PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 31453072-0 2019 Erratum: Co (II) Boron Imidazolate Framework with Rigid Auxiliary Linkers for Stable Electrocatalytic Oxygen Evolution Reaction. Oxygen 102-108 mitochondrially encoded cytochrome c oxidase II Homo sapiens 9-15 30776354-4 2019 In the present study, we used a gene microarray and western blotting analysis to show that the expression of mitochondrially encoded cytochrome c oxidase subunit 2 (MT-CO2, COXII) increased significantly in SH-SY5Y cells stimulated by alpha-Syn for 24 h. Furthermore, the decline in ATP levels, the decreased mitochondrial membrane potential, and the enhanced reactive oxygen species in cells treated by alpha-Syn was reversed by inhibiting MT-CO2 gene expression. Oxygen 369-375 mitochondrially encoded cytochrome c oxidase II Homo sapiens 165-171 30848866-2 2019 CoII sites associated with oxygen vacancies were favored at low temperatures and performed selective C-O hydrogenolysis, in which Sr-substitution facilitated oxygen vacancy formation, leading to approximately 10 times higher reactivity compared to undoped LaCoO3 . Oxygen 27-33 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-4 30848866-2 2019 CoII sites associated with oxygen vacancies were favored at low temperatures and performed selective C-O hydrogenolysis, in which Sr-substitution facilitated oxygen vacancy formation, leading to approximately 10 times higher reactivity compared to undoped LaCoO3 . Oxygen 158-164 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-4 30398331-0 2018 Oxygen-Oxygen Bond Cleavage and Formation in Co(II)-Mediated Stoichiometric O2 Reduction via the Potential Intermediacy of a Co(IV) Oxyl Radical. Oxygen 0-6 mitochondrially encoded cytochrome c oxidase II Homo sapiens 45-51 30888790-5 2019 The functional utility of Co(II)-MOF is demonstrated by employing it toward oxygen evolution reaction (OER) in a photoelectrochemical cell, exhibiting appreciable photocurrents of up to 5.89 mA/cm2 when used as an anode in a photoelectrochemical cell, while also displaying encouraging electrocatalytic currents of 9.32 mA/cm2 (at 2.01 V vs RHE) for the OER. Oxygen 76-82 mitochondrially encoded cytochrome c oxidase II Homo sapiens 26-32 30724472-0 2019 Efficient Fe-Co-N-C Electrocatalyst Towards Oxygen Reduction Derived from a Cationic CoII -based Metal-Organic Framework Modified by Anion-Exchange with Potassium Ferricyanide. Oxygen 44-50 mitochondrially encoded cytochrome c oxidase II Homo sapiens 85-89 31562623-1 2019 The Cyclooxygenase enzymes (COX-1 and COX-2) incorporate 2 molecules of O2 into arachidonic acid (AA), resulting in an array of bioactive prostaglandins. Oxygen 72-74 mitochondrially encoded cytochrome c oxidase II Homo sapiens 38-43 30398331-0 2018 Oxygen-Oxygen Bond Cleavage and Formation in Co(II)-Mediated Stoichiometric O2 Reduction via the Potential Intermediacy of a Co(IV) Oxyl Radical. Oxygen 7-13 mitochondrially encoded cytochrome c oxidase II Homo sapiens 45-51 30398331-0 2018 Oxygen-Oxygen Bond Cleavage and Formation in Co(II)-Mediated Stoichiometric O2 Reduction via the Potential Intermediacy of a Co(IV) Oxyl Radical. Oxygen 76-78 mitochondrially encoded cytochrome c oxidase II Homo sapiens 45-51 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. Oxygen 41-44 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. Oxygen 108-110 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. Oxygen 195-197 mitochondrially encoded cytochrome c oxidase II Homo sapiens 134-140 31458563-10 2018 The calculations show that a small part of the inorganic spins are delocalized over the oxygens from hfac {~0.03 for Co(II) and ~0.015 for Mn(II)}, whereas a more significant fraction {~0.24 for Mn(II) and ~0.13 for Co(II)} of delocalized spins from the metal ion is transferred to the coordinated oxygen atom(s) of nitronyl nitroxide. Oxygen 88-95 mitochondrially encoded cytochrome c oxidase II Homo sapiens 117-123 29741888-0 2018 Electron and Oxygen Atom Transfer Chemistry of Co(II) in a Proton Responsive, Redox Active Ligand Environment. Oxygen 13-19 mitochondrially encoded cytochrome c oxidase II Homo sapiens 47-53 29799201-2 2018 XPS analysis shows the CuCo2O4@CQDs possesses the Co(II)-rich surface associated with the oxygen vacancies, which can effectively boost the Faradaic reactions and oxygen evolution reaction (OER) activity. Oxygen 90-96 mitochondrially encoded cytochrome c oxidase II Homo sapiens 50-56 29799201-2 2018 XPS analysis shows the CuCo2O4@CQDs possesses the Co(II)-rich surface associated with the oxygen vacancies, which can effectively boost the Faradaic reactions and oxygen evolution reaction (OER) activity. Oxygen 163-169 mitochondrially encoded cytochrome c oxidase II Homo sapiens 50-56 29799201-5 2018 The synergy of Co(II)-rich surface, oxygen vacancies, and well-defined 3D hollow structures facilitates the subsequent surface electrochemical reactions. Oxygen 36-42 mitochondrially encoded cytochrome c oxidase II Homo sapiens 15-20 29407982-4 2018 Docking studies revealed the capacity of this compound to occupy the selective COX-2 cavity establishing additional hydrogen bonds between the oxygen of the methoxy group and the His90 and Arg513 of the binding site of the enzyme. Oxygen 143-149 mitochondrially encoded cytochrome c oxidase II Homo sapiens 79-84 31458563-10 2018 The calculations show that a small part of the inorganic spins are delocalized over the oxygens from hfac {~0.03 for Co(II) and ~0.015 for Mn(II)}, whereas a more significant fraction {~0.24 for Mn(II) and ~0.13 for Co(II)} of delocalized spins from the metal ion is transferred to the coordinated oxygen atom(s) of nitronyl nitroxide. Oxygen 88-94 mitochondrially encoded cytochrome c oxidase II Homo sapiens 117-123 28621377-1 2017 Two bis-tridentate chelated cobalt(ii) complexes, which differ in the ligand structure by a methylene group, activate molecular oxygen (O2), and give different oxidation products. Oxygen 128-134 mitochondrially encoded cytochrome c oxidase II Homo sapiens 35-37 29086874-0 2017 Reversible uptake of molecular oxygen by heteroligand Co(II)-L-alpha-amino acid-imidazole systems: equilibrium models at full mass balance. Oxygen 31-37 mitochondrially encoded cytochrome c oxidase II Homo sapiens 54-60 29086874-1 2017 BACKGROUND: The paper examines Co(II)-amino acid-imidazole systems (where amino acid = L-alpha-amino acid: alanine, asparagine, histidine) which, when in aqueous solutions, activate and reversibly take up dioxygen, while maintaining the structural scheme of the heme group (imidazole as axial ligand and O2 uptake at the sixth, trans position) thus imitating natural respiratory pigments such as myoglobin and hemoglobin. Oxygen 205-213 mitochondrially encoded cytochrome c oxidase II Homo sapiens 31-37 29086874-1 2017 BACKGROUND: The paper examines Co(II)-amino acid-imidazole systems (where amino acid = L-alpha-amino acid: alanine, asparagine, histidine) which, when in aqueous solutions, activate and reversibly take up dioxygen, while maintaining the structural scheme of the heme group (imidazole as axial ligand and O2 uptake at the sixth, trans position) thus imitating natural respiratory pigments such as myoglobin and hemoglobin. Oxygen 304-306 mitochondrially encoded cytochrome c oxidase II Homo sapiens 31-37 29086874-7 2017 RESULTS: Investigations of oxygenation of the Co(II)-amino acid-imidazole systems indicated that dioxygen uptake proceeds along with a rise in pH to 9-10. Oxygen 97-105 mitochondrially encoded cytochrome c oxidase II Homo sapiens 46-52 29086874-14 2017 CONCLUSIONS: The Co(II)-amac-Himid systems formed by using a [Co(imid)2]n polymer as starting material demonstrate that the reversible uptake of molecular oxygen occurs by forming dimeric mu-peroxy adducts. Oxygen 155-161 mitochondrially encoded cytochrome c oxidase II Homo sapiens 17-23 28758752-4 2017 In the above heteroleptic complexes, the Lewis acidic, coordinatively unsaturated CoII/FeII centers chelated by two hexafluoroacetylacetonate (hfac) ligands maintain bridging interactions with oxygen atoms of acetylacetonate (acac) groups that chelate the neighboring FeIII metal ion. Oxygen 193-199 mitochondrially encoded cytochrome c oxidase II Homo sapiens 82-86 29308820-3 2018 The S-nitrosylation detection and subsequent kinetic investigations into the arachidonic acid (AA) oxidation of COX enzymes indicate that NO S-nitrosylates both COX-1 and COX-2 in an oxygen-dependent manner, but enhances only the dioxygenase activity of COX-2. Oxygen 183-189 mitochondrially encoded cytochrome c oxidase II Homo sapiens 171-176 29308820-4 2018 The solution viscosity, deuterium kinetic isotope effect (KIE), and oxygen-18 KIE experiments further demonstrate that NO activates COX-2 by altering the protein conformation to stimulate substrate association/product release and by accelerating the rate of hydrogen abstraction from AA by catalytic tyrosine radicals. Oxygen 68-74 mitochondrially encoded cytochrome c oxidase II Homo sapiens 132-137 29058412-1 2017 Exposure to humid O2 or ambient air affords a 5-order-of-magnitude increase in electronic conductivity of a new Prussian blue analogue incorporating CoII and VIV-oxo units. Oxygen 18-20 mitochondrially encoded cytochrome c oxidase II Homo sapiens 149-153 29064238-9 2017 The number of electrons transferred (n) during ORRs is 2.0 for the butano(TpYPP)CoII derivatives, consistent with only H2O2 being produced as a product for the reaction with O2. Oxygen 121-123 mitochondrially encoded cytochrome c oxidase II Homo sapiens 80-84 28525865-3 2017 This bidentate ligand coordinates three metal ions of Co(II), Cu(II) and Fe(II) via nitrogen and oxygen atoms. Oxygen 97-103 mitochondrially encoded cytochrome c oxidase II Homo sapiens 54-60 28621377-1 2017 Two bis-tridentate chelated cobalt(ii) complexes, which differ in the ligand structure by a methylene group, activate molecular oxygen (O2), and give different oxidation products. Oxygen 136-138 mitochondrially encoded cytochrome c oxidase II Homo sapiens 35-37 27312695-3 2016 Previously, we had validated the corresponding Co(II) complexes as synthetic model systems for dioxygen-binding heme proteins and demonstrated the structural requirements for proper distal H-bonding to Co(II) -bound dioxygen. Oxygen 95-103 mitochondrially encoded cytochrome c oxidase II Homo sapiens 47-53 31457696-4 2017 The photosensitizing efficiencies of these Ru(II)-photosensitizer-immobilized nanoparticles for the O2 evolution reaction catalyzed by the Co(II)-containing Prussian blue analogue [CoII(H2O)2]1.31[{CoIII(CN)6}0.63{PtII(CN)4}0.37] decreased as the number of Ru(II)-photosensitizing layers increased. Oxygen 100-102 mitochondrially encoded cytochrome c oxidase II Homo sapiens 139-144 28668885-7 2017 TX-1123 bound to the COX2 molecule, and the oxygen atom of the 4-cyclopentene-1,3-dione region of TX-1123 interacted with Cys26 and Gln447 of COX2. Oxygen 44-50 mitochondrially encoded cytochrome c oxidase II Homo sapiens 142-146 28509540-0 2017 Characterization of the High-Spin Co(II) Intermediate Species of the O2-Evolving Co4O4 Cubic Molecules. Oxygen 69-71 mitochondrially encoded cytochrome c oxidase II Homo sapiens 34-40 28509540-8 2017 Additionally, a possible role of the symmetry of the Co(II) species and a proposed model that explains its formation during the O2-evolving process of the Co4O4 cubic molecules are discussed. Oxygen 128-130 mitochondrially encoded cytochrome c oxidase II Homo sapiens 53-58 27312695-3 2016 Previously, we had validated the corresponding Co(II) complexes as synthetic model systems for dioxygen-binding heme proteins and demonstrated the structural requirements for proper distal H-bonding to Co(II) -bound dioxygen. Oxygen 95-103 mitochondrially encoded cytochrome c oxidase II Homo sapiens 202-208 27312695-3 2016 Previously, we had validated the corresponding Co(II) complexes as synthetic model systems for dioxygen-binding heme proteins and demonstrated the structural requirements for proper distal H-bonding to Co(II) -bound dioxygen. Oxygen 216-224 mitochondrially encoded cytochrome c oxidase II Homo sapiens 47-53 27312695-3 2016 Previously, we had validated the corresponding Co(II) complexes as synthetic model systems for dioxygen-binding heme proteins and demonstrated the structural requirements for proper distal H-bonding to Co(II) -bound dioxygen. Oxygen 216-224 mitochondrially encoded cytochrome c oxidase II Homo sapiens 202-208 27312695-5 2016 The H-bond in the dioxygen adducts of the Co(II) porphyrins was directly measured by Q-band Davies-ENDOR spectroscopy. Oxygen 18-26 mitochondrially encoded cytochrome c oxidase II Homo sapiens 42-48 26799113-0 2016 Oxygen Activation by Co(II) and a Redox Non-Innocent Ligand: Spectroscopic Characterization of a Radical-Co(II)-Superoxide Complex with Divergent Catalytic Reactivity. Oxygen 0-6 mitochondrially encoded cytochrome c oxidase II Homo sapiens 21-27 26799113-0 2016 Oxygen Activation by Co(II) and a Redox Non-Innocent Ligand: Spectroscopic Characterization of a Radical-Co(II)-Superoxide Complex with Divergent Catalytic Reactivity. Oxygen 0-6 mitochondrially encoded cytochrome c oxidase II Homo sapiens 105-111 27022316-3 2016 The specific configuration of the alpha-amino acid group affects the eg (1) electron of Co(II) transfer to the pi (*) orbit of O2; this phenomenon also favors the reversible formation and dissociation of Co-O2 bond when O2 coordinates with Co(II) complexes. Oxygen 207-209 mitochondrially encoded cytochrome c oxidase II Homo sapiens 240-246 27022316-3 2016 The specific configuration of the alpha-amino acid group affects the eg (1) electron of Co(II) transfer to the pi (*) orbit of O2; this phenomenon also favors the reversible formation and dissociation of Co-O2 bond when O2 coordinates with Co(II) complexes. Oxygen 207-209 mitochondrially encoded cytochrome c oxidase II Homo sapiens 88-94 27022316-3 2016 The specific configuration of the alpha-amino acid group affects the eg (1) electron of Co(II) transfer to the pi (*) orbit of O2; this phenomenon also favors the reversible formation and dissociation of Co-O2 bond when O2 coordinates with Co(II) complexes. Oxygen 207-209 mitochondrially encoded cytochrome c oxidase II Homo sapiens 240-246 27648004-1 2016 This paper introduces the structural characterization and studies on reversible oxygenation behavior of a new oxygen carrier Co(II)-2,4-diaminobutanoic acid (DABA) complex in aqueous solution. Oxygen 80-86 mitochondrially encoded cytochrome c oxidase II Homo sapiens 125-131 25659740-3 2015 The Cu(II) and Co(II) complexes interacted with CT-DNA via intercalative mode with the respective Kb value of 3.2x10(4) M(-1) and 2.9x10(4) M(-1) and acted as proficient photocleavers of SC pUC19 DNA in UV-A light, forming (1)O2 as the reactive oxygen species with the quantum yield of 0.38 and 0.36, respectively. Oxygen 226-228 mitochondrially encoded cytochrome c oxidase II Homo sapiens 15-21 26677076-2 2016 Polyunsaturated fatty acids (PUFA) metabolism impaired by cyclooxygenases (COX-1, COX-2), which are responsible for formation of several eicosanoids, and by lipoxygenases (LOXs) that catalyze the addition of oxygen to linolenic, arachidonic (AA), and docosahexaenoic acids (DHA) and other PUFA leading to formation of bioactive lipids, significantly affects the course of neurodegenerative diseases. Oxygen 63-69 mitochondrially encoded cytochrome c oxidase II Homo sapiens 82-87 25917121-3 2015 The mechanism of mediated oxygen reduction by single VB12 droplets is revealed as via both Co(II) and Co(I) reduced from Co(III) in VB12 through one or two electron transfer followed by the four-electron reduction of oxygen. Oxygen 26-32 mitochondrially encoded cytochrome c oxidase II Homo sapiens 91-97 25917121-3 2015 The mechanism of mediated oxygen reduction by single VB12 droplets is revealed as via both Co(II) and Co(I) reduced from Co(III) in VB12 through one or two electron transfer followed by the four-electron reduction of oxygen. Oxygen 217-223 mitochondrially encoded cytochrome c oxidase II Homo sapiens 91-97 25798900-4 2015 A paramagnetic S = 3/2 impurity that forms during the synthesis of [Co(II)(dmgH)2P(nBu)3] when exposed to adventitious oxygen has also been characterized. Oxygen 119-125 mitochondrially encoded cytochrome c oxidase II Homo sapiens 68-74 27022316-1 2016 We systematically investigated the reversibility, time lapse, and oxygenation-deoxygenation properties of 15 natural alpha-amino acid-Co(II) complexes through UV-vis spectrophotometer, polarographic oxygen electrode, and DFT calculations, respectively, to explore the relationship between the coordinating structure and reversible oxygenation of alpha-amino acid-Co(II) complexes. Oxygen 66-72 mitochondrially encoded cytochrome c oxidase II Homo sapiens 134-140 27022316-3 2016 The specific configuration of the alpha-amino acid group affects the eg (1) electron of Co(II) transfer to the pi (*) orbit of O2; this phenomenon also favors the reversible formation and dissociation of Co-O2 bond when O2 coordinates with Co(II) complexes. Oxygen 127-129 mitochondrially encoded cytochrome c oxidase II Homo sapiens 88-94 27022316-3 2016 The specific configuration of the alpha-amino acid group affects the eg (1) electron of Co(II) transfer to the pi (*) orbit of O2; this phenomenon also favors the reversible formation and dissociation of Co-O2 bond when O2 coordinates with Co(II) complexes. Oxygen 127-129 mitochondrially encoded cytochrome c oxidase II Homo sapiens 240-246 27022316-3 2016 The specific configuration of the alpha-amino acid group affects the eg (1) electron of Co(II) transfer to the pi (*) orbit of O2; this phenomenon also favors the reversible formation and dissociation of Co-O2 bond when O2 coordinates with Co(II) complexes. Oxygen 207-209 mitochondrially encoded cytochrome c oxidase II Homo sapiens 88-94 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. Oxygen 202-208 mitochondrially encoded cytochrome c oxidase II Homo sapiens 161-167 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. Oxygen 100-106 mitochondrially encoded cytochrome c oxidase II Homo sapiens 168-174 26400662-9 2015 A more accentuated evolution occurs under continuous irradiation, where Electron Paramagnetic Resonance (EPR) spectroscopy reveals the formation of Co(ii) intermediates, likely contributing to the catalytic process that evolves oxygen. Oxygen 228-234 mitochondrially encoded cytochrome c oxidase II Homo sapiens 148-154 24882526-11 2014 Each neutral Co(II) porphyrin was also examined as to its catalytic activity for electroreduction of molecular oxygen when coated on an edge-plane pyrolytic graphite electrode in 1.0 M HClO4. Oxygen 111-117 mitochondrially encoded cytochrome c oxidase II Homo sapiens 13-19 25751962-5 2014 If antioxidant structures with active ingredients of traditional Chinese medicines were introduced to improve the antioxidant activity of NSAIDs, they could scavenge the active oxygen species to protect the normal function of vascular endothelia and enhance the bioavailability of NO, which is conducive to enhance the cardiovascular safety of cyclooxygenase (COX-2) inhibitor. Oxygen 177-183 mitochondrially encoded cytochrome c oxidase II Homo sapiens 360-365 24983538-5 2014 The additional H-bonds with the oxygen of the amide and/or H of NH of the amide with the amino acid residues may be responsible for the higher binding affinity of this group of compounds towards COX-2. Oxygen 32-38 mitochondrially encoded cytochrome c oxidase II Homo sapiens 195-200 23984829-11 2014 Path analysis indicated that number of atoms, oxygen & nitrogen atoms, and Log P are the greatest determinants for formula weight for known COX-2 inhibitors. Oxygen 46-52 mitochondrially encoded cytochrome c oxidase II Homo sapiens 144-149 24562186-0 2014 Outer Co(II) ions in Co-ZIF-67 reversibly adsorb oxygen from both gas phase and liquid water. Oxygen 49-55 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. Oxygen 55-61 mitochondrially encoded cytochrome c oxidase II Homo sapiens 6-12 24564195-5 2014 The Co(II)-poly(EGDE-DA)/H2O2 heterogeneous system produced O2, an anion superoxide (O2( ) ), and a hydroxyl radical (OH( )), which diffused into the solution at the time that a decrease in pH was detected. Oxygen 27-29 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-11 24564195-5 2014 The Co(II)-poly(EGDE-DA)/H2O2 heterogeneous system produced O2, an anion superoxide (O2( ) ), and a hydroxyl radical (OH( )), which diffused into the solution at the time that a decrease in pH was detected. Oxygen 60-62 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-11 24564195-9 2014 In addition, the pharmaceutical product epinephrine was partially oxidized to adrenochrome by the O2( ) released from the Co(II)-poly(EGDE-DA)/H2O2 heterogeneous system. Oxygen 98-100 mitochondrially encoded cytochrome c oxidase II Homo sapiens 123-130 24590498-8 2014 As Ni(II) and Co(II) ions especially favor octahedral coordination geometry in oxygen-ligand fields, Ni(II) ions and Co(II) ions could only selectively exchange with the octahedral Zn(II) ions, as was also confirmed by the experimental results. Oxygen 79-85 mitochondrially encoded cytochrome c oxidase II Homo sapiens 14-20 24590498-8 2014 As Ni(II) and Co(II) ions especially favor octahedral coordination geometry in oxygen-ligand fields, Ni(II) ions and Co(II) ions could only selectively exchange with the octahedral Zn(II) ions, as was also confirmed by the experimental results. Oxygen 79-85 mitochondrially encoded cytochrome c oxidase II Homo sapiens 117-123 24673361-3 2014 When exposed to O2, it transformed from an EPR inactive to an EPR active species indicative of oxidation of Co(I) to Co(II) with the formation of H2O2. Oxygen 16-18 mitochondrially encoded cytochrome c oxidase II Homo sapiens 117-123 24000351-1 2013 The reaction site of the Co(II) porphyrin created by an amide group and coordinating 1,2-dimethylimidazole at the fifth site activated an O2 molecule, and then hydroxylated the meso-carbon of the ligand. Oxygen 138-140 mitochondrially encoded cytochrome c oxidase II Homo sapiens 25-31 24286132-14 2013 CONCLUSIONS: The present findings revealed that FN-fs are more potent than IL-1beta in exerting catabolic effects dependent on oxygen tension via iNOS and COX-2 upregulation. Oxygen 127-133 mitochondrially encoded cytochrome c oxidase II Homo sapiens 155-160 23695032-0 2013 Tuning affinity and reversibility for O2 binding in dinuclear Co(II) complexes. Oxygen 38-40 mitochondrially encoded cytochrome c oxidase II Homo sapiens 62-68 23842534-0 2013 Two novel Co(II) coordination polymers based on 1,4-bis(3-pyridylaminomethyl)benzene as electrocatalysts for oxygen evolution from water. Oxygen 109-115 mitochondrially encoded cytochrome c oxidase II Homo sapiens 10-16 23695032-6 2013 Using density functional theory calculations, we conclude that the Co(II) atoms of the deoxy complexes coordinate solvent molecules as auxiliary ligands and that a conformation change of the ligand is involved in the reversible O2 binding process. Oxygen 228-230 mitochondrially encoded cytochrome c oxidase II Homo sapiens 67-72 23471155-8 2013 Whereas in complex 3, H2L(-) ligand links two Co(II) centers via one oxygen and one sulphur atoms. Oxygen 69-75 mitochondrially encoded cytochrome c oxidase II Homo sapiens 46-52 23646986-4 2013 The Co(II)-Ln(III) and Ni(II)-Ln(III) complexes are crystallized in an isomorphous monoclinic space group P2(1)/c, where the Co(II) or Ni(II) ion at the high-spin state has an octahedral coordination environment with N2O2 donor atoms of 3-MeOsaltn at the equatorial sites, and one oxygen atom of the bridged acetato and a methanol oxygen atom at the two axial sites. Oxygen 281-287 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 23646986-4 2013 The Co(II)-Ln(III) and Ni(II)-Ln(III) complexes are crystallized in an isomorphous monoclinic space group P2(1)/c, where the Co(II) or Ni(II) ion at the high-spin state has an octahedral coordination environment with N2O2 donor atoms of 3-MeOsaltn at the equatorial sites, and one oxygen atom of the bridged acetato and a methanol oxygen atom at the two axial sites. Oxygen 331-337 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 22715144-2 2013 A metal ion-chelating ligand complex with a Co(II) ion and a chelating reagent like ethylenediaminetetraacetic acid (EDTA) produced highly enhanced chemiluminescence (CL) intensity as well as longer lifetime in the luminol-H2 O2 system compared to metals that exist as free ions. Oxygen 226-228 mitochondrially encoded cytochrome c oxidase II Homo sapiens 44-50 23343346-2 2013 The two-electron reduction of O(2) by 1,1"-dibromoferrocene (Br(2)Fc) was catalyzed by Co(II)(Ch), whereas virtually no reduction of O(2) occurred with Co(II)(OEP). Oxygen 30-34 mitochondrially encoded cytochrome c oxidase II Homo sapiens 87-93 23343346-2 2013 The two-electron reduction of O(2) by 1,1"-dibromoferrocene (Br(2)Fc) was catalyzed by Co(II)(Ch), whereas virtually no reduction of O(2) occurred with Co(II)(OEP). Oxygen 30-34 mitochondrially encoded cytochrome c oxidase II Homo sapiens 152-163 23343346-3 2013 In addition, Co(II)(Ch) is more stable than Co(II)(OEP), where the catalytic turnover number (TON) of the two-electron reduction of O(2) catalyzed by Co(II)(Ch) exceeded 30000. Oxygen 132-136 mitochondrially encoded cytochrome c oxidase II Homo sapiens 13-19 23343346-3 2013 In addition, Co(II)(Ch) is more stable than Co(II)(OEP), where the catalytic turnover number (TON) of the two-electron reduction of O(2) catalyzed by Co(II)(Ch) exceeded 30000. Oxygen 132-136 mitochondrially encoded cytochrome c oxidase II Homo sapiens 44-50 23343346-3 2013 In addition, Co(II)(Ch) is more stable than Co(II)(OEP), where the catalytic turnover number (TON) of the two-electron reduction of O(2) catalyzed by Co(II)(Ch) exceeded 30000. Oxygen 132-136 mitochondrially encoded cytochrome c oxidase II Homo sapiens 51-54 23343346-3 2013 In addition, Co(II)(Ch) is more stable than Co(II)(OEP), where the catalytic turnover number (TON) of the two-electron reduction of O(2) catalyzed by Co(II)(Ch) exceeded 30000. Oxygen 132-136 mitochondrially encoded cytochrome c oxidase II Homo sapiens 44-50 23343346-4 2013 The detailed kinetic studies have revealed that the rate-determining step in the catalytic cycle is the proton-coupled electron transfer reduction of O(2) with the protonated Co(II)(Ch) ([Co(II)(ChH)](+)) that is produced by facile electron-transfer reduction of [Co(III)(ChH)](2+) by ferrocene derivative in the presence of HClO(4). Oxygen 150-154 mitochondrially encoded cytochrome c oxidase II Homo sapiens 175-185 23343346-4 2013 The detailed kinetic studies have revealed that the rate-determining step in the catalytic cycle is the proton-coupled electron transfer reduction of O(2) with the protonated Co(II)(Ch) ([Co(II)(ChH)](+)) that is produced by facile electron-transfer reduction of [Co(III)(ChH)](2+) by ferrocene derivative in the presence of HClO(4). Oxygen 150-154 mitochondrially encoded cytochrome c oxidase II Homo sapiens 175-181 23343346-6 2013 Such a positive shift of [Co(III)(Ch)](+) by protonation resulted in enhancement of the catalytic reactivity of [Co(III)(ChH)](2+) for the two-electron reduction of O(2) with a lower overpotential as compared with that of [Co(III)(OEP)](+). Oxygen 165-169 mitochondrially encoded cytochrome c oxidase II Homo sapiens 231-234 22299646-5 2012 The protonation of Co(II)(Ph(8)Pc) inhibits the direct reduction of O(2); however, the proton-coupled electron transfer from Me(10)Fc to Co(II)(Ph(8)Pc) and the protonated [Co(II)(Ph(8)PcH)](+) occurs to produce Co(I)(Ph(8)PcH) and [Co(I)(Ph(8)PcH(2))](+), respectively, which react immediately with O(2). Oxygen 300-304 mitochondrially encoded cytochrome c oxidase II Homo sapiens 19-25 22301678-9 2012 On the other hand, the latter Co(II) complexes showed a seven-coordinate face-capped octahedron with one amine nitrogen, three pyridyl nitrogens, two pivalamide carbonyl oxygens and MeCN or MeOH. Oxygen 170-177 mitochondrially encoded cytochrome c oxidase II Homo sapiens 30-36 23092306-7 2012 XPS determined binding energies were interpreted to imply that after oxidation in an oxygen/argon mixture of the grafted sample both Pd(II) and Co(II) were oxidized to produce PdO(2) (337.5 eV) and Co(III)(2)O(3) (781.1 eV) which most probably interacts with the silicon surface via Pd(IV)-O-Si and Co(III)-O-Si bonds. Oxygen 85-91 mitochondrially encoded cytochrome c oxidase II Homo sapiens 144-150 22299646-5 2012 The protonation of Co(II)(Ph(8)Pc) inhibits the direct reduction of O(2); however, the proton-coupled electron transfer from Me(10)Fc to Co(II)(Ph(8)Pc) and the protonated [Co(II)(Ph(8)PcH)](+) occurs to produce Co(I)(Ph(8)PcH) and [Co(I)(Ph(8)PcH(2))](+), respectively, which react immediately with O(2). Oxygen 300-304 mitochondrially encoded cytochrome c oxidase II Homo sapiens 137-143 22299646-5 2012 The protonation of Co(II)(Ph(8)Pc) inhibits the direct reduction of O(2); however, the proton-coupled electron transfer from Me(10)Fc to Co(II)(Ph(8)Pc) and the protonated [Co(II)(Ph(8)PcH)](+) occurs to produce Co(I)(Ph(8)PcH) and [Co(I)(Ph(8)PcH(2))](+), respectively, which react immediately with O(2). Oxygen 300-304 mitochondrially encoded cytochrome c oxidase II Homo sapiens 137-143 22299646-6 2012 The rate-determining step is a proton-coupled electron-transfer reduction of O(2) by Co(II)(Ph(8)Pc) in the Co(II)(Ph(8)Pc)-catalyzed cycle with Me(2)Fc, whereas it is changed to the electron-transfer reduction of [Co(II)(Ph(8)PcH)](+) by Me(10)Fc in the Co(I)(Ph(8)PcH)-catalyzed cycle with Me(10)Fc. Oxygen 77-81 mitochondrially encoded cytochrome c oxidase II Homo sapiens 85-91 22299646-6 2012 The rate-determining step is a proton-coupled electron-transfer reduction of O(2) by Co(II)(Ph(8)Pc) in the Co(II)(Ph(8)Pc)-catalyzed cycle with Me(2)Fc, whereas it is changed to the electron-transfer reduction of [Co(II)(Ph(8)PcH)](+) by Me(10)Fc in the Co(I)(Ph(8)PcH)-catalyzed cycle with Me(10)Fc. Oxygen 77-81 mitochondrially encoded cytochrome c oxidase II Homo sapiens 108-114 22299646-6 2012 The rate-determining step is a proton-coupled electron-transfer reduction of O(2) by Co(II)(Ph(8)Pc) in the Co(II)(Ph(8)Pc)-catalyzed cycle with Me(2)Fc, whereas it is changed to the electron-transfer reduction of [Co(II)(Ph(8)PcH)](+) by Me(10)Fc in the Co(I)(Ph(8)PcH)-catalyzed cycle with Me(10)Fc. Oxygen 77-81 mitochondrially encoded cytochrome c oxidase II Homo sapiens 108-114 22207007-2 2012 The deprotonated tolfenamato ligands are coordinated to Co(II) ion through carboxylato oxygen atoms. Oxygen 87-93 mitochondrially encoded cytochrome c oxidase II Homo sapiens 56-62 22299646-1 2012 Proton-coupled electron-transfer reduction of dioxygen (O(2)) to afford hydrogen peroxide (H(2)O(2)) was investigated by using ferrocene derivatives as reductants and saddle-distorted (alpha-octaphenylphthalocyaninato)cobalt(II) (Co(II)(Ph(8)Pc)) as a catalyst under acidic conditions. Oxygen 46-54 mitochondrially encoded cytochrome c oxidase II Homo sapiens 230-236 22299646-1 2012 Proton-coupled electron-transfer reduction of dioxygen (O(2)) to afford hydrogen peroxide (H(2)O(2)) was investigated by using ferrocene derivatives as reductants and saddle-distorted (alpha-octaphenylphthalocyaninato)cobalt(II) (Co(II)(Ph(8)Pc)) as a catalyst under acidic conditions. Oxygen 56-61 mitochondrially encoded cytochrome c oxidase II Homo sapiens 230-236 22299646-4 2012 The active species to react with O(2) in the catalytic reaction is switched from Co(II)(Ph(8)Pc) to protonated Co(I)(Ph(8)PcH), depending on the reducing ability of ferrocene derivatives employed. Oxygen 33-37 mitochondrially encoded cytochrome c oxidase II Homo sapiens 81-87 22299646-5 2012 The protonation of Co(II)(Ph(8)Pc) inhibits the direct reduction of O(2); however, the proton-coupled electron transfer from Me(10)Fc to Co(II)(Ph(8)Pc) and the protonated [Co(II)(Ph(8)PcH)](+) occurs to produce Co(I)(Ph(8)PcH) and [Co(I)(Ph(8)PcH(2))](+), respectively, which react immediately with O(2). Oxygen 68-72 mitochondrially encoded cytochrome c oxidase II Homo sapiens 19-25 22299646-5 2012 The protonation of Co(II)(Ph(8)Pc) inhibits the direct reduction of O(2); however, the proton-coupled electron transfer from Me(10)Fc to Co(II)(Ph(8)Pc) and the protonated [Co(II)(Ph(8)PcH)](+) occurs to produce Co(I)(Ph(8)PcH) and [Co(I)(Ph(8)PcH(2))](+), respectively, which react immediately with O(2). Oxygen 68-72 mitochondrially encoded cytochrome c oxidase II Homo sapiens 137-143 22299646-5 2012 The protonation of Co(II)(Ph(8)Pc) inhibits the direct reduction of O(2); however, the proton-coupled electron transfer from Me(10)Fc to Co(II)(Ph(8)Pc) and the protonated [Co(II)(Ph(8)PcH)](+) occurs to produce Co(I)(Ph(8)PcH) and [Co(I)(Ph(8)PcH(2))](+), respectively, which react immediately with O(2). Oxygen 68-72 mitochondrially encoded cytochrome c oxidase II Homo sapiens 137-143 22070750-5 2011 The abundant oxygen-containing functional groups on the surfaces of graphene oxide nanosheets played an important role on Cd(II) and Co(II) sorption. Oxygen 13-19 mitochondrially encoded cytochrome c oxidase II Homo sapiens 133-139 22178666-2 2012 The deprotonated naproxen acts as monodentate ligand coordinated to Co(II) ion through a carboxylato oxygen. Oxygen 101-107 mitochondrially encoded cytochrome c oxidase II Homo sapiens 68-74 21180730-0 2011 Catalytic dioxygen activation by Co(II) complexes employing a coordinatively versatile ligand scaffold. Oxygen 10-18 mitochondrially encoded cytochrome c oxidase II Homo sapiens 33-39 21890358-3 2011 Molecular modeling studies for 9f showed that the SO(2)NH(2) group assumes a position within the secondary pocket of the COX-2 active site wherein the SO(2)NH(2) oxygen atom is hydrogen bonded to the H90 residue (2.90A), the SO(2)NH(2) nitrogen atom forms a hydrogen bond with L352 (N O=2.80A), and the acetyl group is positioned in the vicinity of the S530 residue where the acetyl oxygen atom undergoes hydrogen bonding to L531 (2.99A). Oxygen 162-168 mitochondrially encoded cytochrome c oxidase II Homo sapiens 121-126 21890358-3 2011 Molecular modeling studies for 9f showed that the SO(2)NH(2) group assumes a position within the secondary pocket of the COX-2 active site wherein the SO(2)NH(2) oxygen atom is hydrogen bonded to the H90 residue (2.90A), the SO(2)NH(2) nitrogen atom forms a hydrogen bond with L352 (N O=2.80A), and the acetyl group is positioned in the vicinity of the S530 residue where the acetyl oxygen atom undergoes hydrogen bonding to L531 (2.99A). Oxygen 383-389 mitochondrially encoded cytochrome c oxidase II Homo sapiens 121-126 21833390-3 2011 Compound 2 having a I4(1)/a space group exhibits a tetranuclear Co(II) cluster with a cubane topology in which the central Co(II) ion and oxygen atoms from bm occupy the alternate vertices of the cube. Oxygen 138-144 mitochondrially encoded cytochrome c oxidase II Homo sapiens 64-70 20372735-2 2010 The experimental data suggest that mefenamic acid acts as deprotonated monodentate ligand coordinated to Co(II) ion through a carboxylato oxygen. Oxygen 138-144 mitochondrially encoded cytochrome c oxidase II Homo sapiens 105-111 21082809-6 2010 The magnetic susceptibility and solid-state/frozen solution EPR data on 1 support the presence of a high-spin octahedral Co(II) in an oxygen environment, having a ground state with an effective spin of S = 1/2. Oxygen 134-140 mitochondrially encoded cytochrome c oxidase II Homo sapiens 121-127 20657942-2 2010 The central Co(II) ion, of each trinuclear entity, exhibits a distorted octahedral geometry, with two ligand molecules coordinating through their carbonyl oxygen atoms along with two bridging Cl(-) ions and two pyridine N atoms from the neighboring molecules. Oxygen 155-161 mitochondrially encoded cytochrome c oxidase II Homo sapiens 12-18 20804197-3 2010 Molecular modeling studies showed that the methylsulfone group of these compounds was inserted deep in the pocket of the human COX-2 binding site, in an orientation that precludes hydrogen bonding with Arg120, Ser353, and Tyr355 through their oxygen atoms. Oxygen 243-249 mitochondrially encoded cytochrome c oxidase II Homo sapiens 127-132 19658385-8 2009 The octahedral sites of Co(II) are occupied by oxygens, thereby reflecting the nature of interactions between the divalent metal ion and quinic acid. Oxygen 47-54 mitochondrially encoded cytochrome c oxidase II Homo sapiens 24-30 20023878-0 2009 Kinetics and mechanism of the Co(II)-assisted oxidation of L-ascorbic acid by dioxygen and nitrite in aqueous solution. Oxygen 78-86 mitochondrially encoded cytochrome c oxidase II Homo sapiens 30-35 19658385-9 2009 The magnetic and EPR data on 1 and 3 support the presence of a high-spin octahedral Co(II) in an oxygen environment, having a ground state with an effective spin of S = 1/2. Oxygen 97-103 mitochondrially encoded cytochrome c oxidase II Homo sapiens 84-90 19014992-7 2009 By utilizing both antioxidants or specific COX inhibitors, it was shown that COX-2 upregulation was dependent on ROS, specifically, O2(-). Oxygen 132-134 mitochondrially encoded cytochrome c oxidase II Homo sapiens 77-82 19128155-5 2009 The two terminal Co(II) ions contain a facial coordination environment (3N, 3O) comprising three imino nitrogen atoms and three phenolate oxygen atoms. Oxygen 138-144 mitochondrially encoded cytochrome c oxidase II Homo sapiens 17-23 18854902-6 2008 The results indicate that Co(II) binds O2 in the presence of GGH, and leads to the formation of a DMPO-HO adduct without first forming free superoxide or hydroxyl radical, supporting the participation of a reactive high-valent cobalt complex. Oxygen 39-41 mitochondrially encoded cytochrome c oxidase II Homo sapiens 26-32 18534903-8 2008 The IR spectra of the starting CoII complexes indicate that both L1 and L3 behave in bidentate manner coordinating via the carbonyl oxygen and NH2 groups, but L2 behaves as a tridentate fashion coordinating via the carbonyl oxygen, azomethine (C=N2) and SH groups with displacement of a hydrogen atom from the latter group. Oxygen 132-138 mitochondrially encoded cytochrome c oxidase II Homo sapiens 31-35 18534903-8 2008 The IR spectra of the starting CoII complexes indicate that both L1 and L3 behave in bidentate manner coordinating via the carbonyl oxygen and NH2 groups, but L2 behaves as a tridentate fashion coordinating via the carbonyl oxygen, azomethine (C=N2) and SH groups with displacement of a hydrogen atom from the latter group. Oxygen 224-230 mitochondrially encoded cytochrome c oxidase II Homo sapiens 31-35 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. Oxygen 174-180 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-74 18808197-3 2008 The complexes of Fe(II) and Co(II) with phthalocyanines are extremely good catalysts of oxidation of organic compounds with molecular oxygen and hydrogen peroxide. Oxygen 134-140 mitochondrially encoded cytochrome c oxidase II Homo sapiens 28-34 18808197-10 2008 It was determined that oxidation of DNA by molecular oxygen catalyzed by complex of Fe(II)-phthalocyanines proceeds with higher rate than in the case of Co(II)-phthalocyanines but the latter led to a greater extent of target DNA modification. Oxygen 53-59 mitochondrially encoded cytochrome c oxidase II Homo sapiens 153-159 17564434-1 2007 The properties of Cu(II) and Co(II) complexes with oxygen- or nitrogen-containing macrocycles have been extensively studied; however, less attention has been paid to the study of complexes containing sulfur atoms in the first coordination sphere. Oxygen 51-57 mitochondrially encoded cytochrome c oxidase II Homo sapiens 29-35 18441204-8 2008 The HNP-induced COX-2 and ET-1 production was attenuated by the treatment with the oxygen free radical scavenger N-acetyl-L-cysteine and the inhibitors of p38 MAPK and NF-kappaB, respectively. Oxygen 83-89 mitochondrially encoded cytochrome c oxidase II Homo sapiens 16-21 18225859-2 2008 The Co(II) ion in the title compound is octahedrally coordinated by six phosphonate oxygen atoms from four carboxylate phosphonate ligands. Oxygen 84-90 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 16634581-13 2006 The coordination environment around the bridging Co(II) ion contains four oxygen (two P-O units, one chelating nitrate) and two nitrogen atoms (pyridyloxy nitrogens). Oxygen 74-80 mitochondrially encoded cytochrome c oxidase II Homo sapiens 49-55 17410782-12 2007 In contrast to samples prepared in air, XAS experiments with samples prepared in the absence of oxygen revealed solely the presence of Co(II). Oxygen 96-102 mitochondrially encoded cytochrome c oxidase II Homo sapiens 135-141 17117223-3 2006 Roughened EPG electrodes coated with the Co(II)/Pt(II) bimetallic porphyrin show a catalytic shift of 500 mV for the reduction of O2 when compared to the reduction of O2 at a bare EPG electrode. Oxygen 130-132 mitochondrially encoded cytochrome c oxidase II Homo sapiens 41-47 17117223-3 2006 Roughened EPG electrodes coated with the Co(II)/Pt(II) bimetallic porphyrin show a catalytic shift of 500 mV for the reduction of O2 when compared to the reduction of O2 at a bare EPG electrode. Oxygen 167-169 mitochondrially encoded cytochrome c oxidase II Homo sapiens 41-47 17117223-5 2006 100 mV is observed for O2 reduction at an EPG electrode coated with the Co(II)/Pt(II) porphyrin which has been oxidized in 1.0 M HClO4. Oxygen 23-25 mitochondrially encoded cytochrome c oxidase II Homo sapiens 72-78 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. Oxygen 70-72 mitochondrially encoded cytochrome c oxidase II Homo sapiens 97-103 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. Oxygen 43-49 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. Oxygen 43-49 mitochondrially encoded cytochrome c oxidase II Homo sapiens 6-11 15996511-4 2006 In the light of these results, it was suggested that two ligands coordinate to each metal atom by hydroxyl oxygen, imino nitrogen and thiazole ring nitrogen to form high spin octahedral complexes with Cr(III), Co(II), Ni(II) and Cu(II). Oxygen 107-113 mitochondrially encoded cytochrome c oxidase II Homo sapiens 210-216 16553373-4 2006 Here, by using density functional theory calculations, we modeled the reaction route from the reaction components to the high-spin metal-oxide intermediate in the activation of oxygen molecule by 2OG-dependent enzymes for three metal ions Fe(II), Ni(II), and Co(II) in the active site. Oxygen 177-183 mitochondrially encoded cytochrome c oxidase II Homo sapiens 259-265 16435846-0 2006 Phosphonation of arenes with dialkyl phosphites catalyzed by Mn(II)/Co(II)/O2 redox couple. Oxygen 75-77 mitochondrially encoded cytochrome c oxidase II Homo sapiens 68-74 17497004-3 2006 The complexes of Co(II) with phthalocyanines are extremely good catalysts of oxidation of organic compounds with molecular oxygen and hydrogen peroxide. Oxygen 123-129 mitochondrially encoded cytochrome c oxidase II Homo sapiens 17-22 17497012-6 2006 A conjugate of Co(II)-tetracarboxyphthalocyanine with the oligonucleotide was found to modify the DNA target in the presence of O(2) and 2-mercaptoethanol or in the presence of H(2)O(2). Oxygen 128-132 mitochondrially encoded cytochrome c oxidase II Homo sapiens 15-21 11412976-2 2001 The energetic and structural results point to the Ile to Val mutation at residue 523 as the key contributor to COX-2 selectivity; unfavorable steric contact between a sulfonamide oxygen and the delta methyl group of Ile523 destabilizes the complex with COX-1. Oxygen 179-185 mitochondrially encoded cytochrome c oxidase II Homo sapiens 111-116 15657055-5 2005 Single scattering fits of EXAFS data indicate that the metal ions in both native Zn(II)-containing and Co(II)-substituted VanX have the same coordination number and that the metal ions are coordinated by 5 nitrogen/oxygen ligands at approximately 2.0 angstroms. Oxygen 215-221 mitochondrially encoded cytochrome c oxidase II Homo sapiens 103-109 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. Oxygen 124-131 mitochondrially encoded cytochrome c oxidase II Homo sapiens 46-52 15330628-1 2004 In this work, a new method for highly efficient and selective oxidative deprotection of a variety of structurally diverse trimethylsilyl (TMS) and tert-butyldimethylsilyl (TBS) ethers using molecular oxygen in the presence of N-hydroxyphthalimide (NHPI) and various types of Co(II) complexes is reported. Oxygen 200-206 mitochondrially encoded cytochrome c oxidase II Homo sapiens 275-281 15252628-4 2004 DFT studies are also performed to gain an insight into the stabilization of the lower oxidation state of the CoL2(2+/3+) couple in order to understand the different reactivity of the Co(II) complexes towards dioxygen. Oxygen 208-216 mitochondrially encoded cytochrome c oxidase II Homo sapiens 183-189 15252555-1 2004 Dioxygen uptake by their dinuclear Co(II) complexes. Oxygen 0-8 mitochondrially encoded cytochrome c oxidase II Homo sapiens 35-41 15252555-6 2004 Under aerobic conditions the binuclear Co(II) complexes of the ligands L1-L3 are able to bind molecular oxygen, with a bridging coordination of O2 between the two metals. Oxygen 104-110 mitochondrially encoded cytochrome c oxidase II Homo sapiens 39-45 15252555-6 2004 Under aerobic conditions the binuclear Co(II) complexes of the ligands L1-L3 are able to bind molecular oxygen, with a bridging coordination of O2 between the two metals. Oxygen 144-146 mitochondrially encoded cytochrome c oxidase II Homo sapiens 39-45 15356722-2 2004 The oxidation of Ni(II) and Co(II) tetraglycine complexes in borate buffer aqueous solution, by dissolved oxygen, is strongly accelerated by sulfite. Oxygen 106-112 mitochondrially encoded cytochrome c oxidase II Homo sapiens 28-34 12874281-5 2003 In fresh human monocytes exposed to hypoxia (1% O2), there was an increase in COX-2 protein compared with cells in normoxia, and this was attributable to increased transcription and mRNA stability. Oxygen 48-50 mitochondrially encoded cytochrome c oxidase II Homo sapiens 78-83 12759799-3 2003 The proposed derivatization procedure protects Co(II) from oxidation by dissolved oxygen and enables rapid determination of all three metal species within a single run. Oxygen 82-88 mitochondrially encoded cytochrome c oxidase II Homo sapiens 47-53 18968885-4 2003 The utility is here applied to the determination, by UV-Vis spectroscopy, of the stability constant for the uptake of molecular dioxygen by the 1:2 complex of Co(II) with N,N"-dimethylethylenediamine (dmen) in the aprotic solvent dimethylsulfoxide (dmso) at 298 K and in a medium adjusted to 0.1 mol dm(-3) with Et(4)NClO(4). Oxygen 128-136 mitochondrially encoded cytochrome c oxidase II Homo sapiens 159-164 12209459-1 2002 The generation of singlet molecular oxygen ((1)O(2)) and hydroxyl radicals (HO*) during peroxidation of bopindolol in the presence of Co(II) ions was studied using electron spin resonance (ESR) and spectrophotometry methods. Oxygen 18-42 mitochondrially encoded cytochrome c oxidase II Homo sapiens 134-140 12079454-8 2002 In it, there exist mononuclear octahedral sites of Co(II) surrounded by oxygens, belonging to terminal phosphonates and bound water molecules. Oxygen 72-79 mitochondrially encoded cytochrome c oxidase II Homo sapiens 51-57 12079454-11 2002 The magnetic and EPR data on 1 support the presence of a high-spin octahedral Co(II) in an oxygen environment, having a ground state with an effective spin S = (1)/(2). Oxygen 91-97 mitochondrially encoded cytochrome c oxidase II Homo sapiens 78-84 15739015-0 2005 Kinetics and mechanism of the Co(II)-assisted oxidation of thioureas by dioxygen. Oxygen 72-80 mitochondrially encoded cytochrome c oxidase II Homo sapiens 30-35 15514750-0 2004 Synthesis and magnetism of oxygen-bridged tetranuclear defect dicubane Co(II) and Ni(II) clusters. Oxygen 27-33 mitochondrially encoded cytochrome c oxidase II Homo sapiens 71-77 15356722-7 2004 In both Ni(II) and Co(II) complexes the metal ion oxidation in the presence of oxygen and sulfite involves the reduction of some initial Ni(III) or Co(III) by sulfite to produce the SO(3).- radical, which rapidly reacts with dissolved oxygen to produce SO(5).-, which then oxidizes Ni(II) or Co(II). Oxygen 79-85 mitochondrially encoded cytochrome c oxidase II Homo sapiens 19-25 15356722-7 2004 In both Ni(II) and Co(II) complexes the metal ion oxidation in the presence of oxygen and sulfite involves the reduction of some initial Ni(III) or Co(III) by sulfite to produce the SO(3).- radical, which rapidly reacts with dissolved oxygen to produce SO(5).-, which then oxidizes Ni(II) or Co(II). Oxygen 79-85 mitochondrially encoded cytochrome c oxidase II Homo sapiens 292-298 15356722-7 2004 In both Ni(II) and Co(II) complexes the metal ion oxidation in the presence of oxygen and sulfite involves the reduction of some initial Ni(III) or Co(III) by sulfite to produce the SO(3).- radical, which rapidly reacts with dissolved oxygen to produce SO(5).-, which then oxidizes Ni(II) or Co(II). Oxygen 235-241 mitochondrially encoded cytochrome c oxidase II Homo sapiens 19-25 12968887-1 2003 Co(II)-catalyzed peroxidation of dienes including (S)-limonene in the presence of molecular oxygen and triethylsilane provided in each case the corresponding 2,3-dioxabicyclo[3.3.1]nonane derivatives via the intramolecular cyclization of the unsaturated peroxy radical intermediates. Oxygen 92-98 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-6 12868935-0 2003 Addition of carboxyalkyl radicals to alkenes through a catalytic process, using a Mn(II)/Co(II)/O2 redox system. Oxygen 96-98 mitochondrially encoded cytochrome c oxidase II Homo sapiens 89-95 12868935-1 2003 A novel strategy for production of mono- and dicarboxylic acids by the addition of carboxyalkyl radicals to alkenes and dienes, respectively, was successfully developed through a catalytic process with use of Mn(II)/Co(II)/O(2) system. Oxygen 223-227 mitochondrially encoded cytochrome c oxidase II Homo sapiens 216-222 12379927-8 2002 4MeOH, where Co(II) ion is in an octahedral environment of oxygen atoms. Oxygen 59-65 mitochondrially encoded cytochrome c oxidase II Homo sapiens 13-19 11677234-2 2002 Prostaglandin synthesis by cyclooxygenases-1 and -2 (COX-1 and COX-2) involves an initial oxygenation of arachidonic acid at C-11, followed by endoperoxide and cyclopentane ring formation, and then a second reaction with molecular oxygen in the S configuration at C-15. Oxygen 32-38 mitochondrially encoded cytochrome c oxidase II Homo sapiens 63-68 11842416-5 2002 In addition, the chelated species in the 2 : 1 Co(II)/Carnos system is found to bind oxygen to a lesser degree. Oxygen 85-91 mitochondrially encoded cytochrome c oxidase II Homo sapiens 47-53 11842416-6 2002 With respect to the coordination sites, each Co(II) ion of the binuclear dioxygenated complexes is bound to one oxygen atom and four nitrogen atoms: N(pi) and N(tau) of two Carnos molecules, the peptide, and the terminal amino nitrogen atoms. Oxygen 75-81 mitochondrially encoded cytochrome c oxidase II Homo sapiens 45-51 11686499-4 2001 Since COII carries a binding site for cytochrome c in the respiratory chain, and since it is required for the passage of chain electrons to molecular oxygen, driving the production of ATP, we hypothesized that metabolic dysfunction resulting from TBI alters COII gene expression directly, perhaps influencing the synaptic plasticity that occurs during postinjury recovery processes. Oxygen 150-156 mitochondrially encoded cytochrome c oxidase II Homo sapiens 6-10 10766441-10 2000 Co(II) and Cd(II) complexes of non-native F1-CS peptides are more sensitive to oxidation by O2, relative to F1-SC, suggestive of a higher lability in the non-native chelate. Oxygen 92-94 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-6 21336918-2 2001 After activation of cellular phospholipases and release of free arachidonic acid, catalyzed insertion of oxygen occurs enzymatically via action of one of the two known cyclooxygenase isoenzymes (COX-1 and COX-2). Oxygen 105-111 mitochondrially encoded cytochrome c oxidase II Homo sapiens 205-210 10767759-6 2000 Also, certain Co(II) and Fe(II) ion pair complexes undergo oxidation reactions in which species such as dioxygen and nitric oxide from the counterions ClO4- and NO3- are transferred to the Co(II) and Fe(II) complexes, showing the inherent affinity of these metals for these molecules. Oxygen 104-112 mitochondrially encoded cytochrome c oxidase II Homo sapiens 14-20 10767759-6 2000 Also, certain Co(II) and Fe(II) ion pair complexes undergo oxidation reactions in which species such as dioxygen and nitric oxide from the counterions ClO4- and NO3- are transferred to the Co(II) and Fe(II) complexes, showing the inherent affinity of these metals for these molecules. Oxygen 104-112 mitochondrially encoded cytochrome c oxidase II Homo sapiens 189-195 10576684-1 1999 By inserting an oxygen link between the 3-fluorophenyl and the lactone ring of 5,5-dimethyl-3-(3fluorophenyl)-4-(4-methanesulfonylphenyl)-2 (5H)-furanone 1 (DFU), analogs with enhanced in vitro COX-2 inhibitory potency as well as in vivo potency in models of inflammation were obtained. Oxygen 16-22 mitochondrially encoded cytochrome c oxidase II Homo sapiens 194-199 11669965-5 1997 With trace amounts of oxygen, the reaction of Co(II)(TPP) with hydroxylamine led to the formation of a stable cobalt(III)-bis(hydroxylamine) complex. Oxygen 22-28 mitochondrially encoded cytochrome c oxidase II Homo sapiens 46-52 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. Oxygen 207-214 mitochondrially encoded cytochrome c oxidase II Homo sapiens 95-101 9893946-8 1998 These results suggest that the expression of mitochondrial encoded subunits (CO-I, CO-II and F0F1-ATPase 6) is up-regulated in response to oxygen and NO reactive species. Oxygen 139-145 mitochondrially encoded cytochrome c oxidase II Homo sapiens 83-88 9720310-6 1998 UV and O2 consumption measurements showed that the reaction of Co with water consumed molecular oxygen and generated Co(II). Oxygen 7-9 mitochondrially encoded cytochrome c oxidase II Homo sapiens 117-123 9622066-2 1998 Recent observations suggest that reactive oxygen intermediates play a role in tumor cell growth regulation and expression of the inducible COX, COX-2. Oxygen 42-48 mitochondrially encoded cytochrome c oxidase II Homo sapiens 144-149 9524553-8 1998 This reaction is not inhibited by O2, indicating that reoxidation of the Co(II) intermediate by O2 is not rapid enough to compete with ligand dissociation. Oxygen 96-98 mitochondrially encoded cytochrome c oxidase II Homo sapiens 73-79 1416035-3 1992 For such sensors, potentiometric oxygen response is attributed to a mixed potential originating from the underlying platinum electrode surface as well as a change in redox potential of the Co(II)-tetren-doped film as the complex binds oxygen reversibly. Oxygen 33-39 mitochondrially encoded cytochrome c oxidase II Homo sapiens 189-195 11669790-3 1997 The active species in oxygen uptake is the CoL(2) complex already suggested in the Co(II)-histamine-O(2) system; however, in the case of pseudopeptides, both CoLH(-)(1) and CoL(2)H(-)(1) complexes can take up oxygen. Oxygen 22-28 mitochondrially encoded cytochrome c oxidase II Homo sapiens 83-88 11669790-3 1997 The active species in oxygen uptake is the CoL(2) complex already suggested in the Co(II)-histamine-O(2) system; however, in the case of pseudopeptides, both CoLH(-)(1) and CoL(2)H(-)(1) complexes can take up oxygen. Oxygen 209-215 mitochondrially encoded cytochrome c oxidase II Homo sapiens 83-88 11667375-7 1996 A key intermediate in this oxidation is believed to be the phthalimide N-oxyl radical generated from NHPI and molecular oxygen using a Co(II) species. Oxygen 120-126 mitochondrially encoded cytochrome c oxidase II Homo sapiens 135-141 8995407-9 1997 The close similarity of the Co(II)-R6-pentafluorophenolate and Co(II)-R6-phenolate spectra demonstrates that the Co(II)-carbonic anhydrase-like spectral profile is preserved despite a substantial perturbation in the electron withdrawing nature of the coordinated phenolate oxygen atom. Oxygen 273-279 mitochondrially encoded cytochrome c oxidase II Homo sapiens 28-34 8995407-9 1997 The close similarity of the Co(II)-R6-pentafluorophenolate and Co(II)-R6-phenolate spectra demonstrates that the Co(II)-carbonic anhydrase-like spectral profile is preserved despite a substantial perturbation in the electron withdrawing nature of the coordinated phenolate oxygen atom. Oxygen 273-279 mitochondrially encoded cytochrome c oxidase II Homo sapiens 63-69 8995407-9 1997 The close similarity of the Co(II)-R6-pentafluorophenolate and Co(II)-R6-phenolate spectra demonstrates that the Co(II)-carbonic anhydrase-like spectral profile is preserved despite a substantial perturbation in the electron withdrawing nature of the coordinated phenolate oxygen atom. Oxygen 273-279 mitochondrially encoded cytochrome c oxidase II Homo sapiens 63-69 7832763-5 1995 of 1500 nmol of O2/nmol of enzyme, whereas hCOX-2 had a specific activity of 12.2 mumol of O2/mg with a Km of 8.7 microM for arachidonate and a Vmax. Oxygen 91-93 mitochondrially encoded cytochrome c oxidase II Homo sapiens 43-49 1416035-3 1992 For such sensors, potentiometric oxygen response is attributed to a mixed potential originating from the underlying platinum electrode surface as well as a change in redox potential of the Co(II)-tetren-doped film as the complex binds oxygen reversibly. Oxygen 235-241 mitochondrially encoded cytochrome c oxidase II Homo sapiens 189-195 34419911-5 2021 The synergistic effect between ROS and RCS promoted by the enhanced oxygen vacancies and the efficient redox recycling of FeIII/FeII and CoIII/CoII. Oxygen 68-74 mitochondrially encoded cytochrome c oxidase II Homo sapiens 143-147 1370470-0 1992 Reaction of Co(II)bleomycin with dioxygen. Oxygen 33-41 mitochondrially encoded cytochrome c oxidase II Homo sapiens 12-17 1370470-1 1992 The reaction of Co(II)bleomycin with dioxygen has been investigated. Oxygen 37-45 mitochondrially encoded cytochrome c oxidase II Homo sapiens 16-21 1370470-2 1992 Dioxygen binds to the Co(II) complex within the time of mixing according to electron spin resonance and uv-visible spectroscopy and dioxygen analysis. Oxygen 0-8 mitochondrially encoded cytochrome c oxidase II Homo sapiens 22-28 1370470-2 1992 Dioxygen binds to the Co(II) complex within the time of mixing according to electron spin resonance and uv-visible spectroscopy and dioxygen analysis. Oxygen 132-140 mitochondrially encoded cytochrome c oxidase II Homo sapiens 22-28 1370470-10 1992 In contrast, hydrogen peroxide is readily detected during the reaction of Co(II)Blm with O2. Oxygen 89-91 mitochondrially encoded cytochrome c oxidase II Homo sapiens 74-79 1316186-1 1992 The electron paramagnetic resonance (EPR) spin trapping technique was used to study the generation of oxygen free radicals from the reaction of hydrogen peroxide with various Co(II) complexes in pH 7.4 phosphate buffer. Oxygen 102-108 mitochondrially encoded cytochrome c oxidase II Homo sapiens 175-181 1316186-9 1992 In the presence of ethylenediamine, Co(II) bound molecular O2 and directly oxidized DMPO to its DMPO/.OH adduct without first forming free superoxide, hydroxyl radical, or hydrogen peroxide. Oxygen 59-61 mitochondrially encoded cytochrome c oxidase II Homo sapiens 36-42 1846358-4 1991 The order of inducing effect on hydrazine-dependent DNA damage (Mn(III) greater than Mn(II) approximately Cu(II) much greater than Co(II) approximately Fe(III)) was related to that of the accelerating effect on the O2 consumption rate of hydrazine autoxidation. Oxygen 215-217 mitochondrially encoded cytochrome c oxidase II Homo sapiens 131-136 35358381-2 2022 Monomeric aromatic tetrapyrroles (such as porphyrins, phthalocyanines, and corroles) coordinated to Co(II) or Co(III) have been considered as oxygen reduction catalysts due to their low cost and relative ease of synthesis. Oxygen 142-148 mitochondrially encoded cytochrome c oxidase II Homo sapiens 100-106 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. Oxygen 161-163 mitochondrially encoded cytochrome c oxidase II Homo sapiens 294-298 34519734-0 2021 Field-induced single-ion magnet based on a quasi-octahedral Co(II) complex with mixed sulfur-oxygen coordination environment. Oxygen 93-99 mitochondrially encoded cytochrome c oxidase II Homo sapiens 60-66 34519734-2 2021 X-ray diffraction studies reveal the first coordination sphere of the Co(II) ion, consisting of two chelating tridentate TDA ligands with a mixed sulfur-oxygen strongly elongated octahedral coordination environment. Oxygen 153-159 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-76 35395537-5 2022 As a highly efficient catalyst for the activation of PS, Co3V2O8/PS system produces radicals of SO4 -, OH, O2- and 1O2 in the reaction process due to the Co(II) and V(IV) exchange electrons with S2O82- and O2. Oxygen 208-210 mitochondrially encoded cytochrome c oxidase II Homo sapiens 156-162 35628301-3 2022 Volumetric (oxygenation) studies were carried out to determine the uptake of molecular oxygen O2 in the formation of the complexes Co(II)-Hpop and Co(II)-Hpoa. Oxygen 87-93 mitochondrially encoded cytochrome c oxidase II Homo sapiens 147-153 35628301-3 2022 Volumetric (oxygenation) studies were carried out to determine the uptake of molecular oxygen O2 in the formation of the complexes Co(II)-Hpop and Co(II)-Hpoa. Oxygen 94-96 mitochondrially encoded cytochrome c oxidase II Homo sapiens 147-153 35358381-4 2022 Herein, we report the initial synthesis and study of a Co(II) tetrapyrrole complex based on a nonaromatic isocorrole scaffold that is competent for 4e-/4H+ oxygen reduction reaction (ORR). Oxygen 156-162 mitochondrially encoded cytochrome c oxidase II Homo sapiens 55-61 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. Oxygen 246-248 mitochondrially encoded cytochrome c oxidase II Homo sapiens 179-185 7309708-3 1981 The various spectral data indicated that the Co(II) center has tetrahedral geometry (high-spin state) and is linked by two nitrogens and two oxygens. Oxygen 141-148 mitochondrially encoded cytochrome c oxidase II Homo sapiens 45-51 35628301-0 2022 Oxygen Binding by Co(II) Complexes with Oxime-Containing Schiff Bases in Solution. Oxygen 0-6 mitochondrially encoded cytochrome c oxidase II Homo sapiens 18-24 34999424-5 2022 Moreover, spectroscopic studies suggested the formation of a transient six-coordinated (CoII(NO)(O2-)) species. Oxygen 97-101 mitochondrially encoded cytochrome c oxidase II Homo sapiens 88-92 32464763-8 2020 It was suspected that O2 - and H2O2 played important roles in the formation of OH and the cycle of Co(II)/Co(III) and Ni(II)/Ni(III). Oxygen 22-26 mitochondrially encoded cytochrome c oxidase II Homo sapiens 100-106 18962166-1 1977 In neutral unbuffered solutions containing dissolved oxygen, the normal pulse polarograms of certain metal ions [Pb(II), Cd(II), Zn(II), Co(II) and Mn(II)] produce peaks on the limiting plateaux. Oxygen 53-59 mitochondrially encoded cytochrome c oxidase II Homo sapiens 137-143 33293086-6 2021 Yield residue analysis indicated that the high porosity and oxygen-containing functional groups of MFHGs remarkably improved their Co(II)- and Ni(II)-removal capacities. Oxygen 60-66 mitochondrially encoded cytochrome c oxidase II Homo sapiens 131-137 32947702-7 2020 Mechanism investigation suggested that the oxygen vacancies, redox cycles of Co(II)/Co(III) and S22-/(S2- and sulfate species) on the surface of 0.2CoAl-LDH@CoSx were crucial for PMS activation. Oxygen 43-49 mitochondrially encoded cytochrome c oxidase II Homo sapiens 77-83 32768854-4 2020 The PFRs enabled an efficient transfer electron to both cobalt atom and O2, facilitating the recycle of Co(III)/Co(II), and thereby leaded to an excellent catalytic performance. Oxygen 72-74 mitochondrially encoded cytochrome c oxidase II Homo sapiens 112-118 33882668-5 2021 This Co(II)-OOSO3- exhibits several intriguing properties including ability to conduct both one-electron-transfer and oxygen-atom-transfer reactions with selected molecules, both nucleophilic and electrophilic in nature, and strongly pH-dependent reactivity. Oxygen 118-124 mitochondrially encoded cytochrome c oxidase II Homo sapiens 5-11 33080102-5 2021 That complex displays a high spin tetrahedral Co II center, which is reactive towards external substrates including dioxygen. Oxygen 116-124 mitochondrially encoded cytochrome c oxidase II Homo sapiens 46-51 32593823-5 2020 Integrating the trapping experiments and electrochemical analysis, we found the oxygen vacancy on B-TiO2-x capturing the electrons to promote the separation of photogenerated charges, meanwhile the Co(II) in the composite decomposed hydrogen peroxide (H2O2) to produce more OH radical. Oxygen 80-86 mitochondrially encoded cytochrome c oxidase II Homo sapiens 198-204 32186188-2 2020 Co(II) or Co(III) can activate PAA to produce acetyloxyl (CH3C(O)O ) and acetylperoxyl (CH3C(O)OO ) radicals with little OH radical formation, and Co(II)/Co(III) is cycled. Oxygen 63-66 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-6 32697905-3 2020 Mechanistic studies suggest that the reaction operates through a radical chain process initiated by Co(II)/O2/phenol and quenched by the cobalt-based catalyst. Oxygen 107-109 mitochondrially encoded cytochrome c oxidase II Homo sapiens 100-106 32633480-0 2020 2D- MOFs with Ni(II), Cu(II) and Co(II) as Efficient Oxygen Evolution Electrocatalysts: Rationalization of Catalytic Performance vs Structure of the MOFs and Potential of the Redox Couples. Oxygen 53-59 mitochondrially encoded cytochrome c oxidase II Homo sapiens 33-39 31794201-1 2019 Utilizing the oxygen-bridged 5,5"-oxidiisophthalic acid (H4L) linker, one Co(II)-based 3D porous MOF {[Co5(L)2(OH)2(OH2)2(H2O)4] 2DMF H2O}n (1) with pentanuclear [Co5(mu3-OH)2(mu2-OH2)2]8+ cluster was prepared. Oxygen 14-20 mitochondrially encoded cytochrome c oxidase II Homo sapiens 74-79 31648572-7 2020 Abbreviations AKT protein kinase B ARMS alveolar rhabdomyosarcoma ATM ataxia telangiectasia mutated Bax Bcl-2-associated X protein Bcl-2 B-cell lymphoma 2 CDC2 cyclin-dependent kinase 2 Bcl-xL B-cell lymphoma-extra large c-FLIP cellular FLICE-like inhibitory protein CDDP cisplatin COX-2 cyclooxygenase-2 cyt c cytochrome c DNA-PKcs DNA-dependent protein kinase EGFR epidermal growth factor receptor EMT epithelial-mesenchymal transition ERK extracellular signal-regulated kinase ES Ewing`s sarcoma ETS2 erythroblastosis virus transcription factor 2 GBM glioblastoma multiforme HCC hepatocellular carcinoma HNSCC head and neck squamous cell carcinoma IAP inhibitor of apoptosis protein IkappaBalpha inhibitor of kappaB alpha IKK inhibitor of kappaB kinase IR ionizing radiation lncRNA long non-coding RNA luc luciferase Mcl-1 myeloid cell leukemia-1 MDR1 multidrug resistance protein 1 miR microRNA MMP-9 matrix metalloproteinase-9 mTOR mammalian target of rapamycin NB neuroblastoma NF-kappaB nuclear factor-kappaB NPC nasopharyngeal carcinoma NSCLC non-small cell lung cancer OSCC oral squamous cell carcinoma PARP poly-(ADP-ribose)-polymerase pH2AX phosphorylated histone 2AX-immunoreactive PI3K phosphatidylinositol 3-kinase Prp4K Pre-mRNA processing factor 4 kinase RCC renal cell carcinoma ROS reactive oxygen species SCC squamous cell carcinoma SLN solid lipid nanoparticle SOD2 superoxide dismutase 2 TERT telomerase reverse transcriptase TNF-alpha tumor necrosis factor-alpha TxnRd1 thioredoxin reductase-1 VEGF vascular endothelial growth factor XIAP X-linked inhibitor of apoptosis protein DeltaPsim mitochondrial membrane potential. Oxygen 293-299 mitochondrially encoded cytochrome c oxidase II Homo sapiens 282-287 32118423-3 2020 The reaction employs commercially available Co(II) catalyst in the presence of Mn(III) cooxidant and oxygen as a terminal oxidant and proceeds with full preservation of original stereochemistry. Oxygen 101-107 mitochondrially encoded cytochrome c oxidase II Homo sapiens 44-50