 was catalysed only by (2)Br4, which is ascribed to the presence of Br- ions that mediate the catalytic reactions that occurred at CoII active centres. Water 57-62 mitochondrially encoded cytochrome c oxidase II Homo sapiens 294-298 34586126-4 2021 While both (2)Cl4 and (2)Br4 electrochemically catalysed water reduction to H2 in the solid state due to the presence of PdII active centres, water oxidation to O2 was catalysed only by (2)Br4, which is ascribed to the presence of Br- ions that mediate the catalytic reactions that occurred at CoII active centres. Water 142-147 mitochondrially encoded cytochrome c oxidase II Homo sapiens 294-298 34246991-8 2021 However, in real water samples, the selectivity and efficiency for HEDP removal in the Co(II)/PMS process are higher than that in free radicals-mediated advanced oxidation processes. Water 17-22 mitochondrially encoded cytochrome c oxidase II Homo sapiens 87-93 34269774-1 2021 Herein we report heteroleptic Co(ii) diimine complexes (Co(H2bip)2Cl2) (1), (Co(H2bip)2Br2) (2), (Co(H2bip)3)Br2 1MeOH (3) and (Co(H2bip)2(Me2bpy))Br2 (MeCN)0.5 (H2O)0.25 (4) (H2bip = 2,2"-bi-1,4,5,6-tetrahydropyrimidine, bpy = 2,2"-dipyridyl, Me2bpy = 4,4"-Me-2,2"-dipyridyl), purposefully prepared to enable a systematic study of magnetic property changes arising from the increase of overall ligand field from sigma/pi-donor chlorido (1) to pi-acceptor 4,4"Me-2,2"bpy (4). Water 162-165 mitochondrially encoded cytochrome c oxidase II Homo sapiens 30-36 34584766-1 2021 The asymmetric unit of the polymeric title compound {(Co2(C12H7NO8)(H2O)2) 1.6H2O} n comprises two CoII ions, which are coordinated by fully deprotonated 2-aminodi-acetic terephthalic acid (adtp4-) and terminal water mol-ecules in distorted octa-hedral N1O5 and O6 coordination environments. Water 68-71 mitochondrially encoded cytochrome c oxidase II Homo sapiens 99-103 34584766-1 2021 The asymmetric unit of the polymeric title compound {(Co2(C12H7NO8)(H2O)2) 1.6H2O} n comprises two CoII ions, which are coordinated by fully deprotonated 2-aminodi-acetic terephthalic acid (adtp4-) and terminal water mol-ecules in distorted octa-hedral N1O5 and O6 coordination environments. Water 211-216 mitochondrially encoded cytochrome c oxidase II Homo sapiens 99-103 34641564-1 2021 Here we present the synthesis, structure and magnetic properties of complexes of general formula (Mn)(Me2NH2)4)(Mn3(mu-L)6(H2O)6) and (Me2NH2)6(M3(mu-L)6(H2O)6) (M = CoII, NiII and CuII); L-2 = 4-(1,2,4-triazol-4-yl) ethanedisulfonate). Water 154-157 mitochondrially encoded cytochrome c oxidase II Homo sapiens 166-170 34248399-1 2021 In this current experiment, by applying the mixed-ligand synthesis method, two coordination polymers (CPs) containing Co(II) were created triumphantly with reaction between 1,3-bis(1-imidazoly)benzene (mbib) and Co(II) salts with the aid of diverse carboxylic ligands, and their chemical formulae are (Co3(opda)3(mbib)4(H2O)4) 2H2O (1, H2opda is 1,2-phenylenediacetic acid) and (Co(mpda)(mbib)) H2O (2, H2mpda is 1,3-phenylenediacetic acid). Water 320-323 mitochondrially encoded cytochrome c oxidase II Homo sapiens 212-218 34248399-1 2021 In this current experiment, by applying the mixed-ligand synthesis method, two coordination polymers (CPs) containing Co(II) were created triumphantly with reaction between 1,3-bis(1-imidazoly)benzene (mbib) and Co(II) salts with the aid of diverse carboxylic ligands, and their chemical formulae are (Co3(opda)3(mbib)4(H2O)4) 2H2O (1, H2opda is 1,2-phenylenediacetic acid) and (Co(mpda)(mbib)) H2O (2, H2mpda is 1,3-phenylenediacetic acid). Water 395-398 mitochondrially encoded cytochrome c oxidase II Homo sapiens 118-124 34248399-1 2021 In this current experiment, by applying the mixed-ligand synthesis method, two coordination polymers (CPs) containing Co(II) were created triumphantly with reaction between 1,3-bis(1-imidazoly)benzene (mbib) and Co(II) salts with the aid of diverse carboxylic ligands, and their chemical formulae are (Co3(opda)3(mbib)4(H2O)4) 2H2O (1, H2opda is 1,2-phenylenediacetic acid) and (Co(mpda)(mbib)) H2O (2, H2mpda is 1,3-phenylenediacetic acid). Water 395-398 mitochondrially encoded cytochrome c oxidase II Homo sapiens 212-218 35570193-2 2022 Herein we report three heterobimetallic uranyl phosphonates, namely, ((UO2)3M(2-pmbH)4(H2O)4) 2H2O (MU, M = Co(II), CoU; Mn(II), MnU; Zn(II), ZnU; 2-pmbH3 = 2-(phosphonomethyl)benzoic acid). Water 87-90 mitochondrially encoded cytochrome c oxidase II Homo sapiens 108-114 34100579-2 2021 We constructed an acid-/base-stable Co(II)-framework with a unique network topology, wherein unidirectional porous channels are decorated by anionic (Co2(mu2-OH)(COO)4(H2O)3) secondary building units and neutral (CoN2(COO)2) nodes. Water 168-171 mitochondrially encoded cytochrome c oxidase II Homo sapiens 36-42 34070757-5 2021 Anthocyanins, water-soluble flavonoid species, responsible for the red-blue color in plants and commonly found in berries, exert favorable effects on the endothelial function, oxidative stress, inhibit COX-1, and COX-2 enzymes, exert antiatherogenic, antihypertensive, antiglycation, antithrombotic, and anti-inflammatory activity, ameliorate dyslipidemia and arterial stiffness. Water 14-19 mitochondrially encoded cytochrome c oxidase II Homo sapiens 213-218 34306978-4 2021 X-ray absorption fine spectra reveal that the activation of Co (II) ions (in NH4CoPO4 H2O) to Co (III) species constructs the electrocatalytic active sites. Water 86-89 mitochondrially encoded cytochrome c oxidase II Homo sapiens 60-67 34155432-3 2021 The complexes (M(GA)2(H2O)2), where (M = Mn(II), Co(II), and Ni(II)) form octahedral structures, while (M(GA)2) complexes (M = Zn(II), Cd(II), and Hg(II)) display four-coordination geometry. Water 22-25 mitochondrially encoded cytochrome c oxidase II Homo sapiens 49-55 34151097-9 2021 Additionally, the applicability of the current Co(II)-MOF approach in different real water samples, such as tap water, drinking water, Nile River water, and wastewater, was extended. Water 85-90 mitochondrially encoded cytochrome c oxidase II Homo sapiens 47-53 34151097-9 2021 Additionally, the applicability of the current Co(II)-MOF approach in different real water samples, such as tap water, drinking water, Nile River water, and wastewater, was extended. Water 112-117 mitochondrially encoded cytochrome c oxidase II Homo sapiens 47-53 34151097-9 2021 Additionally, the applicability of the current Co(II)-MOF approach in different real water samples, such as tap water, drinking water, Nile River water, and wastewater, was extended. Water 128-133 mitochondrially encoded cytochrome c oxidase II Homo sapiens 47-53 34151097-9 2021 Additionally, the applicability of the current Co(II)-MOF approach in different real water samples, such as tap water, drinking water, Nile River water, and wastewater, was extended. Water 146-151 mitochondrially encoded cytochrome c oxidase II Homo sapiens 47-53 34257875-4 2021 The tetracobalt Weakley sandwich (CoII 4(H2O)2(B-alpha-PW9O34)2)10- (Co4-WS) has been one of the most extensively studied. Water 41-44 mitochondrially encoded cytochrome c oxidase II Homo sapiens 34-38 35172100-0 2022 Catalytic Mechanism of Competing Proton Transfer Events from Water and Acetic Acid by (CoII(bpbH2)Cl2) for Water Splitting Processes. Water 107-112 mitochondrially encoded cytochrome c oxidase II Homo sapiens 87-91 35358381-7 2022 Further, the investigation of the ORR activity of Co(10-DMIC) using a combination of electrochemical and chemical reduction studies revealed that this simple, unadorned monomeric Co(II) tetrapyrrole is ~85% selective for the 4e-/4H+ reduction of O2 to H2O over the more kinetically facile 2e-/2H+ process that delivers H2O2. Water 252-255 mitochondrially encoded cytochrome c oxidase II Homo sapiens 179-185 35234225-0 2022 A tetra Co(II/III) complex with an open cubane Co4O4 core and square-pyramidal Co(II) and octahedral Co(III) centres: bifunctional electrocatalytic activity towards water splitting at neutral pH. Water 165-170 mitochondrially encoded cytochrome c oxidase II Homo sapiens 79-85 35172100-0 2022 Catalytic Mechanism of Competing Proton Transfer Events from Water and Acetic Acid by (CoII(bpbH2)Cl2) for Water Splitting Processes. Water 61-66 mitochondrially encoded cytochrome c oxidase II Homo sapiens 87-91 35172100-1 2022 We performed first principles simulations to explore the water reduction process of the cobalt complex (CoII(bpbH2)Cl2), where bpbH2 = N,N"-bis(2"-pyridine carboxamide)-1,2-benzene. Water 57-62 mitochondrially encoded cytochrome c oxidase II Homo sapiens 104-108 35172100-8 2022 The second proton transfer from water to the CoII-H moiety requires less free energy than acetic acid and is the rate-limiting step. Water 32-37 mitochondrially encoded cytochrome c oxidase II Homo sapiens 45-49 34877950-1 2022 Divalent transition metals such as Co(II) are important targets for removal from water sources, due to their potential toxicity as well as their high value. Water 81-86 mitochondrially encoded cytochrome c oxidase II Homo sapiens 35-41 34991150-4 2022 The Co(II) complex with 3,9-PC2AMtBu shows a similar six-coordinate structure in the solid state, while the Co(II) complex with 3,9-PC2AMH contains a seven-coordinate metal ion, seventh coordination being completed by the presence of an inner-sphere water molecule. Water 250-255 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 34991150-4 2022 The Co(II) complex with 3,9-PC2AMtBu shows a similar six-coordinate structure in the solid state, while the Co(II) complex with 3,9-PC2AMH contains a seven-coordinate metal ion, seventh coordination being completed by the presence of an inner-sphere water molecule. Water 250-255 mitochondrially encoded cytochrome c oxidase II Homo sapiens 108-114 34991150-10 2022 The presence of highly shifted 1H NMR signals due to the amide protons in slow exchange with bulk water results in sizeable CEST signals, which are observed at +67 and +15 ppm for the Co(II) complex with 3,9-PC2AMH and +42 and +7 ppm for the Ni(II) analogue at 25 C. Water 98-103 mitochondrially encoded cytochrome c oxidase II Homo sapiens 184-190