PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20455576-2 2010 The addition of Cu to reactions with Co(II), Fe(III), or Mn(II) leads to the formation of heterobimetallic UMCM-150 isostructural analogues Co(1)Cu(2)(BHTC)(2) (4), Fe(1)Cu(2)(BHTC)(2) (5), and Mn(1)Cu(2)(BHTC)(2) (6) containing both paddlewheel and trinuclear metal clusters. Metals 98-103 mitochondrially encoded cytochrome c oxidase II Homo sapiens 37-43 20225070-5 2010 UV-vis studies of Co(II) and Fe(III) complexes confirm a metal-binding environment similar to previous di-Co(II)- and di-Fe(III)-DF proteins, including the presence of a mu-oxo-di-Fe(III) unit. Metals 57-62 mitochondrially encoded cytochrome c oxidase II Homo sapiens 18-24 20309972-7 2010 Transition metal (Cd(II), Co(II), and Zn(II)) complexes with L-TBA(x)DA(y) self-assembled into rod-, tubule-, wire-, and platelike superstructures. Metals 11-16 mitochondrially encoded cytochrome c oxidase II Homo sapiens 26-31 20024194-1 2010 A novel separation mode of isotachophoresis (ITP) was advanced for the study on the continuous moving chelation boundary (MCB) formed with EDTA and two metal ions of Co(II) and Cu(II). Metals 152-157 mitochondrially encoded cytochrome c oxidase II Homo sapiens 166-172 20337489-1 2010 A hexacarboxamide cryptand featuring appended polyether moieties is used as a binucleating ligand for two Co(II) centers, marking the first time cryptands have been used as hexaanionic N donors for metal coordination. Metals 198-203 mitochondrially encoded cytochrome c oxidase II Homo sapiens 106-112 20188945-1 2010 Functionalization of polyanthranilic acid (PAA) a self-doped conducting polymer with Co(II) metal complex has been reported and is used in the development of azidothymidine drug sensor. Metals 92-97 mitochondrially encoded cytochrome c oxidase II Homo sapiens 85-91 20126795-3 2010 By adding Co(ii) and Ni(ii) ions in acetonitrile solution, 1 : 1 and 1 : 2 metal : merocyanine complexes are formed simultaneously. Metals 75-80 mitochondrially encoded cytochrome c oxidase II Homo sapiens 10-16 20126795-3 2010 By adding Co(ii) and Ni(ii) ions in acetonitrile solution, 1 : 1 and 1 : 2 metal : merocyanine complexes are formed simultaneously. Metals 75-80 mitochondrially encoded cytochrome c oxidase II Homo sapiens 13-15 20391191-2 2010 Metal complexes are [MLX(2)], type where M = Co(II) (5), Cu(II) (6), and X = Cl, and are well characterized by elemental analysis, Fourier transform infrared spectroscopy, (1)H-NMR and electronic spectra. Metals 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 45-51 19798981-4 2009 It was found that heme-iron of myoglobin directly interacted with additional Cu(II), Zn(II) and Co(II), these metal ions could drag iron ion out from heme prosthetic group of myoglobin, and subsequently myoglobin became myoglobin derivatives lacking iron ion. Metals 110-115 mitochondrially encoded cytochrome c oxidase II Homo sapiens 96-102 19505840-12 2009 Ni(II) complex is the most inhibitory metal complex, followed by Cr(III) complex, parent Schiff base then Co(II) complex. Metals 38-43 mitochondrially encoded cytochrome c oxidase II Homo sapiens 106-112 19798981-3 2009 In the present paper, the direct interaction between heme-iron of myoglobin and additional metal ions [Cu (II), Zn (II) and Co( II)] was studied by UV-Vis spectra. Metals 91-96 mitochondrially encoded cytochrome c oxidase II Homo sapiens 124-131 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. Metals 165-170 mitochondrially encoded cytochrome c oxidase II Homo sapiens 55-61 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. Metals 221-226 mitochondrially encoded cytochrome c oxidase II Homo sapiens 55-61 19800127-1 2009 Chromomycin (Chro) forms a 2:1 drug/metal complex through the chelation with Fe(II), Co(II), or Cu(II) ion. Metals 36-41 mitochondrially encoded cytochrome c oxidase II Homo sapiens 85-91 19767234-4 2009 The stoichiometry of the formed complexes was determined by three different methods: Job"s, mole ratio and slope ratio which indicate the formation of 1:2, M:L complexes for Co(II) and Cu(II) and 1:1, Ni(II):L. Beer"s law is valid in the range 0.32-7.04 microg/mL depending on the type of the metal ion. Metals 293-298 mitochondrially encoded cytochrome c oxidase II Homo sapiens 174-197 19581122-1 2009 The coordination compounds of Cr(III), Mn(II) and Co(II) metal ions derived from quinquedentate 2,6-diacetylpyridine derivative have been synthesized and characterized by using the various physicochemical studies like stoichiometric, molar conductivity and magnetic, and spectral techniques like IR, NMR, mass, UV and EPR. Metals 57-62 mitochondrially encoded cytochrome c oxidase II Homo sapiens 50-56 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. Metals 123-128 mitochondrially encoded cytochrome c oxidase II Homo sapiens 24-30 19505840-2 2009 The metal complexes of Cr(III), Mn(II), Fe(II), Fe(III), Co(II), Ni(II), Cu(II) and Zn(II) with the ligand are prepared in good yield from the reaction of the ligand with the corresponding metal salts. Metals 4-9 mitochondrially encoded cytochrome c oxidase II Homo sapiens 57-63 19505840-2 2009 The metal complexes of Cr(III), Mn(II), Fe(II), Fe(III), Co(II), Ni(II), Cu(II) and Zn(II) with the ligand are prepared in good yield from the reaction of the ligand with the corresponding metal salts. Metals 189-194 mitochondrially encoded cytochrome c oxidase II Homo sapiens 57-63 19798981-7 2009 When the ratio of Mb and metal ions is 1 : 10, the interaction intension between the three metal ions and Mb is Co(II), Zn(II) and Cu(II) in turn. Metals 25-30 mitochondrially encoded cytochrome c oxidase II Homo sapiens 112-118 19798981-7 2009 When the ratio of Mb and metal ions is 1 : 10, the interaction intension between the three metal ions and Mb is Co(II), Zn(II) and Cu(II) in turn. Metals 91-96 mitochondrially encoded cytochrome c oxidase II Homo sapiens 112-118 19513479-0 2009 Luminescent sensing and formation of mixed f-d metal ion complexes between a Eu(iii)-cyclen-phen conjugate and Cu(ii), Fe(ii), and Co(ii) in buffered aqueous solution. Metals 47-52 mitochondrially encoded cytochrome c oxidase II Homo sapiens 80-82 19487034-1 2009 Human serum albumin (HSA) is the most abundant protein of blood serum, involved in the transport of metal ions, including Co(II). Metals 100-105 mitochondrially encoded cytochrome c oxidase II Homo sapiens 122-128 19513479-0 2009 Luminescent sensing and formation of mixed f-d metal ion complexes between a Eu(iii)-cyclen-phen conjugate and Cu(ii), Fe(ii), and Co(ii) in buffered aqueous solution. Metals 47-52 mitochondrially encoded cytochrome c oxidase II Homo sapiens 114-116 19513479-0 2009 Luminescent sensing and formation of mixed f-d metal ion complexes between a Eu(iii)-cyclen-phen conjugate and Cu(ii), Fe(ii), and Co(ii) in buffered aqueous solution. Metals 47-52 mitochondrially encoded cytochrome c oxidase II Homo sapiens 131-137 19513479-3 2009 This allowed for the use of as a luminescent sensor for transition metal ions, where the titration with ions such as Cu(ii), Co(ii) and Fe(ii) gave rise to the formation of mixed f-d nuclear complexes, with concomitant changes in the photophysical properties of . Metals 67-72 mitochondrially encoded cytochrome c oxidase II Homo sapiens 120-122 19513479-3 2009 This allowed for the use of as a luminescent sensor for transition metal ions, where the titration with ions such as Cu(ii), Co(ii) and Fe(ii) gave rise to the formation of mixed f-d nuclear complexes, with concomitant changes in the photophysical properties of . Metals 67-72 mitochondrially encoded cytochrome c oxidase II Homo sapiens 125-131 19513479-3 2009 This allowed for the use of as a luminescent sensor for transition metal ions, where the titration with ions such as Cu(ii), Co(ii) and Fe(ii) gave rise to the formation of mixed f-d nuclear complexes, with concomitant changes in the photophysical properties of . Metals 67-72 mitochondrially encoded cytochrome c oxidase II Homo sapiens 128-130 19513479-6 2009 From these changes, we were able to demonstrate the binding stoichiometry and the binding constant for the formation of novel supramolecular complexes between and Cu(ii), Co(ii) and Fe(ii), which showed that either two or three equivalents of complexed to each of these transition metal ions, giving rise to the formation either linear f-d-f or branched f(3)-d based mixed nuclear complexes in solution. Metals 281-286 mitochondrially encoded cytochrome c oxidase II Homo sapiens 166-168 19513479-6 2009 From these changes, we were able to demonstrate the binding stoichiometry and the binding constant for the formation of novel supramolecular complexes between and Cu(ii), Co(ii) and Fe(ii), which showed that either two or three equivalents of complexed to each of these transition metal ions, giving rise to the formation either linear f-d-f or branched f(3)-d based mixed nuclear complexes in solution. Metals 281-286 mitochondrially encoded cytochrome c oxidase II Homo sapiens 171-177 19513479-6 2009 From these changes, we were able to demonstrate the binding stoichiometry and the binding constant for the formation of novel supramolecular complexes between and Cu(ii), Co(ii) and Fe(ii), which showed that either two or three equivalents of complexed to each of these transition metal ions, giving rise to the formation either linear f-d-f or branched f(3)-d based mixed nuclear complexes in solution. Metals 281-286 mitochondrially encoded cytochrome c oxidase II Homo sapiens 174-176 19275264-7 2009 For both catenanes and rotaxanes, removal of the metal ion via reduction under acidic conditions to the more labile Co(II) gave neutral interlocked molecules with well-defined co-conformations stabilized by intercomponent hydrogen bonding. Metals 49-54 mitochondrially encoded cytochrome c oxidase II Homo sapiens 116-122 19368394-2 2009 Here, a Co(II)-mediated dimeric mithramycin (Mith) complex, (Mith)(2)-Co(II), was shown to be resistant to polyamine competition toward the divalent metal ion when compared to the Fe(II)-mediated drug complexes. Metals 149-154 mitochondrially encoded cytochrome c oxidase II Homo sapiens 8-13 19368394-2 2009 Here, a Co(II)-mediated dimeric mithramycin (Mith) complex, (Mith)(2)-Co(II), was shown to be resistant to polyamine competition toward the divalent metal ion when compared to the Fe(II)-mediated drug complexes. Metals 149-154 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-75 19399766-1 2009 Electrospray ionization mass spectrometry (ESI-MS) is used to probe the metal-binding selectivity of a macrocyclic thiacrown ether (C(44)H(32)S(20)) towards Co(II), Ni(II), Cu(II), and Zn(II). Metals 72-77 mitochondrially encoded cytochrome c oxidase II Homo sapiens 157-163 19385618-10 2009 This demetalation reaction was fast for the Co(II)-complexed [3]rotaxane, whereas decomplexation of the Fe(II) equivalent required harsh conditions which were not compatible with the stability of the metal-free rotaxane. Metals 7-12 mitochondrially encoded cytochrome c oxidase II Homo sapiens 44-49 19099070-1 2009 Three Co(II) isomers assembled from D-, or L-, or DL-camphorate together with achiral isonicotinate exhibit a clear relationship between chirality and helicity even though chiral molecules are not in the backbone of the helix: the absolute sense of helix made of achiral components is controlled by chains of metal and enantiopure chiral ligands running perpendicular to helix in two enantiomeric forms. Metals 309-314 mitochondrially encoded cytochrome c oxidase II Homo sapiens 6-12 19064102-1 2009 This work reports the determination of trace Co(II) by adsorptive stripping voltammetry on disposable three-electrode cells with on-chip metal-film electrodes. Metals 137-142 mitochondrially encoded cytochrome c oxidase II Homo sapiens 45-50 18308622-5 2008 The ligand field parameters were calculated for the Co(II) and Ni(II) complexes and the data show that the covalent character of the metal ligand sigma-bond is low. Metals 133-138 mitochondrially encoded cytochrome c oxidase II Homo sapiens 52-58 19024358-3 2008 These task specific ionic liquids have been used for the formation of metal chelates with Cu(II), Ni(II) and Co(II) in aqueous solutions. Metals 70-75 mitochondrially encoded cytochrome c oxidase II Homo sapiens 109-115 18811164-6 2008 The influence of the transition metal is studied by changing Fe (II) for Co (II), Co (III), and Fe (III). Metals 32-37 mitochondrially encoded cytochrome c oxidase II Homo sapiens 73-80 18563879-0 2008 Mechanism of single metal exchange in the reactions of [M4(SPh)10]2- (M = Zn or Fe) with CoX2 (X = Cl or NO3) or FeCl2. Metals 20-25 mitochondrially encoded cytochrome c oxidase II Homo sapiens 89-93 18445468-3 2008 Co(II)-substituted L1 could be prepared by refolding metal-free L1 in the presence of Co(II), and the resulting enzyme contained 1.8 Eq of cobalt, yielded a UV-Vis spectrum consistent with 5-coordinate Co(II), and exhibited a k(cat) of 63 s(-1) and K(m) of 20 microM when using nitrocefin as the substrate. Metals 53-58 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-6 17913572-1 2008 The metal complexes of Cu(II), Ni(II) and Co(II) with Schiff bases of 3-(2-hydroxy-3-ethoxybenzylideneamino)-5-methyl isoxazole [HEBMI] and 3-(2-hydroxy-5-nitrobenzylidene amino)-5-methyl isoxazole [HNBMI] which were obtained by the condensation of 3-amino-5-methyl isoxazole with substituted salicylaldehydes have been synthesized. Metals 4-9 mitochondrially encoded cytochrome c oxidase II Homo sapiens 42-48 18386923-1 2008 The tripodal system [1]3+ forms a 1:1 complex with CoII in which the metal is octahedrally coordinated by three bpy fragments. Metals 69-74 mitochondrially encoded cytochrome c oxidase II Homo sapiens 51-55 18461198-2 2008 The mixed single-carboxylate-aromatic amine ligands bridged metal systems display a new structurally authenticated example of a thick 2D layer, and also indicate homometallic Co(II) clusters with Td-Oh-Td mixed-geometries can result in relatively obvious noncompensation moments, according to different efficient spins of Co(II) at very low temperature, in spite of antiferromagnetic intracluster interactions. Metals 60-65 mitochondrially encoded cytochrome c oxidase II Homo sapiens 175-181 18473059-1 2008 Discrete homo Cu-Cu-Cu and hetero Cu-Pd-Cu or Cu-Co-Cu metal arrays are prepared within an organic-pillared coordination box by inserting M(ii)-azaporphine/porphine cartridges (M = Cu(ii), Pd(ii) or Co(ii)), where the metal arrays show unique spin interactions in ESR: in particular, Deltam(s) = 3 for the Cu-Cu-Cu array. Metals 55-60 mitochondrially encoded cytochrome c oxidase II Homo sapiens 140-142 18473059-1 2008 Discrete homo Cu-Cu-Cu and hetero Cu-Pd-Cu or Cu-Co-Cu metal arrays are prepared within an organic-pillared coordination box by inserting M(ii)-azaporphine/porphine cartridges (M = Cu(ii), Pd(ii) or Co(ii)), where the metal arrays show unique spin interactions in ESR: in particular, Deltam(s) = 3 for the Cu-Cu-Cu array. Metals 55-60 mitochondrially encoded cytochrome c oxidase II Homo sapiens 184-186 18473059-1 2008 Discrete homo Cu-Cu-Cu and hetero Cu-Pd-Cu or Cu-Co-Cu metal arrays are prepared within an organic-pillared coordination box by inserting M(ii)-azaporphine/porphine cartridges (M = Cu(ii), Pd(ii) or Co(ii)), where the metal arrays show unique spin interactions in ESR: in particular, Deltam(s) = 3 for the Cu-Cu-Cu array. Metals 55-60 mitochondrially encoded cytochrome c oxidase II Homo sapiens 184-186 18473059-1 2008 Discrete homo Cu-Cu-Cu and hetero Cu-Pd-Cu or Cu-Co-Cu metal arrays are prepared within an organic-pillared coordination box by inserting M(ii)-azaporphine/porphine cartridges (M = Cu(ii), Pd(ii) or Co(ii)), where the metal arrays show unique spin interactions in ESR: in particular, Deltam(s) = 3 for the Cu-Cu-Cu array. Metals 55-60 mitochondrially encoded cytochrome c oxidase II Homo sapiens 199-205 18461198-2 2008 The mixed single-carboxylate-aromatic amine ligands bridged metal systems display a new structurally authenticated example of a thick 2D layer, and also indicate homometallic Co(II) clusters with Td-Oh-Td mixed-geometries can result in relatively obvious noncompensation moments, according to different efficient spins of Co(II) at very low temperature, in spite of antiferromagnetic intracluster interactions. Metals 60-65 mitochondrially encoded cytochrome c oxidase II Homo sapiens 322-328 17972261-2 2008 Due to the considerable loading amount of the Co(II) complex, another more effective catalyst was pursued by screening (R,R)-salen-transition metal complexes. Metals 142-147 mitochondrially encoded cytochrome c oxidase II Homo sapiens 46-52 18370379-2 2008 Its chelating coordination ability has been demonstrated by the formation of the corresponding transition metal complexes in the presence of M(OAc)2.nH2O (M = Co(II), Ni(II), Cu(II)) and FeCl3.6H2O. Metals 106-111 mitochondrially encoded cytochrome c oxidase II Homo sapiens 159-165 18179273-1 2008 We report on the influence of a series of transition-metal-substituted Wells-Dawson (P2W17MnO62(12-n)-; M = WVI, FeII, CoII, RuII) and Keggin (PW12O40(3-) and PCoW11O39(5-) anions on the oxygen reduction reaction (ORR) at Au, Pd, and Pt. Metals 53-58 mitochondrially encoded cytochrome c oxidase II Homo sapiens 119-123 18097493-11 2008 Cyclic voltammetry experiments in MeCN-CH2Cl2 reveal facile metal-centred reversible-to-quasireversible CoIV-CoIII (or a ligand-centred redox process; 2a), CoIII-CoII (1a, 1b.MeOH, 2a, 2b and 3), CoII-CoI (1a, 1b.MeOH, 2aand 2b), and CoI-Co0 (1a, 1b.MeOH and 2b) redox processes. Metals 60-65 mitochondrially encoded cytochrome c oxidase II Homo sapiens 109-113 18097493-11 2008 Cyclic voltammetry experiments in MeCN-CH2Cl2 reveal facile metal-centred reversible-to-quasireversible CoIV-CoIII (or a ligand-centred redox process; 2a), CoIII-CoII (1a, 1b.MeOH, 2a, 2b and 3), CoII-CoI (1a, 1b.MeOH, 2aand 2b), and CoI-Co0 (1a, 1b.MeOH and 2b) redox processes. Metals 60-65 mitochondrially encoded cytochrome c oxidase II Homo sapiens 156-160 18237116-3 2008 The new ligand comprises two proximate terpyridine-like binding sites and is shown to form discrete [2 x 2]-grid complexes with CoII, MnII, and CuII in a highly selective self-assembly process, even in the presence of excess metal precursor. Metals 225-230 mitochondrially encoded cytochrome c oxidase II Homo sapiens 128-132 17566643-5 2008 The sorption of metal ions onto modified silica gel correlated well with the Langmuir type adsorption isotherm and adsorption capacities were found to be 0.012, 0.014 and 0.018 mmol g(-1) for Cu(II), Ni(II) and Co(II) metal ions, respectively. Metals 16-21 mitochondrially encoded cytochrome c oxidase II Homo sapiens 211-217 19197392-0 2008 Coordination behavior of 3-ethoxycarbonyltetronic acid towards Cu(II) and Co(II) metal ions. Metals 81-86 mitochondrially encoded cytochrome c oxidase II Homo sapiens 74-80 17764174-4 2007 We have found that for the MnII, CoII, CuII, and ZnII complexes, geometry optimizations lead systematically to pentagonal-bipyramidal coordination environments around the metal ions. Metals 171-176 mitochondrially encoded cytochrome c oxidase II Homo sapiens 33-37 17950056-10 2007 The proposed method is tested for the determination of Co(II), Ni(II), Cu(II) and Pd(II) in alloys and water samples spiked with these metal ions. Metals 135-140 mitochondrially encoded cytochrome c oxidase II Homo sapiens 55-61 17030149-4 2007 The electrical conductivity of some ligands and their Co(II), Ni(II) and Cu(II) complexes in the temperature range 293-150K favoured their semiconducting properties where the metal ion forms a bridge to facilitate the flow of the current. Metals 175-180 mitochondrially encoded cytochrome c oxidase II Homo sapiens 54-60 17321788-0 2007 Spectral and thermal studies of solid-phase thermochromism of Co(II) double metal complexes. Metals 76-81 mitochondrially encoded cytochrome c oxidase II Homo sapiens 62-68 17321791-7 2007 Within the studied solids, the most intense and broad metal-to-metal charge transfer bands were found for a series of low spin Co(III) high spin Co(II) hexacyanoferrates(II,III) and with similar features also for ferric ferrocyanide (Prussian blue), assigned to Fe(II)-->Co(III) and Fe(II)-->Fe(III) photo-induced transition, respectively. Metals 54-59 mitochondrially encoded cytochrome c oxidase II Homo sapiens 145-151 17321791-7 2007 Within the studied solids, the most intense and broad metal-to-metal charge transfer bands were found for a series of low spin Co(III) high spin Co(II) hexacyanoferrates(II,III) and with similar features also for ferric ferrocyanide (Prussian blue), assigned to Fe(II)-->Co(III) and Fe(II)-->Fe(III) photo-induced transition, respectively. Metals 63-68 mitochondrially encoded cytochrome c oxidase II Homo sapiens 145-151 17286396-3 2007 From a magnetic point of view, these similar configurations describe a quasilinear, trimeric magnetic model (PTMMC-M(II)-PTMMC), in which the metal [Ni(II) or Co(II)]-radical magnetic-exchange coupling constants have been determined for the first time. Metals 142-147 mitochondrially encoded cytochrome c oxidase II Homo sapiens 159-165 17274600-2 2007 Four metal-binding sites with different specificities have been described in HSA: (i) the N-terminal site provided by Asp1, Ala2, and His3, (ii) the site at the reduced Cys34, (iii) site A, including His67 as a ligand, and (iv) the nonlocalized site B. HSA can bind CoII, and HSA was proposed to be involved in CoII transport. Metals 5-10 mitochondrially encoded cytochrome c oxidase II Homo sapiens 266-270 19071415-2 2007 The metal sorption properties of modified silica were studied towards Pb(II), Cu(II), Ni(II), Co(II) and Cd(II). Metals 4-9 mitochondrially encoded cytochrome c oxidase II Homo sapiens 94-100 17274600-2 2007 Four metal-binding sites with different specificities have been described in HSA: (i) the N-terminal site provided by Asp1, Ala2, and His3, (ii) the site at the reduced Cys34, (iii) site A, including His67 as a ligand, and (iv) the nonlocalized site B. HSA can bind CoII, and HSA was proposed to be involved in CoII transport. Metals 5-10 mitochondrially encoded cytochrome c oxidase II Homo sapiens 311-315 17663446-3 2007 Metal ion-induced self-assembly of 1,4-bis(2,2":6",2""-terpyridin-4"-yl)benzene with Fe(II) or Co(II) results in MEPEs with interesting electrochemical properties. Metals 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 95-101 17140631-5 2007 Putative chelate ring formation is consistent with a relatively negative entropy change in step A, the stronger Co(II) binding step by HA functional groups, and could relate to "non-exchangeable" metal binding by HSs. Metals 196-201 mitochondrially encoded cytochrome c oxidase II Homo sapiens 112-118 17299639-1 2007 The first paramagnetic homo- and hetero-metallic trinuclear complexes with redox active ligands derived from TTF are synthesized, the central metal ion has an octahedral coordination sphere while the outer Co(II) ions are in a distorted bipyramidal surrounding, bearing TTF-ligands, the magnetic properties show antiferromagnetic coupling leading to a magnetic ground state. Metals 40-45 mitochondrially encoded cytochrome c oxidase II Homo sapiens 206-212 16023340-4 2006 Co(II)-sorption kinetics of Mortierella SPS 403 biomass was fast and appreciable quantities of metal [562.5 microM/g] was adsorbed during first 10 min of incubation. Metals 95-100 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-6 17252949-2 2006 The ligands react with Co(II), Ni(II) and Zn(II) metals to yield (1:1) and (1:2) [metal:ligand] complexes. Metals 49-54 mitochondrially encoded cytochrome c oxidase II Homo sapiens 23-29 17723766-4 2006 The sensor can be applied to the quantification of Co(II) with a linear range covering from 1.0 x 10(-7) to 5.0 x 10(-5) M and a detection limit of 5 x 10(-8) M. The experiment results show that the response behavior of 1 to Co(II) is pH-independent in medium condition (pH 4.5-9.5) and show excellent selectivity for Co(II) over transition metal cations except Cu(II). Metals 341-346 mitochondrially encoded cytochrome c oxidase II Homo sapiens 51-57 17723766-4 2006 The sensor can be applied to the quantification of Co(II) with a linear range covering from 1.0 x 10(-7) to 5.0 x 10(-5) M and a detection limit of 5 x 10(-8) M. The experiment results show that the response behavior of 1 to Co(II) is pH-independent in medium condition (pH 4.5-9.5) and show excellent selectivity for Co(II) over transition metal cations except Cu(II). Metals 341-346 mitochondrially encoded cytochrome c oxidase II Homo sapiens 225-231 17723766-4 2006 The sensor can be applied to the quantification of Co(II) with a linear range covering from 1.0 x 10(-7) to 5.0 x 10(-5) M and a detection limit of 5 x 10(-8) M. The experiment results show that the response behavior of 1 to Co(II) is pH-independent in medium condition (pH 4.5-9.5) and show excellent selectivity for Co(II) over transition metal cations except Cu(II). Metals 341-346 mitochondrially encoded cytochrome c oxidase II Homo sapiens 225-231 17017774-2 2006 The intensity of the Co(II) ligand field band at 550 nm decreased (epsilon550 = 140 to 18 M-1 cm-1) when VanX was reacted with substrate, suggesting that the coordination number of the metal increases from 5 to 6 upon substrate binding. Metals 185-190 mitochondrially encoded cytochrome c oxidase II Homo sapiens 21-27 17723397-10 2006 Electron spin resonance (ESR) data indicates that Co(II) metal-ion center of Co-Sal ionophore undergoes oxidation to Co(III). Metals 57-62 mitochondrially encoded cytochrome c oxidase II Homo sapiens 50-56 16633692-1 2006 In this paper, we investigated the reliability of a Car-Parrinello molecular dynamics (CPMD) approach to characterize the binding of Co(II) metal cation to peptide molecules containing cysteine. Metals 140-145 mitochondrially encoded cytochrome c oxidase II Homo sapiens 133-139 16386771-5 2006 Our results show the following: (i) Ni(II), Co(II), V(V), Mn(II), and to a lesser extent As(III) and Cu(II) activated the binding of IRP-1 to IRE after 24 h, while the other metal ions had no effect; (ii) 10 of 12 metal ions induced HIF-1alpha protein but to strikingly different degrees. Metals 174-179 mitochondrially encoded cytochrome c oxidase II Homo sapiens 44-56 16386771-5 2006 Our results show the following: (i) Ni(II), Co(II), V(V), Mn(II), and to a lesser extent As(III) and Cu(II) activated the binding of IRP-1 to IRE after 24 h, while the other metal ions had no effect; (ii) 10 of 12 metal ions induced HIF-1alpha protein but to strikingly different degrees. Metals 214-219 mitochondrially encoded cytochrome c oxidase II Homo sapiens 44-56 16681389-4 2006 Here we demonstrate that histone deacetylase 8 (HDAC8) is catalytically active with a number of divalent metal ions in a 1:1 stoichiometry with the following order of specific activity: Co(II) > Fe(II) > Zn(II) > Ni(II). Metals 105-110 mitochondrially encoded cytochrome c oxidase II Homo sapiens 186-192 16681389-5 2006 The identity of the catalytic metal ion influences both the affinity of the HDAC inhibitor suberoylanilide hydroxamic acid (SAHA) and the Michaelis constant, with Fe(II)- and Co(II)-HDAC8 having K(M) values that are over 5-fold lower than that of Zn(II)-HDAC8. Metals 30-35 mitochondrially encoded cytochrome c oxidase II Homo sapiens 175-187 16633692-7 2006 Overall, our molecular dynamics simulations shed some light on the nature of the Co(II) interaction and reactivity in Co(II)-phytochelatin building block systems related to the biological and environmental activity of the metal, either in the gas or liquid phase. Metals 222-227 mitochondrially encoded cytochrome c oxidase II Homo sapiens 81-87 16633692-7 2006 Overall, our molecular dynamics simulations shed some light on the nature of the Co(II) interaction and reactivity in Co(II)-phytochelatin building block systems related to the biological and environmental activity of the metal, either in the gas or liquid phase. Metals 222-227 mitochondrially encoded cytochrome c oxidase II Homo sapiens 118-124 16579630-4 2006 The MCO reactions with Mn(II), Fe(II), Co(II), and Ni(II) occur to lesser extents than with Cu(II), but oxidation is still extensive enough to allow easy identification of the metal-bound residues. Metals 176-181 mitochondrially encoded cytochrome c oxidase II Homo sapiens 39-44 16602786-5 2006 The same reaction in aqueous solution with a metal/ligand ratio of 1:1 results in the formation of mononuclear complexes, {[M(bpdo)(H2O)5](SO4)(H2O)2} [M = Co(II) (4), Ni(II) (5)], accompanied by the decomposition of the dithionate anions S2O6(2-) to sulfate anions SO4(2-). Metals 45-50 mitochondrially encoded cytochrome c oxidase II Homo sapiens 156-162 16568183-1 2006 The ligating properties of the 24-membered macrocyclic dinucleating hexaazadithiophenolate ligand (L(Me))2- towards the transition metal ions Cr(II), Mn(II), Fe(II), Co(II), Ni(II) and Zn(II) have been examined. Metals 131-136 mitochondrially encoded cytochrome c oxidase II Homo sapiens 166-172 16634581-6 2006 In the dinuclear heterobimetallic derivatives one of the metal ions [Cu(II) or Co(II)] is hexacoordinate and is bound by the cyclophosphazene in a eta5-gem-N5 mode. Metals 25-30 mitochondrially encoded cytochrome c oxidase II Homo sapiens 79-85 16634581-7 2006 The other metal ion in these heterobimetallic derivatives [Co(II) or Zn(II)] is tetracoordinate and is bound in an eta(1)-N(1) fashion. Metals 10-15 mitochondrially encoded cytochrome c oxidase II Homo sapiens 59-65 16552144-6 2006 In contrast, the Co(II)-form selective inhibitor (4) recruits an unexpected third metal ion, forming a trimetallic enzyme-metal-inhibitor complex. Metals 82-87 mitochondrially encoded cytochrome c oxidase II Homo sapiens 17-23 16552144-6 2006 In contrast, the Co(II)-form selective inhibitor (4) recruits an unexpected third metal ion, forming a trimetallic enzyme-metal-inhibitor complex. Metals 106-111 mitochondrially encoded cytochrome c oxidase II Homo sapiens 17-23 15998028-6 2005 The irreversibility displayed by all of the complexes is probably related to an electron-transfer process followed by a rearrangement of the geometry around the metal center for complexes 1 and 3-5 that probably changes from a trigonal bipyramidal (high spin, d7) to octahedral (low spin, d6) as Co(II) is oxidized to Co(III), which is also expected to be accompanied by a spin-state conversion. Metals 161-166 mitochondrially encoded cytochrome c oxidase II Homo sapiens 296-302 16289228-6 2006 Thermodynamic data pairs (DeltaH(A), DeltaS(A)) for metal binding are linearly correlated with previous data for Ca(II), Co(II) and Mg(II) binding by solid HAs. Metals 52-57 mitochondrially encoded cytochrome c oxidase II Homo sapiens 121-127 16529457-1 2006 Metal-organic hybrids of a boronic acid (4-carboxylphenylboronic acid) with Co(II), Mn(II), and Ni(II) salts have been reported for the first time. Metals 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 76-82 15996511-2 2006 Metal complexes of the ligand were prepared from acetate salts of Co(II), Cu(II), Ni(II) and chloride of Cr(III) in dry acetone. Metals 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 66-72 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). Metals 84-89 mitochondrially encoded cytochrome c oxidase II Homo sapiens 210-216 16363839-6 2005 Electronic structure calculations predict a similar ordering of the metal-based beta spin frontier MO for the Mn(II) and Co(II) complexes. Metals 68-73 mitochondrially encoded cytochrome c oxidase II Homo sapiens 121-127 16220162-1 2005 A metal-organic open-framework with an unprecedented (6,3)-helical topology, large channels and mixed ferro- and antiferromagnetic interactions has been synthesized using a three-connecting tricarboxylic polychlorotriphenylmethyl radical and Co(ii) ions. Metals 2-7 mitochondrially encoded cytochrome c oxidase II Homo sapiens 242-248 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. Metals 131-136 mitochondrially encoded cytochrome c oxidase II Homo sapiens 259-265 16112608-5 2005 Novel complexes of Co(II), Ni(II) and Cu(II) with the pyrimidine azodye have been synthesized and characterized on the basis of elemental analyses, molar conductance, magnetic susceptibility measurements, IR, electronic as well as ESR spectral studies The thermal decomposition of the metal complexes is studied by TGA and DTA techniques. Metals 285-290 mitochondrially encoded cytochrome c oxidase II Homo sapiens 19-25 16171367-4 2005 The different response toward Zn(II), Ni(II), and Co(II) metal ions was also investigated and is reported. Metals 57-62 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. Metals 51-56 mitochondrially encoded cytochrome c oxidase II Homo sapiens 88-93 15296324-3 2004 It was found that Co(II) and Ru(III) are the best metal catalysts for the activation of peroxymonosulfate. Metals 50-55 mitochondrially encoded cytochrome c oxidase II Homo sapiens 18-24 15833659-0 2005 Metal ion promoted hydrogels for bovine serum albumin adsorption: Cu(II) and Co(II) chelated poly[(N-vinylimidazole)-maleic acid]. Metals 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 77-83 15674245-5 2005 Two metal centres, modelled as mononuclear copper and dinuclear copper, are located in soluble regions of each pmoB subunit, which resembles cytochrome c oxidase subunit II. Metals 4-9 mitochondrially encoded cytochrome c oxidase II Homo sapiens 141-172 15589231-6 2005 The detection limits of these metal ions were 0.03, 0.4, 0.04, 0.1, 0.15, 0.05, 0.2, and 3.2 microg/kg for Cd(II), Pb(II), Cu(II), Zn(II), Co(II), Ni(II), Cr(VI), and Mo(VI), respectively, with very good accuracy (standard deviation is below 2%). Metals 30-35 mitochondrially encoded cytochrome c oxidase II Homo sapiens 139-145 15651788-1 2005 The regioselectivity of the metal-catalyzed ring opening of unsymmetrical 1,2-dioxines to cis-gamma-hydroxyenones was investigated using two different Co(II) salen complexes. Metals 28-33 mitochondrially encoded cytochrome c oxidase II Homo sapiens 151-157 15627369-1 2005 By utilizing the novel metalloligand l(Cu), [Cu(2,4-pydca)(2)](2)(-) (2,4-pydca(2)(-) = pyridine-2,4-dicarboxylate), which possesses two kinds of coordination groups, selective bond formation with the series of the first-period transition metal ions (Mn(ii), Fe(ii), Co(ii), Cu(ii), and Zn(ii)) has been accomplished. Metals 23-28 mitochondrially encoded cytochrome c oxidase II Homo sapiens 254-256 15627369-1 2005 By utilizing the novel metalloligand l(Cu), [Cu(2,4-pydca)(2)](2)(-) (2,4-pydca(2)(-) = pyridine-2,4-dicarboxylate), which possesses two kinds of coordination groups, selective bond formation with the series of the first-period transition metal ions (Mn(ii), Fe(ii), Co(ii), Cu(ii), and Zn(ii)) has been accomplished. Metals 23-28 mitochondrially encoded cytochrome c oxidase II Homo sapiens 262-264 15627369-1 2005 By utilizing the novel metalloligand l(Cu), [Cu(2,4-pydca)(2)](2)(-) (2,4-pydca(2)(-) = pyridine-2,4-dicarboxylate), which possesses two kinds of coordination groups, selective bond formation with the series of the first-period transition metal ions (Mn(ii), Fe(ii), Co(ii), Cu(ii), and Zn(ii)) has been accomplished. Metals 23-28 mitochondrially encoded cytochrome c oxidase II Homo sapiens 267-273 15627369-1 2005 By utilizing the novel metalloligand l(Cu), [Cu(2,4-pydca)(2)](2)(-) (2,4-pydca(2)(-) = pyridine-2,4-dicarboxylate), which possesses two kinds of coordination groups, selective bond formation with the series of the first-period transition metal ions (Mn(ii), Fe(ii), Co(ii), Cu(ii), and Zn(ii)) has been accomplished. Metals 23-28 mitochondrially encoded cytochrome c oxidase II Homo sapiens 262-264 15627369-1 2005 By utilizing the novel metalloligand l(Cu), [Cu(2,4-pydca)(2)](2)(-) (2,4-pydca(2)(-) = pyridine-2,4-dicarboxylate), which possesses two kinds of coordination groups, selective bond formation with the series of the first-period transition metal ions (Mn(ii), Fe(ii), Co(ii), Cu(ii), and Zn(ii)) has been accomplished. Metals 23-28 mitochondrially encoded cytochrome c oxidase II Homo sapiens 262-264 15794489-3 2005 Maximum metal ion adsorption capacity of these hydrogels was found to be 3.64 mmol/g dry gel for Cu(II) and 1.72 mmol/g dry gel for Co(II) leading to GOx adsorption capacities of 343 and 528 mg enzyme/g dry gel, respectively, as compared to 228 mg for the plain dry PVIm gel. Metals 8-13 mitochondrially encoded cytochrome c oxidase II Homo sapiens 132-138 15522398-0 2004 Ternary complexes metal [Co(II), Ni(II), Cu(II) and Zn(II)]--ortho-iodohippurate (I-hip)--acyclovir. Metals 18-23 mitochondrially encoded cytochrome c oxidase II Homo sapiens 25-31 15476716-0 2004 Metal-ion environment in solid Mn(II), Co(II) and Ni(II) hyaluronates. Metals 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 39-45 15386801-5 2004 In addition to Co(II), other transition metal ions were also tested, and the results showed that the proposed system was highly selective for Co(II). Metals 40-45 mitochondrially encoded cytochrome c oxidase II Homo sapiens 142-148 15236564-6 2004 In the same vein, rate constants for reduction of Co(III) centers to Co(II) were an order of magnitude slower than those for other metal center or phthalocyanine ring reductions because of Franck-Condon restrictions. Metals 131-136 mitochondrially encoded cytochrome c oxidase II Homo sapiens 69-75 15657055-0 2005 A five-coordinate metal center in Co(II)-substituted VanX. Metals 18-23 mitochondrially encoded cytochrome c oxidase II Homo sapiens 34-40 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. Metals 55-60 mitochondrially encoded cytochrome c oxidase II Homo sapiens 103-109 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. Metals 174-179 mitochondrially encoded cytochrome c oxidase II Homo sapiens 103-109 15657055-8 2005 These spectroscopic studies also demonstrate that the metal ion in Co(II)-substituted VanX when complexed with a phosphinate analog of substrate D-Ala-D-Ala is also five-coordinate. Metals 54-59 mitochondrially encoded cytochrome c oxidase II Homo sapiens 67-73 15654764-3 2005 RFQ-EPR spectra of this intermediate demonstrate that the binding of substrate results in a change in the electronic properties of one or both of the Co(II)"s in the enzyme that is consistent with a change in the coordination sphere of this metal ion. Metals 241-246 mitochondrially encoded cytochrome c oxidase II Homo sapiens 150-155 15593132-12 2005 EPR measurements of the complex with one equivalent of CoII show almost no signal at 4 K, which is compatible with an antiferromagnetic spin-coupling of the metal ions in a cluster structure. Metals 157-162 mitochondrially encoded cytochrome c oxidase II Homo sapiens 55-59 15658766-3 2005 We report, herein, the preparation of gel-like metallo-supramolecular polymers prepared from a monomer unit, which consists of a 2,6-bis-(benzimidazolyl)-4-hydroxypyridine unit attached to either end of a polyether chain, mixed with a lanthanoid metal (e.g. La(III), Eu(III)) and a transition metal ion (e.g. Co(II) or Zn(II)). Metals 47-52 mitochondrially encoded cytochrome c oxidase II Homo sapiens 309-315 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. Metals 16-21 mitochondrially encoded cytochrome c oxidase II Homo sapiens 35-41 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). Metals 40-45 mitochondrially encoded cytochrome c oxidase II Homo sapiens 292-298 15214085-4 2004 Whereas the paramagnetic metal cations Cu(II), Fe(II), Ni(II), Co(II), and Mn(II) result in fluorescence quenching, the emission response is not altered by millimolar concentrations of Ca(II) or Mg(II), rendering the sensors selective for Zn(II) among all biologically important metal cations. Metals 25-30 mitochondrially encoded cytochrome c oxidase II Homo sapiens 63-68 15214085-4 2004 Whereas the paramagnetic metal cations Cu(II), Fe(II), Ni(II), Co(II), and Mn(II) result in fluorescence quenching, the emission response is not altered by millimolar concentrations of Ca(II) or Mg(II), rendering the sensors selective for Zn(II) among all biologically important metal cations. Metals 279-284 mitochondrially encoded cytochrome c oxidase II Homo sapiens 63-68 14753813-1 2004 Six new metal-organic coordination networks based on linking unit 2,5-bis(4-pyridyl)-1,3,4-thiadiazole (L(1)) or 2,5-bis(3-pyridyl)-1,3,4-oxadiazole (L(3)) and inorganic Cu(II), Cd(II), and Co(II) salts have been prepared and structurally characterized by single-crystal X-ray analysis. Metals 8-13 mitochondrially encoded cytochrome c oxidase II Homo sapiens 190-196 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). Metals 40-45 mitochondrially encoded cytochrome c oxidase II Homo sapiens 19-25 15074995-2 2004 The kinetics and thermodynamics of these reactions show that the reactivity of these complexes is affected by metal electronic structure and falls into three groups: Mn(II) and Ni(II) complexes are the most reactive, Fe(II) and Co(II) complexes exhibit intermediate reactivity, and Cu(II) and Zn(II) complexes are the least reactive. Metals 110-115 mitochondrially encoded cytochrome c oxidase II Homo sapiens 228-234 14720556-7 2004 The adsorption of Cu(II), Co(II), and Cd(II) on the beads was significantly rapid and reached at equilibrium within 10 min at 25 degrees C. Adsorption isotherms of the metal ions on the beads exhibited Freundlich and/or Langmuir behavior, contrary to gel beads either of alginate or chitosan showing a step-wise shape of adsorption isotherm. Metals 168-173 mitochondrially encoded cytochrome c oxidase II Homo sapiens 26-31 15509014-7 2004 Higher irreversibility of Co(II) and Ni(II) sorption on the biogenic Mn oxides may partly explain higher accumulation of these metal ions in Mn oxide phases in natural environments. Metals 127-132 mitochondrially encoded cytochrome c oxidase II Homo sapiens 26-32 18969204-4 2003 The rate of metal ion uptake i.e. kinetics studies performed under optimum levels showed a time duration of <5 min except for Co(II) which required 20 min, for complete metal ion saturation. Metals 172-177 mitochondrially encoded cytochrome c oxidase II Homo sapiens 129-135 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. Metals 19-24 mitochondrially encoded cytochrome c oxidase II Homo sapiens 36-42 14611204-3 2003 We report, herein, the preparation of gellike metallo-supramolecular polymers prepared from a monomer unit, which consists of a 2,6-bis-(benzimidazolyl)-4-hydroxypyridine unit attached to either end of a polyether chain, mixed with a transition metal ion (e.g., Co(II) or Zn(II)) and a small percentage of a lanthanoid metal (e.g., La(III), Eu(III)). Metals 46-51 mitochondrially encoded cytochrome c oxidase II Homo sapiens 262-268 18969204-3 2003 The developed method showed superior extraction qualities with high metal loading capacities of 71, 85, 182, 130 and 46 mg g(-1) for Ni(II), Cd(II), Pb(II), Cu(II) and Co(II), respectively. Metals 68-73 mitochondrially encoded cytochrome c oxidase II Homo sapiens 168-174 14514319-3 2003 The temperature-dependent electronic and spectral properties of solutions containing the [Co(III)(tpy)(Cat-N-SQ)](+) suggest that this compound undergoes a thermally driven valence tautomeric interconversion to [Co(II)(tpy)(Cat-N-BQ)](+) complex, the metal ion being in high-spin configuration. Metals 251-256 mitochondrially encoded cytochrome c oxidase II Homo sapiens 90-95 14587717-1 2003 Reaction of the bis-bidentate ligand L1, having two bidentate pyrazolyl-pyridine termini, with Co(II) or Zn(II) results in formation of the complexes [M8(L1)12]X16 (X = perchlorate or tetrafluoroborate); [Zn8(L1)2](ClO4)16 has been structurally characterised and is a cube with a metal ion at each corner, a bridging ligand along each edge, and an anion in the central cavity. Metals 280-285 mitochondrially encoded cytochrome c oxidase II Homo sapiens 95-101 12895099-2 2003 The isostructural Co(II) and the Ni(II) complexes show octahedral geometries around the metal ions with the coordination sites occupied by the pyridyl nitrogen atoms and the thioether sulfur atoms of the ligand and cis coordination of the halide ions. Metals 88-93 mitochondrially encoded cytochrome c oxidase II Homo sapiens 18-24 14562919-3 2003 Metal [M = V(III), Cr(III), Mn(II), Fe(III), Ni(II), Cu(II), Zn(II) and Co(II)] diethyldithiocarbamates (DEDTC) were synthesized by the reaction of sodium diethyldithiocarbamate with metal chloride in dichloromethane/water mixture. Metals 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 72-78 14562919-9 2003 The order of percent nitrification inhibition in soil by metal diethyldithiocarbamates was: Zn(II) > Mn(II) > Fe(III) > Cr(III) > V(III) > Co(II) > Ni(II) > Cu(II). Metals 57-62 mitochondrially encoded cytochrome c oxidase II Homo sapiens 154-160 12099873-5 2002 In particular, the electronic charge-transfer and d-d bands of the Co(II)-substituted peptide complexes were used to examine the metal coordination number and geometry. Metals 129-134 mitochondrially encoded cytochrome c oxidase II Homo sapiens 67-72 12885537-3 2003 The maximum ion exchange of metal ions into the zeolite was found to be 120 mg Pb(II), 110 mg Cu(II), and 100 mg Co(II) per gram of zeolite NaY. Metals 28-33 mitochondrially encoded cytochrome c oxidase II Homo sapiens 113-119 12885537-4 2003 It is observed that the exchange capacity of a zeolite varies with the exchanged metal ion and the amount of metal ions exchanged into zeolite decreases in the sequence Pb(II) > Cu(II) > Co(II). Metals 81-86 mitochondrially encoded cytochrome c oxidase II Homo sapiens 193-199 12885537-4 2003 It is observed that the exchange capacity of a zeolite varies with the exchanged metal ion and the amount of metal ions exchanged into zeolite decreases in the sequence Pb(II) > Cu(II) > Co(II). Metals 109-114 mitochondrially encoded cytochrome c oxidase II Homo sapiens 193-199 12705835-6 2003 The electronic absorption spectrum of the Co(II)-substituted LuxS underwent dramatic catalysis-dependent changes, suggesting the direct involvement of the metal ion in catalysis. Metals 155-160 mitochondrially encoded cytochrome c oxidase II Homo sapiens 42-49 12725391-1 2003 In the absence of any special luminescent reagents, a weakly chemiluminescent emission was observed during the decomposition of hydrogen peroxide, catalyzed by transition-metal ions, such as Cu(II) and Co(II), in basic aqueous solution. Metals 171-176 mitochondrially encoded cytochrome c oxidase II Homo sapiens 202-208 12542292-4 2003 The order of the lability of the metal complexes, Co(II) > Ni(II) > Cu(II) < Zn(II), follows the reverse order of the ligand field stabilization energy with the exception of Cu(II); the behavior of Cu(II) is also due to the Jahn-Teller effect, which shortens the equatorial bonds and lengthens the axial bonds of a tetragonally distorted Cu(II)-L6 complex. Metals 33-38 mitochondrially encoded cytochrome c oxidase II Homo sapiens 50-56 12146942-5 2002 In this report, characterization of a set of cysteine substitution mutants of SmtB reveals that SmtB homodimer binds Zn(II) or Co(II) in one of two mutually exclusive metal binding sites, termed alpha3N and alpha5, with very high equilibrium affinities. Metals 167-172 mitochondrially encoded cytochrome c oxidase II Homo sapiens 127-133 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. Metals 134-139 mitochondrially encoded cytochrome c oxidase II Homo sapiens 47-53 12794878-4 2003 CAD of the metal complexes, especially [Co(II) (chalcone-H) 2,2"-bipyridine](+), allowed the most effective differentiation of the isomeric chalcones with several diagnostic fragment ions appearing upon activation of the metal complexes. Metals 11-16 mitochondrially encoded cytochrome c oxidase II Homo sapiens 40-46 12794878-4 2003 CAD of the metal complexes, especially [Co(II) (chalcone-H) 2,2"-bipyridine](+), allowed the most effective differentiation of the isomeric chalcones with several diagnostic fragment ions appearing upon activation of the metal complexes. Metals 221-226 mitochondrially encoded cytochrome c oxidase II Homo sapiens 40-46 12167017-4 2002 The optical absorption spectra of the Co(II) complexes of Ant-F and its derivative proteins suggest that the geometry of the metal center of holo-Ant-F is tetrahedral and that the mutated Cys(2)His(2) residues are involved in the complex formation. Metals 125-130 mitochondrially encoded cytochrome c oxidase II Homo sapiens 38-44 16290410-7 2002 This differential behavior can be effectively used for the decontamination of alkali metal, alkaline earth metal, and ammonium salts from Cu(II), Ni(II), Co(II), and Zn(II) ions via solid phase extraction following AAS measurement. Metals 85-90 mitochondrially encoded cytochrome c oxidase II Homo sapiens 154-159 12079454-0 2002 Synthesis and structural and spectroscopic characterization of a complex between Co(II) and imino-bis(methylphosphonic acid): gaining insight into biologically relevant metal-ion phosphonate interactions or looking at a new Co(II)-organophosphonate material? Metals 169-174 mitochondrially encoded cytochrome c oxidase II Homo sapiens 81-87 12079454-2 2002 As a metal ion, Co(II) assumes forms, which are dictated by the nature of organic binders in biological fluids, and the conditions under which metal ion ligand interactions arise. Metals 5-10 mitochondrially encoded cytochrome c oxidase II Homo sapiens 16-22 12079454-2 2002 As a metal ion, Co(II) assumes forms, which are dictated by the nature of organic binders in biological fluids, and the conditions under which metal ion ligand interactions arise. Metals 143-148 mitochondrially encoded cytochrome c oxidase II Homo sapiens 16-22 12079454-4 2002 As a representative metal ion binder, the organophosphonate ligand H(2)O(3)P-CH(2)-NH(2)(+)-CH(2)-PO(3)H(-) was employed in aqueous reactions with Co(II), ultimately leading to the isolation of complex [Co(C(2)H(8)O(6)NP(2))(2)(H(2)O)(2)] (1) at pH 2. Metals 20-25 mitochondrially encoded cytochrome c oxidase II Homo sapiens 147-153 12148806-4 2002 The kinetics and thermodynamics of acetonitrile addition to the metal complex ions are strongly affected by the chemical environment around the metal center such that significant differences in reactivity are observed for Co(II) and Cu(II) complexes with various coordination spheres. Metals 64-69 mitochondrially encoded cytochrome c oxidase II Homo sapiens 222-228 12148806-4 2002 The kinetics and thermodynamics of acetonitrile addition to the metal complex ions are strongly affected by the chemical environment around the metal center such that significant differences in reactivity are observed for Co(II) and Cu(II) complexes with various coordination spheres. Metals 144-149 mitochondrially encoded cytochrome c oxidase II Homo sapiens 222-228 11929962-3 2002 In contrast, reaction of L(1) and L(2) with Co(II) salts, followed by treatment with tetrafluoroborate or perchlorate, results in assembly of cage complexes having a 4:6 metal:ligand ratio; these complexes have a metal ion at each corner of an approximate tetrahedron, and a bis-bidentate bridging ligand spanning each edge. Metals 170-175 mitochondrially encoded cytochrome c oxidase II Homo sapiens 44-50 11929962-3 2002 In contrast, reaction of L(1) and L(2) with Co(II) salts, followed by treatment with tetrafluoroborate or perchlorate, results in assembly of cage complexes having a 4:6 metal:ligand ratio; these complexes have a metal ion at each corner of an approximate tetrahedron, and a bis-bidentate bridging ligand spanning each edge. Metals 213-218 mitochondrially encoded cytochrome c oxidase II Homo sapiens 44-50 16290410-7 2002 This differential behavior can be effectively used for the decontamination of alkali metal, alkaline earth metal, and ammonium salts from Cu(II), Ni(II), Co(II), and Zn(II) ions via solid phase extraction following AAS measurement. Metals 107-112 mitochondrially encoded cytochrome c oxidase II Homo sapiens 154-159 18476013-2 2002 The title Schiff-base acts as NNS donor tridentate during the complexation reaction with these metal ions having a composition, [M(L)(2)]X(n) where M=Co(II) or Ni(II), L=, X=NO(3) (-), SO(4) (2-), C(2)O(4) (2-) or CH(3)CO(2) (-) and n=1 or 2 and show an octahedral geometry. Metals 95-100 mitochondrially encoded cytochrome c oxidase II Homo sapiens 150-156 11843162-4 2002 The reaction of the pseudorotaxanes with various transition metal ions including CuII, CoII, NiII, AgI, and CdII produces 1D or 2D polyrotaxanes, in which many molecular "beads" are threaded onto 1D or 2D coordination polymers as confirmed by X-ray crystallography. Metals 60-65 mitochondrially encoded cytochrome c oxidase II Homo sapiens 87-91 12164389-2 2001 Here we report the synthesis and inhibition studies against the physiologically relevant isozymes CA I, CA II and CA IV, of a series of metal complexes (Co(II), Ni(II) and Cu(II) derivatives) of a Schiff-base ligand, obtained from sulfanilamide and salicylaldehyde. Metals 136-141 mitochondrially encoded cytochrome c oxidase II Homo sapiens 153-159 10985721-5 2000 In addition, LiR can be used for reaction with a variety of metal complexes (best with NiII, but also with ZnII, CuII, and CoII) and most useful with free base porphyrins. Metals 60-65 mitochondrially encoded cytochrome c oxidase II Homo sapiens 123-127 11817175-0 2001 In vitro study of the interaction between omeprazole and the metal ions Zn(II), Cu(II), and Co(II). Metals 61-66 mitochondrially encoded cytochrome c oxidase II Homo sapiens 92-98 11817175-1 2001 The purpose of this study was to investigate the possibility of a chemical interaction between omeprazole (OM) and the metal ions Zn(II), Cu(II), and Co(II). Metals 119-124 mitochondrially encoded cytochrome c oxidase II Homo sapiens 150-156 11592411-1 2001 Selected metal ions having paramagnetic property were found to exert inhibition effects on aquatic photodegradation of organophosphorus pesticides sensitized by humic acids, according to the increasing order of Cr(III) < Co(II) < Mn(II) < Cu(II). Metals 9-14 mitochondrially encoded cytochrome c oxidase II Homo sapiens 224-230 11324626-4 2001 By using Job"s method of continuous variation, the stoichiometry of the reaction was found to be in the ratio of 1:2, metal:drug, with Cu(II) and Co(II). Metals 118-123 mitochondrially encoded cytochrome c oxidase II Homo sapiens 146-152 11225126-1 2001 Transition-metal-substituted polyoxometalates (TMSP) of the type [MII(H2O)PW11O39]5- (M = Co, Zn) and [SiW9O37(CoII(H2O))3]10- have been chemically anchored to modified macroporous (400 nm pores), mesoporous (2.8 nm pores), and amorphous silica surfaces. Metals 11-16 mitochondrially encoded cytochrome c oxidase II Homo sapiens 111-115 11268132-6 2001 Other transition metal ions, such as NiII, ZnII, CoII and CuII, also show distinctive metal-assisted reactions. Metals 17-22 mitochondrially encoded cytochrome c oxidase II Homo sapiens 49-53 11268132-6 2001 Other transition metal ions, such as NiII, ZnII, CoII and CuII, also show distinctive metal-assisted reactions. Metals 86-91 mitochondrially encoded cytochrome c oxidase II Homo sapiens 49-53 11106490-9 2000 The only other metal ion to cause slight activation of the enzyme was Co(II), with Ca(II), Cu(II), Mg(II), Ni(II), and Zn(II) all being inhibitory. Metals 15-20 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-76 11205498-2 2001 The Co(II) ions were selectively pre-separated on a mercury film electrode (MFE) by on-line reduction, then the accumulated metal was oxidised and selectively stripped back into the flowing solution as Co(II). Metals 124-129 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 11205498-2 2001 The Co(II) ions were selectively pre-separated on a mercury film electrode (MFE) by on-line reduction, then the accumulated metal was oxidised and selectively stripped back into the flowing solution as Co(II). Metals 124-129 mitochondrially encoded cytochrome c oxidase II Homo sapiens 202-208 15819041-1 1999 Direct interaction of Cu2Zn2SOD with inorganic metal compound (CoCl2) and organic metal compound [Co(II)(His)n] was studied by ICP, VIS, NMR and measurement of enzyme activity. Metals 82-87 mitochondrially encoded cytochrome c oxidase II Homo sapiens 98-104 18967999-5 2000 The current was proportional to the concentration of the Co(II) ion in a range of 1x10(-8)-1x10(-6) mol l(-1) for 3 min accumulation and in the range of 1x10(-9)-1x10(-8) mol l(-1) for 5 min accumulation; most of metal ions do not interfere with the determination. Metals 213-218 mitochondrially encoded cytochrome c oxidase II Homo sapiens 57-63 15822301-3 1999 It has found that in aqueous solution, there exists a direct interaction of the metal ions of the active center in the metalloenzyme (Cu2Zn2SOD) with external added Co(His)n. As a result, part of the metal ions in metalloenzyme were replaced and the corresponding metalloenzyme derivatives (Co (II)-substituted derivatives of SOD) were produced and the catalytic activity of enzyme were affected. Metals 80-85 mitochondrially encoded cytochrome c oxidase II Homo sapiens 291-297 15822301-3 1999 It has found that in aqueous solution, there exists a direct interaction of the metal ions of the active center in the metalloenzyme (Cu2Zn2SOD) with external added Co(His)n. As a result, part of the metal ions in metalloenzyme were replaced and the corresponding metalloenzyme derivatives (Co (II)-substituted derivatives of SOD) were produced and the catalytic activity of enzyme were affected. Metals 119-124 mitochondrially encoded cytochrome c oxidase II Homo sapiens 291-297 10858308-8 2000 Both inhibitors perturb the d-d transitions of CoCPD in the 500-600 nm region within milliseconds of mixing but only the CoCPD.D-Cys complex displays a strong S --> Co(II) charge-transfer band at 340 nm indicative of a metal-sulfur bond. Metals 222-227 mitochondrially encoded cytochrome c oxidase II Homo sapiens 168-174 12958939-3 2000 As a result, part of the metal ions in metalloenzyme were replaced and the corresponding metalloenzyme derivatives (Co(II)-substituted derivatives of SOD) were produced and the catalytic activity of enzyme were affected. Metals 25-30 mitochondrially encoded cytochrome c oxidase II Homo sapiens 116-121 11257482-1 2000 We have investigated the chemiluminescence signal of luminol and hydrogen peroxide in the presence of a transition metal (Co(II), Cu(I), Fe(II), Fe(III)) and of a chelator (EDTA, citric acid) in pH 8.5, 9 and 10 borate buffer solutions. Metals 115-120 mitochondrially encoded cytochrome c oxidase II Homo sapiens 122-128 18475936-0 2000 Synthesis, Characterization and Biological Properties of Anions of Bivalent Transition Metal [Co(II) and Ni(II)] Complexes With Acylhydrazine Derived ONO Donor Schiff Bases. Metals 87-92 mitochondrially encoded cytochrome c oxidase II Homo sapiens 94-100 18475936-1 2000 Some acylhydrazine derived ONO donor Schiff bases and their Co(II) and Ni(II) complexes have been prepared having the same metal ion (cation) but different anions. Metals 123-128 mitochondrially encoded cytochrome c oxidase II Homo sapiens 60-66 15819047-1 1999 Three new solid complexes of transition metal Co(II), Ni(II) and Cu(II) with quinoxaline-2,3-dicarboxamide were synthesized, and the composition of the complexes was confirmed to be M(Qxda)2Cl2 [M = Co(II), Ni(II), Cu(II)] by elemental analysis, molar conductance and thermal analysis. Metals 40-45 mitochondrially encoded cytochrome c oxidase II Homo sapiens 46-52 9020770-4 1997 In an effort to understand the origin of the stability of the metal complex, we have employed an anaerobic optical spectroscopic, competitive metal binding assay to determine the coordination geometry and association constants (Ka) for the binding of Co(II) to wild-type gp32 and a series of zinc ligand substitution mutants. Metals 62-67 mitochondrially encoded cytochrome c oxidase II Homo sapiens 251-257 9417062-0 1998 The dynamic properties of the M121H azurin metal site as studied by NMR of the paramagnetic Cu(II) and Co(II) metalloderivatives. Metals 43-48 mitochondrially encoded cytochrome c oxidase II Homo sapiens 103-109 9020770-4 1997 In an effort to understand the origin of the stability of the metal complex, we have employed an anaerobic optical spectroscopic, competitive metal binding assay to determine the coordination geometry and association constants (Ka) for the binding of Co(II) to wild-type gp32 and a series of zinc ligand substitution mutants. Metals 142-147 mitochondrially encoded cytochrome c oxidase II Homo sapiens 251-257 9055202-2 1997 The fluorescence of pyrene-monophosphatase is enhanced upon addition of the activating metal ions Co(II) and Mg(II). Metals 87-92 mitochondrially encoded cytochrome c oxidase II Homo sapiens 98-104 8785352-3 1996 The transition metal cations that effectively bind DNA to mica are Ni(II), Co(II), and Zn(II), which have ionic radii from 0.69 to 0.74 A. Metals 15-20 mitochondrially encoded cytochrome c oxidase II Homo sapiens 75-81 8157637-6 1994 Metal coordination by the mutant proteins was evaluated by atomic absorption spectroscopy, Co(II) electronic spectroscopy, and 113Cd NMR spectroscopy. Metals 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 91-97 10479422-5 1996 The EDTA complexes of the divalent metals Ca, Zn, Ni, Cu, Co(II), and Pb, which are quinquedentate in solution (free donor atoms bound to the metal ion), all showed the same ligand-like adsorption behavior. Metals 35-40 mitochondrially encoded cytochrome c oxidase II Homo sapiens 58-63 18475756-3 1996 Together with the arsonolipids previously investigated, the active compounds of this series - the "lipothioarsenites"- constitute a novel class of CA inhibitors that bind to the metal ion within the enzyme active site, as proved by changes in the electronic spectra of adducts of such inhibitors with Co(II)CA. Metals 178-183 mitochondrially encoded cytochrome c oxidase II Homo sapiens 301-306 18966309-3 1995 The results show that most platinum metal ions, Co(II) and Cu(II) can form ternary mixed ligand complexes with MBTAE and salicylic acid. Metals 36-41 mitochondrially encoded cytochrome c oxidase II Homo sapiens 48-54 7957953-0 1994 A 1H NMR NOE study on Co(II) stellacyanin: some clues about the structure of the metal site. Metals 81-86 mitochondrially encoded cytochrome c oxidase II Homo sapiens 22-28 34075750-5 2021 When NO2 is evacuated, MOF A quickly changes from a conductor back to an insulator in 42 s. In the crystal structure of NO2-adsorbed MOF (termed as A-NO2), NO2 molecule connects Co(II) and uncoordinated carboxylate groups through hydrogen-bonding interactions to form a conductive pathway, greatly reducing the electron transmission distance between each two metal clusters. Metals 359-364 mitochondrially encoded cytochrome c oxidase II Homo sapiens 178-184 7956977-3 1994 The affinity of both metal binding sites for Co(II) is also altered. Metals 21-26 mitochondrially encoded cytochrome c oxidase II Homo sapiens 45-51 8257435-2 1993 Although the native Zn(II)-containing and the Co(II)-reconstituted enzymes have closely similar Michaelis constants and maximal velocities, the kinetics for both the inactivation by OP and the reconstitution of the apoenzyme with the metal ions differs considerably. Metals 234-239 mitochondrially encoded cytochrome c oxidase II Homo sapiens 46-52 8371984-3 1993 We carried out X-ray diffraction analyses of the interactions of the two transition metal ions Co(II) and Cu(II) and an alkaline earth metal ion Ba(II), with DNA of different conformations. Metals 84-89 mitochondrially encoded cytochrome c oxidase II Homo sapiens 95-101 1327111-4 1992 The EPR spectrum of the binuclear Co(II) derivative contains a resonance at g approximately 13, which is characteristic of integer spin systems and indicates coupled metal ions; the excess Co(II) bound to crude products exhibits an EPR signal at g approximately 4. Metals 166-171 mitochondrially encoded cytochrome c oxidase II Homo sapiens 34-40 1327111-6 1992 The intensity of the optical absorption in the visible region due to Co(II) increases with increasing stoichiometry of specifically bound metal [up to 2 Co(II) per protein monomer], but the intensity of the Co(II) EPR signal increases only during the formation of a mononuclear derivative. Metals 138-143 mitochondrially encoded cytochrome c oxidase II Homo sapiens 69-75 33815493-7 2021 The XRD pattern of the metal complexes showed that both Co(II) and Ni(II) have amorphous nature, while Zn(II) complex has monoclinic crystallinity with an average size of 9.10 nm. Metals 23-28 mitochondrially encoded cytochrome c oxidase II Homo sapiens 56-62 10536875-3 1999 Metal complexes of some of these Schiff bases with divalent transition ions such as Zn(II), Cu(II), Co(II) and Ni(II) have also been obtained. Metals 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 100-117 34818808-6 2022 The results show that pyrene biodegradation on montmorillonite was markedly influenced by surface metal ions, with degradation efficiency following the order Fe(III) > Na(I) Co(II) > Ni(II) Cu(II). Metals 98-103 mitochondrially encoded cytochrome c oxidase II Homo sapiens 176-182 34963412-7 2021 The molecular docking was used to predict the efficiency of binding of the metal complexes with COX- 2.Communicated by Ramaswamy H. Sarma. Metals 75-80 mitochondrially encoded cytochrome c oxidase II Homo sapiens 96-102 34641564-0 2021 Crystal Structure and Magnetic Properties of Trinuclear Transition Metal Complexes (MnII, CoII, NiII and CuII) with Bridging Sulfonate-Functionalized 1,2,4-Triazole Derivatives. Metals 67-72 mitochondrially encoded cytochrome c oxidase II Homo sapiens 90-94 34443477-3 2021 Treatment of these disks and domes with metal ions such as Fe(II), Cu(II), Zn(II), Co(II), and Ru(III) triggered the formation of microcages, and micron-sized cup-like structures. Metals 40-45 mitochondrially encoded cytochrome c oxidase II Homo sapiens 83-89 34128639-3 2021 At pH 7.0, other metal ions (i.e., Fe(II), Fe(III), Mn(II), Mn(III), Co(II), Cu(II), and Ni(II)) in 10 mM phosphate could activate PAA to oxidize SMX only up to 20%. Metals 17-22 mitochondrially encoded cytochrome c oxidase II Homo sapiens 69-75 1359966-5 1992 Other divalent metal ions [Zn(II), Co(II), Mn(II), Cu(II) and Ni(II)] also reduced the fluorescence intensity of the human enzyme by 12-30% when added in stoichiometric amounts. Metals 15-20 mitochondrially encoded cytochrome c oxidase II Homo sapiens 35-41 1933852-16 1991 DNA damage in chromatin caused by Ni(II) and Co(II) ions in the presence of H2O2 may contribute to the established genotoxicity and carcinogenicity of these metal ions. Metals 157-162 mitochondrially encoded cytochrome c oxidase II Homo sapiens 45-51 1676967-6 1991 All three isozymes were rapidly activated (13-40-fold) by incubation with Fe(II) salts (concentration of iron at half-maximal activation = 6-14 microM), and were inhibited by other divalent metal ions, e.g. Zn(II), Co(II) and Ni(II). Metals 190-195 mitochondrially encoded cytochrome c oxidase II Homo sapiens 215-221 1848978-2 1991 The order of inducing effect of metal ions on hydralazine-dependent DNA damage [Cu(II) greater than Co(II) greater than Fe(III)] was related to that of accelerating effect on the O2 consumption rate of hydralazine autoxidation. Metals 32-37 mitochondrially encoded cytochrome c oxidase II Homo sapiens 100-106 34741938-3 2022 The experimental results of the batch tests revealed that in single-metal systems, the removal efficiency of Cu(II), Co(II), Cr(VI) and As(III) could reach 98% at equilibrium. Metals 68-73 mitochondrially encoded cytochrome c oxidase II Homo sapiens 117-123 34577066-1 2021 New magnetic metal complexes with organic radical ligands, (M(hfac)2(PyBTM)2) (M = NiII, CoII; hfac = hexafluoroacetylacetonato, PyBTM = (3,5-dichloro-4-pyridyl)bis(2,4,6-trichlorophenyl)methyl radical), were prepared and their crystal structures, magnetic properties, and electronic structures were investigated. Metals 13-18 mitochondrially encoded cytochrome c oxidase II Homo sapiens 89-93 34211959-1 2021 In the search for novel, metal-based drug complexes that may be of value as anticancer agents, five new transition metal complexes of sulfaclozine (SCZ) with Cu(II), Co(II), Ni(II), Zn(II), and Fe(II) were successfully synthesized. Metals 25-30 mitochondrially encoded cytochrome c oxidase II Homo sapiens 166-172 34211959-1 2021 In the search for novel, metal-based drug complexes that may be of value as anticancer agents, five new transition metal complexes of sulfaclozine (SCZ) with Cu(II), Co(II), Ni(II), Zn(II), and Fe(II) were successfully synthesized. Metals 115-120 mitochondrially encoded cytochrome c oxidase II Homo sapiens 166-172 34151097-2 2021 Herein, we report a novel approach for the detection and determination of fluoride ion (F-) sensing based on a salen-cobalt metal-organic framework (Co(II)-MOF). Metals 124-129 mitochondrially encoded cytochrome c oxidase II Homo sapiens 149-155 35401918-6 2022 The new manganese-based SOD mimics display a higher intrinsic SOD activity and also improved kinetic inertness in metal ion exchange processes (with Zn(II), Cu(II), Ni(II), and Co(II)). Metals 114-119 mitochondrially encoded cytochrome c oxidase II Homo sapiens 177-183 35477280-1 2022 A new porous metal-organic framework, (Co (oba) (bpdh)) (DMF) (TMU-63), containing accessible nitrogen-rich diazahexadiene groups was successfully prepared with the solvothermal assembly of 5-bis(4-pyridyl)-3,4-diaza-2,4-hexadiene (4-bpdh), 4,4"-oxybis(benzoic) acid (oba), and Co(II) ions. Metals 13-18 mitochondrially encoded cytochrome c oxidase II Homo sapiens 278-284 35448899-2 2022 In proof-of-concept studies, M-CPOnes based on ZnII, FeII and CoII are stable in the dark but undergo light-triggered CO release with the cyclopropenone substituents and metal ions enabling tuning of the photophysical properties. Metals 170-175 mitochondrially encoded cytochrome c oxidase II Homo sapiens 62-66 35475313-3 2022 Moreover, the characteristic spectrum of Co(II) ion makes it a powerful probe for the characterization of metal-binding proteins through the formation of cobalt-ligand bonds. Metals 106-111 mitochondrially encoded cytochrome c oxidase II Homo sapiens 41-47 35378654-6 2022 The extent of recovery in biomass, when the supply of Co(II) metal ion was discontinued in the inlet stream, was explored. Metals 61-66 mitochondrially encoded cytochrome c oxidase II Homo sapiens 54-60 35230085-4 2022 When the complexed metal ion is Mn(II), Fe(II), Co(II), or Ni(II), both incoherent tunneling and hysteresis are observed for a voltage range between +1.0 V and -1.0 V. When the metal ion is Cr(II) or Cu(II), however, only resonant (one-step) tunneling is observed, and the junctions exhibit no hysteresis and do not enter the incoherent tunneling regime. Metals 19-24 mitochondrially encoded cytochrome c oxidase II Homo sapiens 48-54 35230085-4 2022 When the complexed metal ion is Mn(II), Fe(II), Co(II), or Ni(II), both incoherent tunneling and hysteresis are observed for a voltage range between +1.0 V and -1.0 V. When the metal ion is Cr(II) or Cu(II), however, only resonant (one-step) tunneling is observed, and the junctions exhibit no hysteresis and do not enter the incoherent tunneling regime. Metals 177-182 mitochondrially encoded cytochrome c oxidase II Homo sapiens 48-54 3216199-6 1988 Based on the enthalpies, it is suggested that the order of combining affinity of these metal cations for phytic acid is Cu(II) greater than or equal to Zn(II) greater than or less than Cd(II) greater than Mn(II) greater than Mg(II) greater than Co(II) greater than Ni(II) The heats of precipitations (which includes binding, solvation changes, etc.) Metals 87-92 mitochondrially encoded cytochrome c oxidase II Homo sapiens 245-251 35113092-6 2022 The excellent performance can be attributed to the strong interactions between the metal and support, highly dispersed cobalt nanoparticles and the Lewis acid sites induced by the coordinated unsaturated Co(II) sites in phyllosilicate. Metals 83-88 mitochondrially encoded cytochrome c oxidase II Homo sapiens 204-210 34988578-1 2022 In the present report, three mononuclear azo-aromatic complexes of Co(II), 1-3, and an imine-based Co(II) complex, 4, were synthesized through a reaction of respective amine-functionalized pincer-like ligands, HL1-4, with CoCl2 6H2O in the ligand-to-metal ratio of 1 : 1. Metals 250-255 mitochondrially encoded cytochrome c oxidase II Homo sapiens 99-105 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. Metals 167-172 mitochondrially encoded cytochrome c oxidase II Homo sapiens 108-114 35337616-4 2022 For these biosynthetic pathways, selectivity for Co(II) over other divalent metal ions with similar ionic radii and coordination chemistry remains an open question with three competing hypotheses proposed: metal affinity, tetrapyrrole distortion, and product inhibition. Metals 76-81 mitochondrially encoded cytochrome c oxidase II Homo sapiens 49-55 35337616-4 2022 For these biosynthetic pathways, selectivity for Co(II) over other divalent metal ions with similar ionic radii and coordination chemistry remains an open question with three competing hypotheses proposed: metal affinity, tetrapyrrole distortion, and product inhibition. Metals 206-211 mitochondrially encoded cytochrome c oxidase II Homo sapiens 49-55 35364808-1 2022 An enantiopure ligand with four bidentate metal-binding sites and four (S)-carbon stereocenters self-assembles with octahedral ZnII or CoII to produce O-symmetric M8L6 coordination cages. Metals 42-47 mitochondrially encoded cytochrome c oxidase II Homo sapiens 135-139 35209092-1 2022 Metal-organic frameworks (M2(2-I-bdc)2bpe) (M = Zn(II) (1), Co(II) (2), 2-I-bdc = 2-iodoterephtalic acid, and bpe = 1,2-bis(4-pyridyl)ethane) were prepared and characterized by X-ray diffractometry. Metals 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 60-66 18964222-3 1986 The relative orders of the Langmuir constants K and the column retention-capacity factors k" for the four transition-metal ions are the same as the natural order of the stabilities predicted for their metal chelates: Fe(II) < Co(II) < Ni(II) < Cu(II). Metals 117-122 mitochondrially encoded cytochrome c oxidase II Homo sapiens 229-235 3853074-5 1985 N-7 can become a ligand to many metal ions such as Os(VI) from OsO3 X (Py)2, Pt(II) from square-planar cis- or trans-dichlorodiammine complexes, Co(II), and Mn(II). Metals 32-37 mitochondrially encoded cytochrome c oxidase II Homo sapiens 145-150 2990529-2 1985 The Co(II) enzyme, unlike all other metal-substituted derivatives, has functional properties closely similar to those of the native zinc enzyme. Metals 36-41 mitochondrially encoded cytochrome c oxidase II Homo sapiens 4-10 3002884-3 1986 There appears to be an additional transition metal-binding site on clostridiopeptidase A, accepting Zn(II), which is inhibitory (Ki = 550 microM), or Co(II), which is stimulatory (Kact = 200 microM). Metals 45-50 mitochondrially encoded cytochrome c oxidase II Homo sapiens 150-156 6329671-7 1984 Thus, in Co(II)7-metallothionein, the Co(II)-specific ESR signals are effectively suppressed by antiferromagnetic coupling of juxtaposed paramagnetic metal ions. Metals 17-22 mitochondrially encoded cytochrome c oxidase II Homo sapiens 9-15 6466647-4 1984 Electron paramagnetic resonance and absorption measurements of the Co(II) derivative are in agreement with the presence of a metal-thiolate cluster in this protein. Metals 125-130 mitochondrially encoded cytochrome c oxidase II Homo sapiens 67-73 6329671-10 1984 Up to binding of four equivalents of Co(II), the ESR amplitude increases in proportion to the metal content, indicating generation of magnetically noninteracting high-spin complexes. Metals 94-99 mitochondrially encoded cytochrome c oxidase II Homo sapiens 37-43 6164390-3 1981 For the Cu(II)-- and Co(II)--drug complexes, we have been able to identify imidazole as a metal ligand. Metals 90-95 mitochondrially encoded cytochrome c oxidase II Homo sapiens 21-26 6400891-0 1983 Interaction of adenosine 5"-triphosphate with metal ions X-ray structure of ternary complexes containing Mg(II), Ca(II), Mn(II), Co(II), ATP and 2,2"-dipyridylamine. Metals 46-51 mitochondrially encoded cytochrome c oxidase II Homo sapiens 129-135 6626154-10 1983 The formation of the "metachromatic complex" between Ret-P and Mn(II) or Co(II) inhibited the synthesis of retinyl phosphate mannose (Ret-P-Man) from exogenous and endogenous Ret-P and guanosine diphosphate [14C]mannose when bovine serum albumin was added after the metal ion. Metals 266-271 mitochondrially encoded cytochrome c oxidase II Homo sapiens 73-79 6863259-7 1983 For the two inverted repeats examined within pVH51, various divalent metal ions and spermidine resulted in the following hierarchy: Mn(II) less than Zn(II) less than Mg(II) less than Co(II) less than spermidine, where the transition midpoint was at lowest negative density values for Mn(II) and highest for spermidine. Metals 69-74 mitochondrially encoded cytochrome c oxidase II Homo sapiens 183-189 7107362-1 1982 Misonidazole and desmethylmisonidazole react in chemical systems with metal ions such as Zn(II), Co(II), Fe(II) and Fe(III). Metals 70-75 mitochondrially encoded cytochrome c oxidase II Homo sapiens 97-103 6794641-1 1981 X-ray absorption near-edge spectroscopy (XANES) of Co(II) in three derivatives of superoxide dismutase, namely [Cu(II)-Co(II)], [Cu(I)-Co(II)] and [...-Co(II)], suggests a tetrahedral coordination of the metal for all compounds. Metals 204-209 mitochondrially encoded cytochrome c oxidase II Homo sapiens 51-57 6794641-2 1981 Significant differences, detected in the spectrum of the [Cu(II)-Co(II)] derivative as compared to the other species, indicate that a conformational change and/or a different charge of the imidazole bridging the two metal sites in superoxide dismutase occur in coincidence with the change of copper valence. Metals 216-221 mitochondrially encoded cytochrome c oxidase II Homo sapiens 65-71 6969292-5 1980 Competition between Zn(II) and Co(II) for the first metal binding site suggests a value of 0.7 microM (pH 6.0, 30 degrees C, 1 M NaCl) for the dissociation constant of Zn(II). Metals 52-57 mitochondrially encoded cytochrome c oxidase II Homo sapiens 31-37 6969292-6 1980 The electronic spectra of the Co(II) enzyme lead to the suggestion that the coordination geometries around the metal ions in the first and second sites are related to those of a distorted tetrahedron and octahedron, respectively. Metals 111-116 mitochondrially encoded cytochrome c oxidase II Homo sapiens 30-36 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. Metals 101-106 mitochondrially encoded cytochrome c oxidase II Homo sapiens 137-143 93598-3 1979 The results of potentiometric titration also indicate that the stability of bleomycin-metal complexes is in the order Fe(II) less than Co(II) less than Ni(II) less than Cu(II) greater than Zn(II) and that these divalent metal complexes have a similar coordination environment. Metals 86-91 mitochondrially encoded cytochrome c oxidase II Homo sapiens 135-141 6821370-3 1980 Analysis of the spectra suggests that Co(II) binds at the same two metal-binding sites as does Zn(II). Metals 67-72 mitochondrially encoded cytochrome c oxidase II Homo sapiens 38-44 6821370-7 1980 A significant fraction of the protons in the whole molecule are affected by the binding of Co(II) at the first metal-ion-binding site (where the ligands are the enzyme"s sole thiol group and three histidine residues). Metals 111-116 mitochondrially encoded cytochrome c oxidase II Homo sapiens 91-97 117692-1 1978 In the present study use was made of the chelating ability of EDTA and the activating property of some metal ions Ca(II), Mg(II) or Mn(II) to counteract the inhibitory effect of Cu(II), Co(II), Pb(II) or Zn(II) ions on the B6-dependent kynurenine hydrolase and on kynurenine aminotransferase. Metals 103-108 mitochondrially encoded cytochrome c oxidase II Homo sapiens 186-192 163245-1 1975 High resolution electron spin resonance spectra of the stepwise formation of CN- complexes of Co(II) and Cu(II) carbonic anhydrase show that both metal enzymes form successive 1:1 and 2:1 addition products with CN- at 112 K. The 1:1 complex with the Cu(II) enzyme has a rhombic ESR spectrum similar to the spectra of the 1:1 complexes of the Cu(II) enzyme with CH3COO-, OCN-, N3-, and SH-. Metals 146-151 mitochondrially encoded cytochrome c oxidase II Homo sapiens 94-100 18212-1 1977 Mixed aquo-N-methylimidazole complexes of Co(II) have been studied as a function of pH to gain a fuller understanding of the metal-binding site in Co(II)-carbonic anhydrase. Metals 125-130 mitochondrially encoded cytochrome c oxidase II Homo sapiens 147-153 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. Metals 288-293 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. Metals 288-293 mitochondrially encoded cytochrome c oxidase II Homo sapiens 59-65 240709-2 1975 At pH 4.6 the addition of Co(II), Cd(II) or Mn(II) to the apoenzyme results in a destabilization of the native protein conformation, but in the range of pH 5.5--8.8 these metal ions, and Zn(II), slightly increase the conformational stability of the protein, in so far as they reduce the probability phi of solvent exposure of the peptide groups. Metals 171-176 mitochondrially encoded cytochrome c oxidase II Homo sapiens 26-32 33755727-6 2021 It revealed a tuning effect of different metal ions on the anti-cancer activities with that for Mn(II) and Zn(II) being much higher than that for Co(II) and Ni(II) in this system. Metals 41-46 mitochondrially encoded cytochrome c oxidase II Homo sapiens 146-152 4320976-8 1970 The similarity of the esr spectra of spin-labeled Zn(II) and Co(II) carbonic anhydrases suggests that the conformation at the active center is similar in the two metal derivatives. Metals 162-167 mitochondrially encoded cytochrome c oxidase II Homo sapiens 61-67 33910746-2 2021 The presence of active sites such as hydroxyl, carbonyl, thioethers, and amines, gave the membranes high adsorption capacities for the metal ions Au (III), Co (II), and Fe (III), as well as the cationic organic dye methylene blue (MB). Metals 135-140 mitochondrially encoded cytochrome c oxidase II Homo sapiens 156-163 33403814-1 2021 We report the synthesis of a novel metal-organic capsule constructed from six pyrogallol[4]arene macrocycles, which are switched together by 16 Fe(III) and 16 Co(II) ions. Metals 35-40 mitochondrially encoded cytochrome c oxidase II Homo sapiens 159-165 33901329-5 2021 The predictable magnetic behavior of the rotaxane Co II complexes demonstrates that interlocked ligands offer a new strategy to design metal complexes with interesting functionality. Metals 135-140 mitochondrially encoded cytochrome c oxidase II Homo sapiens 50-55 33932662-4 2021 Outdoor exposure exhibited different effects on adsorption property of MPs for metal ions, where adsorption capacities of PE and PS MPs for Co(II) were increased with aging degrees, while few change occurred on different aged PP MPs. Metals 79-84 mitochondrially encoded cytochrome c oxidase II Homo sapiens 140-146 33458549-7 2021 In the regeneration experiments, the Fe3O4@S-S/PMAA nanoparticles could be easily recovered by desorbing heavy metal ions from the adsorbents with eluents and showed good adsorption capacity for Co(II) and Pb(II) after eight recycles. Metals 111-116 mitochondrially encoded cytochrome c oxidase II Homo sapiens 195-201 33290612-2 2021 In this context, we report new artificial peptide ligands that fold into chiral helicates in the presence of labile metal ions such as Fe(II) and Co(II). Metals 116-121 mitochondrially encoded cytochrome c oxidase II Homo sapiens 146-152 33889784-0 2021 Speciation study involving mononuclear binary transition metal (CoII, NiII and CuII) complexes of L-methionine in non-ionic micellar medium. Metals 57-62 mitochondrially encoded cytochrome c oxidase II Homo sapiens 64-68 33889784-1 2021 The present work aims to evaluate the binding capacities of binary complexes of L-Methionine with transition metal ions CoII, NiII and CuII in Triton X 100-water mixtures, a non-ionic micellar media of different compositions (0.0-2.5% (v/v)), investigated under the experimental conditions of 0.16 mol/dm3 ionic strength using NaNO3 at a temperature of 303.0 +- 0.1 K Potentiometrically. Metals 109-114 mitochondrially encoded cytochrome c oxidase II Homo sapiens 120-124 33336849-2 2021 The reaction of ATBS with transition metal salts of Cu(II), Co(II), Ni(II), and Mn(II) afforded the corresponding ATBS-M complexes. Metals 37-42 mitochondrially encoded cytochrome c oxidase II Homo sapiens 60-66 33652868-0 2021 3D Metal-Organic Frameworks Based on Co(II) and Bithiophendicarboxylate: Synthesis, Crystal Structures, Gas Adsorption, and Magnetic Properties. Metals 3-8 mitochondrially encoded cytochrome c oxidase II Homo sapiens 37-43 33608553-7 2021 Thus, CoII is the cognate metal. Metals 26-31 mitochondrially encoded cytochrome c oxidase II Homo sapiens 6-10 33161270-11 2021 The geometrical structure around the metal centers were proved to be square planar for Cu(II) complex and tetrahedral for Co(II) an Ni(II) complexes. Metals 37-42 mitochondrially encoded cytochrome c oxidase II Homo sapiens 122-128 33325957-1 2021 Three new NiII/CoII-metal organic frameworks were self-assembled by the reaction of C3 symmetric 1,3,5-tribenzoic acid (H3BTC) and 2,4,6-tris(4-pyridyl)-1,3,5-triazine (4-TPT) ligands and NiII/CoII salts under solvothermal conditions. Metals 20-25 mitochondrially encoded cytochrome c oxidase II Homo sapiens 15-19 33325957-1 2021 Three new NiII/CoII-metal organic frameworks were self-assembled by the reaction of C3 symmetric 1,3,5-tribenzoic acid (H3BTC) and 2,4,6-tris(4-pyridyl)-1,3,5-triazine (4-TPT) ligands and NiII/CoII salts under solvothermal conditions. Metals 20-25 mitochondrially encoded cytochrome c oxidase II Homo sapiens 193-197 32815718-5 2020 Coordination of the weak donor THF to [CoII(DPP 2-)] changes the orbital overlap between the DPP 2- ligand radical pi-orbitals and the cobalt(II) metalloradical d-orbitals, which results in a spin-flip to the triplet ground state without changing the oxidation states of the metal or DPP 2- ligand. Metals 146-151 mitochondrially encoded cytochrome c oxidase II Homo sapiens 39-43 32729641-4 2020 While Co(II) possibly holds the record of having the largest number of zero-field SIMs known for any transition metal ions, controlling the magnetic anisotropy in these systems are is still a challenge. Metals 112-117 mitochondrially encoded cytochrome c oxidase II Homo sapiens 6-12 32485604-7 2020 Co(II) ions create a unique absorption peak during the complex formation and this peak provides sensitive determination of this metal ion in existence of other metal ions. Metals 128-133 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-6 32485604-7 2020 Co(II) ions create a unique absorption peak during the complex formation and this peak provides sensitive determination of this metal ion in existence of other metal ions. Metals 160-165 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-6 32485604-11 2020 The proposed metal ion sensor provides a very facile and convenient way to determine the concentration of Co(II) ions in aqueous system. Metals 13-18 mitochondrially encoded cytochrome c oxidase II Homo sapiens 106-112 33463025-2 2020 Among those SMMs based on one single transition metal, tetrahedral CoII-complexes are prominent, and their large zero-field splitting arises exclusively from coupling between the d x 2 - y 2 and dxy orbitals. Metals 48-53 mitochondrially encoded cytochrome c oxidase II Homo sapiens 67-71 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. Metals 137-142 mitochondrially encoded cytochrome c oxidase II Homo sapiens 20-27 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. Metals 144-149 mitochondrially encoded cytochrome c oxidase II Homo sapiens 118-125 32871348-3 2020 We evaluated the contribution of different side chains to binding of Co(II), Ni(II), Zn(II) and Mn(II) using systematic mutagenesis of the amino acids that constitute the primary metal coordination and outer spheres. Metals 179-184 mitochondrially encoded cytochrome c oxidase II Homo sapiens 69-75 32984710-2 2020 During the Co(II) adsorption process, these two kinds of geopolymeric adsorbents could be combined with heavy metal ions to optimize each other and form heavy metal-grown aid adsorbents. Metals 110-115 mitochondrially encoded cytochrome c oxidase II Homo sapiens 11-17 32984710-2 2020 During the Co(II) adsorption process, these two kinds of geopolymeric adsorbents could be combined with heavy metal ions to optimize each other and form heavy metal-grown aid adsorbents. Metals 159-164 mitochondrially encoded cytochrome c oxidase II Homo sapiens 11-17 32568423-3 2020 Atomic replacements of the Fe II by other metal(II) ions (e.g., Zn II /Co II ) via synthesizing isostructural trinuclear-complex precursors (Fe 2 Zn/Fe 2 Co), namely the "heteroatom modulator approach", realizes the inhibition of iron atoms aggregating toward nanoclusters with formation of a stable iron-dimer cluster in an optimal metal-nitrogen moiety within the carbon layer, clearly identified by direct transmission electron microscope imaging with X-ray absorption fine structure analyses. Metals 333-338 mitochondrially encoded cytochrome c oxidase II Homo sapiens 71-76 32478511-7 2020 Four metal-mediated base pairs are observed between the N7 atoms of G and CoII, an interaction that strongly preserves the central junction site. Metals 5-10 mitochondrially encoded cytochrome c oxidase II Homo sapiens 74-78 32526144-0 2020 Structural Transformation and Spatial Defect Formation of a Co(II) MOF Triggered by Varied Metal-Center Coordination Configuration. Metals 91-96 mitochondrially encoded cytochrome c oxidase II Homo sapiens 60-66 32306254-1 2020 In the present study, a geopolymer from dolochar ash was synthesized and used for the removal of heavy metal ions such as Co(II), Ni(II), Cd(II), and Pb(II) from the aqueous solution through the adsorption process. Metals 103-108 mitochondrially encoded cytochrome c oxidase II Homo sapiens 122-128 32794423-9 2021 Binding interactions and energies of ligand and its metal complexes [ML]2+ (M = VO(IV), Mn(II), Co(II), Ni(II), Cu(II), Zn(II)) against the receptors EGFR and HER2 are performed using the Auto dock module. Metals 52-57 mitochondrially encoded cytochrome c oxidase II Homo sapiens 96-102 32312397-2 2020 In the extraction of Mn(II), Co(II), Ni(II), Tb(III) and Dy(III), the compositions of the extracted metal complexes were determined from the measurements of the magnetophoretic velocity of a single droplet as a function of the mole ratio of the metal ion and the ligand. Metals 100-105 mitochondrially encoded cytochrome c oxidase II Homo sapiens 29-35 32368977-4 2020 Formation of the Schiff base and the metal (Zn[II], Cu[II], Co[II] and Ni[II]) chelates was supported by spectral and analytical data. Metals 37-42 mitochondrially encoded cytochrome c oxidase II Homo sapiens 60-65 31874761-2 2020 For comparison, and to justify the grafting of BPED groups onto the GO sheets, the GO-based material obtained after each step was used as a solid phase adsorbent for removing Cu(II), Ni(II) and Co(II) metal ions from aqueous solutions. Metals 201-206 mitochondrially encoded cytochrome c oxidase II Homo sapiens 194-200 31874761-4 2020 Additionally, it was demonstrated that the equilibrium adsorption capacities of these metal ions followed the order of Cu(II)>Ni(II)>Co(II) whatever the GO-based adsorbent. Metals 86-91 mitochondrially encoded cytochrome c oxidase II Homo sapiens 133-139 32250753-4 2020 The influence of diverse parameters on remediation of ZnII/CoII was examined, involving pH of metal ion solutions (pH 1-7), reaction time (1-60 min), solid amount (5-100 mg) and ionic concentration (0.1-2.0 mol/L). Metals 94-99 mitochondrially encoded cytochrome c oxidase II Homo sapiens 59-63 31832938-6 2020 The results of spectroscopic analysis also indicated that good adsorption performance of Co(II) mainly depends on surface chelation between functional groups and metal ions. Metals 162-167 mitochondrially encoded cytochrome c oxidase II Homo sapiens 89-95 31247880-5 2019 CoII titrations reveal that both metallochaperones have similar electronic absorption characteristics that indicate the presence of two tetrahedral metal coordination sites. Metals 33-38 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-4 31468606-2 2019 The modified oligonucleotides were shown to complex a range of different transition metal cations including Ni(II), Cu(II), Zn(II) and Co(II), as indicated by UV/Vis spectroscopy and ion mobility mass spectrometry. Metals 84-89 mitochondrially encoded cytochrome c oxidase II Homo sapiens 135-141 31247880-6 2019 High-affinity metal binding at the CXCC motif activates the GTPase activity of both enzymes, with ZnII more effective than CoII. Metals 14-19 mitochondrially encoded cytochrome c oxidase II Homo sapiens 123-127 31508635-3 2019 The reaction of Rad2 with the 3d transition metal complexes M(hfac)2 xH2O (hfac- = hexafluoroacetylacetonate) led to mononuclear metal complexes of general formula M(hfac)2(Rad2) [M = Zn(ii) (1); Ni(ii) (2) and Co(ii) (3)] whose structures have been determined by single crystal X-ray diffraction. Metals 44-49 mitochondrially encoded cytochrome c oxidase II Homo sapiens 187-189 31508635-3 2019 The reaction of Rad2 with the 3d transition metal complexes M(hfac)2 xH2O (hfac- = hexafluoroacetylacetonate) led to mononuclear metal complexes of general formula M(hfac)2(Rad2) [M = Zn(ii) (1); Ni(ii) (2) and Co(ii) (3)] whose structures have been determined by single crystal X-ray diffraction. Metals 44-49 mitochondrially encoded cytochrome c oxidase II Homo sapiens 199-201 31508635-3 2019 The reaction of Rad2 with the 3d transition metal complexes M(hfac)2 xH2O (hfac- = hexafluoroacetylacetonate) led to mononuclear metal complexes of general formula M(hfac)2(Rad2) [M = Zn(ii) (1); Ni(ii) (2) and Co(ii) (3)] whose structures have been determined by single crystal X-ray diffraction. Metals 44-49 mitochondrially encoded cytochrome c oxidase II Homo sapiens 211-217 31508635-3 2019 The reaction of Rad2 with the 3d transition metal complexes M(hfac)2 xH2O (hfac- = hexafluoroacetylacetonate) led to mononuclear metal complexes of general formula M(hfac)2(Rad2) [M = Zn(ii) (1); Ni(ii) (2) and Co(ii) (3)] whose structures have been determined by single crystal X-ray diffraction. Metals 129-134 mitochondrially encoded cytochrome c oxidase II Homo sapiens 187-189 31508635-3 2019 The reaction of Rad2 with the 3d transition metal complexes M(hfac)2 xH2O (hfac- = hexafluoroacetylacetonate) led to mononuclear metal complexes of general formula M(hfac)2(Rad2) [M = Zn(ii) (1); Ni(ii) (2) and Co(ii) (3)] whose structures have been determined by single crystal X-ray diffraction. Metals 129-134 mitochondrially encoded cytochrome c oxidase II Homo sapiens 199-201 31508635-3 2019 The reaction of Rad2 with the 3d transition metal complexes M(hfac)2 xH2O (hfac- = hexafluoroacetylacetonate) led to mononuclear metal complexes of general formula M(hfac)2(Rad2) [M = Zn(ii) (1); Ni(ii) (2) and Co(ii) (3)] whose structures have been determined by single crystal X-ray diffraction. Metals 129-134 mitochondrially encoded cytochrome c oxidase II Homo sapiens 211-217 31508635-5 2019 In the case of the Zn(ii) complex (1) through-space intermolecular radicalradical antiferromagnetic exchange interactions via pi*pi* contacts are observed, whereas strong intramolecular through-bond metal-radical ferromagnetic interactions [J = +59.3(9) cm-1] are observed for the Ni(ii) complex (2). Metals 199-204 mitochondrially encoded cytochrome c oxidase II Homo sapiens 22-24 31508635-6 2019 For the Co(ii) complex (3), computational and magnetic studies reveal substantial zero field splitting and ferromagnetic metal-radical interactions. Metals 121-126 mitochondrially encoded cytochrome c oxidase II Homo sapiens 8-14 31066416-3 2019 The ligand (H2L) comprises two different asymmetric binding pockets; however, when reacted with Mn(ii), Co(ii), Cu(ii) and Zn(ii) salts, very stable self-assembled [2 x 2] grid complexes form regardless of the employed metal-to-ligand ratio. Metals 219-224 mitochondrially encoded cytochrome c oxidase II Homo sapiens 99-101 31434303-7 2019 The method was then applied to the fabrication of a heavy metal adsorbent that possessed a sufficient adsorption capacity of Co(II) ions. Metals 58-63 mitochondrially encoded cytochrome c oxidase II Homo sapiens 125-131 31035130-5 2019 Furthermore, the influence of bivalent metal ions on the binding affinity was resulted in order of Cu(II) > Ca(II) > Co(II) > Zn(II). Metals 39-44 mitochondrially encoded cytochrome c oxidase II Homo sapiens 123-129 30913819-4 2019 The presence of Zn(II) metal ion is determined through the band at 150 cm-1 (T2g(1) phonon mode), which is not present in the pure Co-ferrite, a blue-shift of the Eg vibrational mode depending on Zn(II)/Co(II) cationic distribution and a shoulder at ~250 cm-1, which appears when zinc enters in the structure, and a broadening and a red-shift in the A1g phonon mode is observed in Raman spectra of 2-4 samples. Metals 23-28 mitochondrially encoded cytochrome c oxidase II Homo sapiens 203-209 31350722-7 2019 Unexpectedly, collisional activation of the complex formed between the peptide and [CoIII(NH3)6]3+ induced gas-phase reduction of the metal to CoII, allowing the peptide to fragment via radical-based dissociation pathways. Metals 134-139 mitochondrially encoded cytochrome c oxidase II Homo sapiens 84-88 31521068-4 2019 Photoexcitation at 525 nm produces a low-spin CoII ligand-to-metal charge transfer state which undergoes intersystem crossing to high-spin CoII in 67 fs. Metals 61-66 mitochondrially encoded cytochrome c oxidase II Homo sapiens 46-50 31521068-4 2019 Photoexcitation at 525 nm produces a low-spin CoII ligand-to-metal charge transfer state which undergoes intersystem crossing to high-spin CoII in 67 fs. Metals 61-66 mitochondrially encoded cytochrome c oxidase II Homo sapiens 139-143 31317334-2 2019 As inhalation of heavy metal ions like cobalt can lead to lung cancer, a fluorescent probe was designed for the determination of Co(II) both in aqueous solutions and living cells. Metals 23-28 mitochondrially encoded cytochrome c oxidase II Homo sapiens 129-135 31489168-5 2019 These show the peptide is trimeric and binds to both Cu(ii) and Ni(ii) in a 1 : 1 ratio with the histidine residues involved in the metal coordination, as designed. Metals 132-137 mitochondrially encoded cytochrome c oxidase II Homo sapiens 67-69 31066416-3 2019 The ligand (H2L) comprises two different asymmetric binding pockets; however, when reacted with Mn(ii), Co(ii), Cu(ii) and Zn(ii) salts, very stable self-assembled [2 x 2] grid complexes form regardless of the employed metal-to-ligand ratio. Metals 219-224 mitochondrially encoded cytochrome c oxidase II Homo sapiens 104-110 31066416-3 2019 The ligand (H2L) comprises two different asymmetric binding pockets; however, when reacted with Mn(ii), Co(ii), Cu(ii) and Zn(ii) salts, very stable self-assembled [2 x 2] grid complexes form regardless of the employed metal-to-ligand ratio. Metals 219-224 mitochondrially encoded cytochrome c oxidase II Homo sapiens 107-109 31066416-3 2019 The ligand (H2L) comprises two different asymmetric binding pockets; however, when reacted with Mn(ii), Co(ii), Cu(ii) and Zn(ii) salts, very stable self-assembled [2 x 2] grid complexes form regardless of the employed metal-to-ligand ratio. Metals 219-224 mitochondrially encoded cytochrome c oxidase II Homo sapiens 107-109 30951298-5 2019 The central transition-metal ion M n+ (MnII, FeIII, CoII, NiII, CuII, ZnII, PdII) in the POP structure and also the nature of the capping group (AsO43-, SeO32-, PO43-, phenyl-AsO32-) influence the resulting catalytic performance. Metals 23-28 mitochondrially encoded cytochrome c oxidase II Homo sapiens 52-56 31083943-0 2019 Biomimetic Self-Assembly of CoII-Seamed Hexameric Metal-Organic Nanocapsules. Metals 50-55 mitochondrially encoded cytochrome c oxidase II Homo sapiens 28-32 30740917-0 2019 Anchoring CoII Ions into a Thiol-Laced Metal-Organic Framework for Efficient Visible-Light-Driven Conversion of CO2 into CO. Metals 39-44 mitochondrially encoded cytochrome c oxidase II Homo sapiens 10-14 30740917-3 2019 To address this, catalytically active CoII centers can be anchored into the porous matrix of metal-organic frameworks (MOFs) by utilizing a robust Zr-based MOF (Zr-DMBD) functionalized with freestanding thiol groups to enable efficient post-synthetic metal insertion. Metals 93-98 mitochondrially encoded cytochrome c oxidase II Homo sapiens 38-42 30740917-3 2019 To address this, catalytically active CoII centers can be anchored into the porous matrix of metal-organic frameworks (MOFs) by utilizing a robust Zr-based MOF (Zr-DMBD) functionalized with freestanding thiol groups to enable efficient post-synthetic metal insertion. Metals 251-256 mitochondrially encoded cytochrome c oxidase II Homo sapiens 38-42 30865746-4 2019 The binding ratio of the sensor to Fe(ii), Co(ii), and Cu(ii) is 2 sensors to 1 metal ion. Metals 80-85 mitochondrially encoded cytochrome c oxidase II Homo sapiens 38-40 30865746-4 2019 The binding ratio of the sensor to Fe(ii), Co(ii), and Cu(ii) is 2 sensors to 1 metal ion. Metals 80-85 mitochondrially encoded cytochrome c oxidase II Homo sapiens 43-48 30865746-4 2019 The binding ratio of the sensor to Fe(ii), Co(ii), and Cu(ii) is 2 sensors to 1 metal ion. Metals 80-85 mitochondrially encoded cytochrome c oxidase II Homo sapiens 46-48 31205453-1 2019 This paper includes synthesis and characterization of mixed ligand complexes derived from mefenamic acid and metformin using transition metal ions such as Co(II) and Cu(II). Metals 136-141 mitochondrially encoded cytochrome c oxidase II Homo sapiens 155-161 30997801-0 2019 Three Co(II) Metal-Organic Frameworks with Diverse Architectures for Selective Gas Sorption and Magnetic Studies. Metals 13-18 mitochondrially encoded cytochrome c oxidase II Homo sapiens 6-12 31459576-9 2019 The thermodynamic data reveal that the interaction best suited for Al(III) ion compared to other metal ions (Al(III) > Co(II) > Hg(II) > Cr(III) Cr(VI)). Metals 97-102 mitochondrially encoded cytochrome c oxidase II Homo sapiens 122-128 30888790-1 2019 The structural diversity of Co(II) metal centers is known to influence their physicochemical properties. Metals 35-40 mitochondrially encoded cytochrome c oxidase II Homo sapiens 28-34 31459694-5 2019 The Mn(II) (1b) and Co(II) (1c) complexes show antiferromagnetic coupling between the two associated metal centers via the H-bonding interaction pathway. Metals 101-106 mitochondrially encoded cytochrome c oxidase II Homo sapiens 20-26 30968885-1 2019 A photoactive, hetero-metallic CoII/RuII-based metal-organic framework (MOF) with a large channel aperture, ca. Metals 22-27 mitochondrially encoded cytochrome c oxidase II Homo sapiens 31-35 30874271-2 2019 From this ligand and a bis-bidentate nitronyl nitroxide ligand, metal complexes of MnII and CoII ions were also synthesized and characterized. Metals 64-69 mitochondrially encoded cytochrome c oxidase II Homo sapiens 92-96 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. Metals 97-102 mitochondrially encoded cytochrome c oxidase II Homo sapiens 85-89 30724472-2 2019 Herein, we report on a unique strategy to prepare Fe-Co-N-C-x (x refers to the pyrolysis temperature) electrocatalysts which involves anion-exchange of [Fe(CN)6 ]3- into a cationic CoII -based metal-organic framework precursor prior to heat treatment. Metals 193-198 mitochondrially encoded cytochrome c oxidase II Homo sapiens 181-185 30724472-4 2019 This is the first example of Fe-Co-N-C electrocatalysts fabricated from a cationic CoII -based MOF precursor that dopes the Fe element via anion-exchange, and our current work provides a new entrance towards MOF-derived transition-metal (e.g. Fe or Co) and nitrogen-codoped carbon electrocatalysts with excellent ORR activity. Metals 231-236 mitochondrially encoded cytochrome c oxidase II Homo sapiens 83-87 30835450-0 2019 Slow Magnetic Relaxation of Co(II) Single Chains Embedded within Metal-Organic Superstructures. Metals 65-70 mitochondrially encoded cytochrome c oxidase II Homo sapiens 28-33 30835450-2 2019 The compounds feature 2D and 3D metal-organic networks that encapsulate Co(II)-based chains in a rigid superstructure. Metals 32-37 mitochondrially encoded cytochrome c oxidase II Homo sapiens 72-77 31458347-7 2018 The order of the selectivity of cross-linked chitosan derivatives toward metal ions was found to be Cu(II) > Cd(II) > Fe(II) > Co(II) > Ni(II). Metals 73-78 mitochondrially encoded cytochrome c oxidase II Homo sapiens 136-142 30512937-3 2018 Here, we provide evidence for multiple NOR turnover in monoformyl-heme-containing FeBMb1 proteins loaded with FeII, CoII, or ZnII metal ions at the FeB site (FeII/CoII/ZnII-FeBMb1(MF-heme)). Metals 130-135 mitochondrially encoded cytochrome c oxidase II Homo sapiens 163-167 30739202-2 2019 The resulting metal-organic gel (MOG) shows enhanced peroxidase-like activity, most likely due to the synergetic redox cycling between Co(III)/Co(II) and Cu(II)/Cu(I) pairs. Metals 14-19 mitochondrially encoded cytochrome c oxidase II Homo sapiens 143-149 30675786-1 2019 Chiral coordination compounds of Co(II) and other open-shell metal complexes display enhanced vibrational circular dichroism (VCD) spectra associated with the existence of low-lying excited states (LLESs). Metals 61-66 mitochondrially encoded cytochrome c oxidase II Homo sapiens 33-39 32801406-4 2019 Competitive adsorption tests using multi metals showed that the adsorption affinity of metal ions on the rGO and its NHs follows the order (Cu(II), Zn(II)) > Ni(II) > Co(II) > (Pb(II), Cd(II)), which is similar to the order observed for single-metal adsorption experiments. Metals 87-92 mitochondrially encoded cytochrome c oxidase II Homo sapiens 167-173 30207688-6 2018 Octahedral metal ions, such as FeII, CoII, NiII, ZnII, and CdII, constitute the vertices. Metals 11-16 mitochondrially encoded cytochrome c oxidase II Homo sapiens 37-41 30362217-4 2018 The increased photocatalytic performance of CoZn is due to the enhanced dinuclear metal synergistic catalysis (DMSC) effect between ZnII and CoII , which dramatically lowers the activation barriers of both transition states of CO2 reduction. Metals 82-87 mitochondrially encoded cytochrome c oxidase II Homo sapiens 141-145 30303221-4 2018 One-electron oxidation of 1 by silver triflate produces the [(imSQC(O)Ph)CoII(imQC(O)Ph)]OTf 2toluene (2) derivative with the trigonal prismatic coordination environment of the metal arising from the additional coordination of -C(O)Ph hemilabile groups. Metals 177-182 mitochondrially encoded cytochrome c oxidase II Homo sapiens 73-77 30276925-2 2018 Several metal ions (CuII , NiII , MgII , MnII , CoII , and ZnII ) were selected as the central metal ion, and chiral drugs ezetimibe (EZM) and ambrisentan (AMB) were used as the reference to each other for isomeric differentiation by using electrospray ionization quadrupole time-of-flight mass spectrometry. Metals 8-13 mitochondrially encoded cytochrome c oxidase II Homo sapiens 48-52 30276925-2 2018 Several metal ions (CuII , NiII , MgII , MnII , CoII , and ZnII ) were selected as the central metal ion, and chiral drugs ezetimibe (EZM) and ambrisentan (AMB) were used as the reference to each other for isomeric differentiation by using electrospray ionization quadrupole time-of-flight mass spectrometry. Metals 95-100 mitochondrially encoded cytochrome c oxidase II Homo sapiens 48-52 30378605-4 2018 The considered binuclear CoII diketonate adducts manifest the capability of undergoing one- and two-step spin transitions induced by intramolecular electron transfers between the metal ions and the ligand system. Metals 179-184 mitochondrially encoded cytochrome c oxidase II Homo sapiens 25-29 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. Metals 158-163 mitochondrially encoded cytochrome c oxidase II Homo sapiens 84-88 29975380-5 2018 Most interestingly, the mixed-metal systems can show a higher blocking temperature than the Co(ii) compound, suggesting that the randomly distributed metal ions have synergistic effects on slow relaxation of magnetization. Metals 150-155 mitochondrially encoded cytochrome c oxidase II Homo sapiens 92-98 30227633-4 2018 In addition, water hydration and divalent metal ion (CoII) interactions also play a crucial role in the stabilization of CCG trinucleotide repeats (TNRs). Metals 42-47 mitochondrially encoded cytochrome c oxidase II Homo sapiens 53-57 30111101-6 2018 Metal chelates of CH3C(O)NHOH catalyze the hydrolysis of CH3C(O)N O at the efficacy order of CuII > ZnII > NiII > CoII where only CuII catalyzes the hydrolysis also in the absence of the hydroxamate. Metals 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 123-127 29951660-4 2018 Furthermore, the incorporation of a paramagnetic Co(ii) metal ion into the framework caused 1 to show spin-flop behaviour as the result of a field-induced magnetic transition. Metals 56-61 mitochondrially encoded cytochrome c oxidase II Homo sapiens 49-55 29951660-5 2018 The incorporation of two flexible ligands and Co(ii) metal ions represents a feasible approach for the advancement of multifunctional materials. Metals 53-58 mitochondrially encoded cytochrome c oxidase II Homo sapiens 46-52 29492773-5 2018 The ability of these metal ions to produce oligosaccharide adduct ions by ESI had the general trend: Ca(II) > Mg(II) > Ni(II) > Co(II) > Zn(II) > Cu(II) > Na(I) > K(I) > Al(III) Fe(III) Cr(III). Metals 21-26 mitochondrially encoded cytochrome c oxidase II Homo sapiens 137-143 29975380-3 2018 These behaviors are quite different from the parent Co(ii) and Ni(ii) materials, and even a small amount of metal replacement can cause significant magnetic changes. Metals 108-113 mitochondrially encoded cytochrome c oxidase II Homo sapiens 52-58 29975380-3 2018 These behaviors are quite different from the parent Co(ii) and Ni(ii) materials, and even a small amount of metal replacement can cause significant magnetic changes. Metals 108-113 mitochondrially encoded cytochrome c oxidase II Homo sapiens 55-57 29975380-5 2018 Most interestingly, the mixed-metal systems can show a higher blocking temperature than the Co(ii) compound, suggesting that the randomly distributed metal ions have synergistic effects on slow relaxation of magnetization. Metals 30-35 mitochondrially encoded cytochrome c oxidase II Homo sapiens 92-98 29436750-0 2018 A Moisture-Stable 3D Microporous CoII -Metal-Organic Framework with Potential for Highly Selective CO2 Separation under Ambient Conditions. Metals 39-44 mitochondrially encoded cytochrome c oxidase II Homo sapiens 33-37 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. Metals 81-86 mitochondrially encoded cytochrome c oxidase II Homo sapiens 153-157 29178431-3 2018 Metal ions such as cobalt(II), iron(III), platinum(IV) and nickel(II) are found to partition preferentially to one of the phases of the acidic aqueous biphasic system and it is here shown that it successfully allows the difficult separation of CoII from NiII , here studied at 24 and 50 C. Metals 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 244-248 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. Metals 81-86 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-74 29562094-4 2018 At pH 9.0, the affinity of both generations towards heavy metal ions was also observed in the decreasing order of Zn(II) > Co(II) > Ni(II) > Cu(II) > Cd(II). Metals 58-63 mitochondrially encoded cytochrome c oxidase II Homo sapiens 126-132 29211477-0 2018 Titanium(III)-Oxo Clusters in a Metal-Organic Framework Support Single-Site Co(II)-Hydride Catalysts for Arene Hydrogenation. Metals 32-37 mitochondrially encoded cytochrome c oxidase II Homo sapiens 76-81 29064238-7 2017 The first oxidation is metal-centered for the (TpYPP)Co and benzo(TpYPP)CoII derivatives, leading to generation of a cobalt(III) porphyrin with an intact pi-ring system, but this redox process is ring-centered in the case of butano(TpYPP)CoII and gives a CoII pi-cation radical product. Metals 23-28 mitochondrially encoded cytochrome c oxidase II Homo sapiens 72-76 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. Metals 345-350 mitochondrially encoded cytochrome c oxidase II Homo sapiens 43-47 28683368-5 2017 Cyclic voltammetry studies showed that structural modifications made in the L2- ligands caused a slight influence on the electronic density of the metal center, and the E1/2 values for the CoIII/CoII redox couple increased following the electronic effect of the R-substituent, in the order: 2 (R=OCH3)<1 (R=H)<3 (R=Cl). Metals 147-152 mitochondrially encoded cytochrome c oxidase II Homo sapiens 189-193 29231218-1 2018 We successfully developed an approach to synthesize a metal oxide- and N-codoped carbon nanosheet, NC@CoO/CuO, derived from a metal-organic framework nanofiber, Cu(ii)-Asp@Co(II) (Asp = l-aspartate). Metals 54-59 mitochondrially encoded cytochrome c oxidase II Homo sapiens 172-178 29064238-7 2017 The first oxidation is metal-centered for the (TpYPP)Co and benzo(TpYPP)CoII derivatives, leading to generation of a cobalt(III) porphyrin with an intact pi-ring system, but this redox process is ring-centered in the case of butano(TpYPP)CoII and gives a CoII pi-cation radical product. Metals 23-28 mitochondrially encoded cytochrome c oxidase II Homo sapiens 238-242 29064238-7 2017 The first oxidation is metal-centered for the (TpYPP)Co and benzo(TpYPP)CoII derivatives, leading to generation of a cobalt(III) porphyrin with an intact pi-ring system, but this redox process is ring-centered in the case of butano(TpYPP)CoII and gives a CoII pi-cation radical product. Metals 23-28 mitochondrially encoded cytochrome c oxidase II Homo sapiens 238-242 28617591-0 2017 Control of Interchain Antiferromagnetic Coupling in Porous Co(II)-Based Metal-Organic Frameworks by Tuning the Aromatic Linker Length: How Far Does Magnetic Interaction Propagate? Metals 72-77 mitochondrially encoded cytochrome c oxidase II Homo sapiens 59-64 28525865-3 2017 This bidentate ligand coordinates three metal ions of Co(II), Cu(II) and Fe(II) via nitrogen and oxygen atoms. Metals 40-45 mitochondrially encoded cytochrome c oxidase II Homo sapiens 54-60 29250391-5 2017 A barium-mu2-oxygen motif develops along the a axis, connecting symmetry-related dinuclear BaII-CoII cationic fragments in a wave-like chain, forming a one-dimensional metal coordination polymer. Metals 168-173 mitochondrially encoded cytochrome c oxidase II Homo sapiens 96-100 28803372-9 2017 The addition of a transition metal as catalyst, such as Fe(II) or Co(II), increased considerably the TOC removal efficiency higher than 50%, but not in all cases. Metals 29-34 mitochondrially encoded cytochrome c oxidase II Homo sapiens 66-72 28937969-3 2017 The proposed method displayed high selectivity toward Co(II) over other metal ions. Metals 72-77 mitochondrially encoded cytochrome c oxidase II Homo sapiens 54-60 28729223-3 2017 These polymeric Schiff base ligands, SBOPA and SBPBA generates polymeric metal complexes in high yields on reaction with transition metal acetates, M(CH3COO)2.xH2O where M = Mn(II), Co(II), Ni(II), Cu(II) and Zn(II). Metals 73-78 mitochondrially encoded cytochrome c oxidase II Homo sapiens 182-188 28621377-0 2017 Controlling the oxidation of bis-tridentate cobalt(ii) complexes having bis(2-pyridylalkyl)amines: ligand vs. metal oxidation. Metals 110-115 mitochondrially encoded cytochrome c oxidase II Homo sapiens 51-53 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. Metals 274-279 mitochondrially encoded cytochrome c oxidase II Homo sapiens 82-86 28488285-3 2017 Experimental results revealed that the parent [CoII CoII ] complex undergoes two successive metal-based 1 e- reductions to generate the catalytically active species [CoI CoI ], and DFT calculations suggested that addition of a proton to one CoI triggers a cooperative 1 e- transfer by each of these CoI centers. Metals 92-97 mitochondrially encoded cytochrome c oxidase II Homo sapiens 47-51 28488285-3 2017 Experimental results revealed that the parent [CoII CoII ] complex undergoes two successive metal-based 1 e- reductions to generate the catalytically active species [CoI CoI ], and DFT calculations suggested that addition of a proton to one CoI triggers a cooperative 1 e- transfer by each of these CoI centers. Metals 92-97 mitochondrially encoded cytochrome c oxidase II Homo sapiens 52-56 28561569-1 2017 In this work, the effects of ligand field strength as well as the metal coordination geometry on magnetic anisotropy of pentacoordinated CoII complexes have been investigated using a combined experimental and theoretical approach. Metals 66-71 mitochondrially encoded cytochrome c oxidase II Homo sapiens 137-141 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. Metals 31-36 mitochondrially encoded cytochrome c oxidase II Homo sapiens 126-132 28257185-0 2017 Incorporation of Pyrazine and Bipyridine Linkers with High-Spin Fe(II) and Co(II) in a Metal-Organic Framework. Metals 87-92 mitochondrially encoded cytochrome c oxidase II Homo sapiens 75-81 28517938-1 2017 Escherichia coli RcnR (resistance to cobalt and nickel regulator, EcRcnR) is a metal-responsive repressor of the genes encoding the Ni(II) and Co(II) exporter proteins RcnAB by binding to PRcnAB. Metals 79-84 mitochondrially encoded cytochrome c oxidase II Homo sapiens 143-149 28517938-2 2017 The DNA binding affinity is weakened when the cognate ions Ni(II) and Co(II) bind to EcRcnR in a six-coordinate site that features a (N/O)5S ligand donor-atom set in distinct sites: while both metal ions are bound by the N terminus, Cys35, and His64, Co(II) is additionally bound by His3. Metals 193-198 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-76 28517938-12 2017 The spectroscopic and functional data obtained on the mutants were used to calculate models of the metal-site structures of EcRcnR bound to Ni(II), Co(II), and Zn(II). Metals 99-104 mitochondrially encoded cytochrome c oxidase II Homo sapiens 148-154 28347141-3 2017 Here we demonstrate that elemental halogens quantitatively oxidize coordinatively unsaturated Co(II) ions in a robust azolate metal-organic framework (MOF) to produce stable and safe-to-handle Co(III) materials featuring terminal Co(III)-halogen bonds. Metals 126-131 mitochondrially encoded cytochrome c oxidase II Homo sapiens 94-100 28083807-1 2017 New phthalonitrile compound with Schiff base, carbothioamide and thiazole moieties as substituents and its corresponding metal-free and metallophthalocyanines (Zn(II), Ni(II), Co(II), and Cu(II)) were synthesized and characterized for the first time. Metals 121-126 mitochondrially encoded cytochrome c oxidase II Homo sapiens 176-181 28436418-0 2017 Oxoaporphine Metal Complexes (CoII, NiII, ZnII) with High Antitumor Activity by Inducing Mitochondria-Mediated Apoptosis and S-phase Arrest in HepG2. Metals 13-18 mitochondrially encoded cytochrome c oxidase II Homo sapiens 30-34 28225611-1 2017 The magnetic properties of pseudotetrahedral Co(II) complexes spawned intense interest after (PPh4)2[Co(SPh)4] was shown to be the first mononuclear transition-metal complex displaying slow relaxation of the magnetization in the absence of a direct current magnetic field. Metals 160-165 mitochondrially encoded cytochrome c oxidase II Homo sapiens 45-51 29386985-1 2017 Co(II) electronic configuration allows its use as a spectroscopic probe in UV-Vis experiments to characterize the metal coordination sphere that is an essential component of the functional structure of zinc-binding proteins and to evaluate the metal ion affinities of these proteins. Metals 114-119 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-6 28106394-1 2017 The structure and properties of metallo-supramolecular polyelectrolytes (MEPEs) self-assembled from rigid 2,6-bis(2-pyridyl)pyrimidine and the metal ions FeII and CoII are presented. Metals 32-37 mitochondrially encoded cytochrome c oxidase II Homo sapiens 163-167 27541797-2 2017 Co(II), Ni(II), Cu(II) and Zn(II) of the synthesized Schiff bases were prepared by using a molar ratio of ligand:metal as 1:1. Metals 113-118 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-6 29386985-1 2017 Co(II) electronic configuration allows its use as a spectroscopic probe in UV-Vis experiments to characterize the metal coordination sphere that is an essential component of the functional structure of zinc-binding proteins and to evaluate the metal ion affinities of these proteins. Metals 244-249 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-6 29386985-2 2017 Here, exploiting the capability of the prokaryotic zinc finger to use different combinations of residues to properly coordinate the structural metal ion, we provide the UV-Vis characterization of Co(II) addition to Ros87 and its mutant Ros87_C27D which bears an unusual CysAspHis2 coordination sphere. Metals 143-148 mitochondrially encoded cytochrome c oxidase II Homo sapiens 196-202 27725279-1 2016 Mononuclear transition metal complexes of Cu(II), Co(II) and Ni(II) with a newly synthesised macrocyclic ligand derived from 1, 4-dicarbonyl-phenyl-dihydrazide and 1,2-diphenylethane-1,2-dione (2:2) have been synthesised. Metals 23-28 mitochondrially encoded cytochrome c oxidase II Homo sapiens 50-56 27731868-3 2016 Among metal ions studied, Cr(iii), Mn(ii), Fe(ii), Co(ii), Cu(ii) and Zn(ii) were found to enhance the photocurrent by 30-300%; whereas photocurrent density significantly dropped by 90% in Ni(ii) solution after 90 min of illumination. Metals 6-11 mitochondrially encoded cytochrome c oxidase II Homo sapiens 29-31 27731868-3 2016 Among metal ions studied, Cr(iii), Mn(ii), Fe(ii), Co(ii), Cu(ii) and Zn(ii) were found to enhance the photocurrent by 30-300%; whereas photocurrent density significantly dropped by 90% in Ni(ii) solution after 90 min of illumination. Metals 6-11 mitochondrially encoded cytochrome c oxidase II Homo sapiens 38-40 27731868-3 2016 Among metal ions studied, Cr(iii), Mn(ii), Fe(ii), Co(ii), Cu(ii) and Zn(ii) were found to enhance the photocurrent by 30-300%; whereas photocurrent density significantly dropped by 90% in Ni(ii) solution after 90 min of illumination. Metals 6-11 mitochondrially encoded cytochrome c oxidase II Homo sapiens 51-57 27731868-3 2016 Among metal ions studied, Cr(iii), Mn(ii), Fe(ii), Co(ii), Cu(ii) and Zn(ii) were found to enhance the photocurrent by 30-300%; whereas photocurrent density significantly dropped by 90% in Ni(ii) solution after 90 min of illumination. Metals 6-11 mitochondrially encoded cytochrome c oxidase II Homo sapiens 38-40 27731868-3 2016 Among metal ions studied, Cr(iii), Mn(ii), Fe(ii), Co(ii), Cu(ii) and Zn(ii) were found to enhance the photocurrent by 30-300%; whereas photocurrent density significantly dropped by 90% in Ni(ii) solution after 90 min of illumination. Metals 6-11 mitochondrially encoded cytochrome c oxidase II Homo sapiens 38-40 27731868-3 2016 Among metal ions studied, Cr(iii), Mn(ii), Fe(ii), Co(ii), Cu(ii) and Zn(ii) were found to enhance the photocurrent by 30-300%; whereas photocurrent density significantly dropped by 90% in Ni(ii) solution after 90 min of illumination. Metals 6-11 mitochondrially encoded cytochrome c oxidase II Homo sapiens 38-40 27420328-3 2016 The tandem repeats of the Cysteine-Glycine-Histidine (CGH) metal ion binding motif exhibited concerted binding to Co(II) ions, suggesting that conformational transition of peptide was triggered by the sequential metal ion binding. Metals 59-64 mitochondrially encoded cytochrome c oxidase II Homo sapiens 114-120 27420328-3 2016 The tandem repeats of the Cysteine-Glycine-Histidine (CGH) metal ion binding motif exhibited concerted binding to Co(II) ions, suggesting that conformational transition of peptide was triggered by the sequential metal ion binding. Metals 212-217 mitochondrially encoded cytochrome c oxidase II Homo sapiens 114-120 27420328-4 2016 Evaluation of the free thiol content after reduction by reducing reagent showed that metal-ion binding elicited strong retardation of cysteine oxidation in the order of Zn(II)>Ni(II)>Co(II). Metals 85-90 mitochondrially encoded cytochrome c oxidase II Homo sapiens 189-195 26509841-1 2015 Subcomponent self-assembly of two isomeric bis(3-aminophenyl)pyrenes, 2-formylpyridine and the metal ions Fe(II), Co(II), and Zn(II) led to the formation of two previously unidentified structure types: a C2-symmetric M(II)4L6 assembly with meridionally coordinated metal centers, and a C3-symmetric self-included M(II)4L6 assembly with facially coordinated metal centers. Metals 95-100 mitochondrially encoded cytochrome c oxidase II Homo sapiens 114-119 27088506-1 2016 To estimate the biological preference of synthetic small drugs towards DNA target, new metal based chemotherapeutic agents of nano-sized Cr(III), Fe(II), Co(II) and Ni(II) Schiff base complexes having N,N,O donor system were synthesized and thoroughly characterized by physic-chemical techniques. Metals 87-92 mitochondrially encoded cytochrome c oxidase II Homo sapiens 154-160 27151823-3 2016 The structures of and consist of two-dimensional grids of cobalt(ii) ions where each metal atom is linked to the other four metal centres by single dca bridges exhibiting the mu1,5-dca coordination mode [Co-Ndca = 2.190(3)-2.220(3) () and 2.127(3)-2.153(3) A ()]. Metals 85-90 mitochondrially encoded cytochrome c oxidase II Homo sapiens 65-67 27151823-3 2016 The structures of and consist of two-dimensional grids of cobalt(ii) ions where each metal atom is linked to the other four metal centres by single dca bridges exhibiting the mu1,5-dca coordination mode [Co-Ndca = 2.190(3)-2.220(3) () and 2.127(3)-2.153(3) A ()]. Metals 124-129 mitochondrially encoded cytochrome c oxidase II Homo sapiens 65-67 27054774-2 2016 Herein 3D chiral and 2D achiral cobalt(ii) coordination compounds based on single metal nodes with a 4-(benzimidazole-1-yl)benzoic acid (Hbmzbc) ligand, namely, [Co(bmzbc)2(1,2-etdio)]n () (1,2-etdio = 1,2-ethanediol) and [Co(bmzbc)2(Hbmzbc)]n (), have been synthesized and structurally characterized. Metals 82-87 mitochondrially encoded cytochrome c oxidase II Homo sapiens 39-41 26900671-2 2016 Subsequently, single-crystal-to-single-crystal metal cation exchange using the constructed MOF is investigated, and the results show that Cu(II) and Co(II) ions can selectively be introduced into the MOF without compromising the crystallinity of the pristine framework. Metals 47-52 mitochondrially encoded cytochrome c oxidase II Homo sapiens 149-155 27375886-4 2016 The metal-metal distance is very close to that in a related compound exhibiting weak anti-ferromagnetic exchange between the Co(II) ions, and the title compound can thus be useful for obtaining more information about the contribution of different bridges to the magnetic coupling between paramagnetic ions. Metals 4-9 mitochondrially encoded cytochrome c oxidase II Homo sapiens 125-131 27375886-4 2016 The metal-metal distance is very close to that in a related compound exhibiting weak anti-ferromagnetic exchange between the Co(II) ions, and the title compound can thus be useful for obtaining more information about the contribution of different bridges to the magnetic coupling between paramagnetic ions. Metals 10-15 mitochondrially encoded cytochrome c oxidase II Homo sapiens 125-131 26820843-6 2016 The subsequent oxidation of the Co(II) ions inside the macrocycle into Co(III) ions made the metal-ligand bonds almost inert, thus affording a kinetically locked 4 : 4 metallomacrocycle. Metals 93-98 mitochondrially encoded cytochrome c oxidase II Homo sapiens 32-38 26701372-2 2016 Depending on the electronic effects of the substituents on the ligand, the redox of the metal center was systematically modulated, and the magnetic behavior from essentially high-spin Co(II) in 3 versus completely diamagnetic Co(III) in 1 to Co(II) spin-crossover in 2 can be achieved. Metals 88-93 mitochondrially encoded cytochrome c oxidase II Homo sapiens 184-190 27273116-6 2016 While maintains near-TP configurations in the presence of metal ions with strong octahedral preferences, distorts towards predominantly octahedral co-ordination geometries, increasing in the order Co(II) < Ni(II) < Fe(II) and no trigonal prismatic structures. Metals 58-63 mitochondrially encoded cytochrome c oxidase II Homo sapiens 197-203 27243450-1 2016 The ionic liquid trihexyl(tetradecyl)phosphonium thiocyanate has been used for the extraction of the transition metal ions Co(ii), Ni(ii), Zn(ii), and the rare-earth ions La(iii), Sm(iii) and Eu(iii) from aqueous solutions containing nitrate or chloride salts. Metals 112-117 mitochondrially encoded cytochrome c oxidase II Homo sapiens 123-129 27243450-1 2016 The ionic liquid trihexyl(tetradecyl)phosphonium thiocyanate has been used for the extraction of the transition metal ions Co(ii), Ni(ii), Zn(ii), and the rare-earth ions La(iii), Sm(iii) and Eu(iii) from aqueous solutions containing nitrate or chloride salts. Metals 112-117 mitochondrially encoded cytochrome c oxidase II Homo sapiens 126-128 27243450-1 2016 The ionic liquid trihexyl(tetradecyl)phosphonium thiocyanate has been used for the extraction of the transition metal ions Co(ii), Ni(ii), Zn(ii), and the rare-earth ions La(iii), Sm(iii) and Eu(iii) from aqueous solutions containing nitrate or chloride salts. Metals 112-117 mitochondrially encoded cytochrome c oxidase II Homo sapiens 134-136 27386557-1 2016 Metal-free carbon-based electrocatalysts for dye-sensitized solar cells (DSSCs) are sufficiently active in Co(II)/Co(III) electrolytes but are not satisfactory in the most commonly used iodide/triiodide (I(-)/I3 (-)) electrolytes. Metals 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 107-113 29997819-3 2016 Emphasis was given to the spectroscopic investigation of the coordination preferences and spin configurations among the different 3d6 CoIII, 3d7 CoII, and 3d8 CoI oxidation states of the metal, and to the catalytic proton reduction with an evaluation of the pathways for the generation of H2via CoIII-H- or CoII-H- intermediates by mono and bimetallic routes. Metals 187-192 mitochondrially encoded cytochrome c oxidase II Homo sapiens 134-138 29997819-3 2016 Emphasis was given to the spectroscopic investigation of the coordination preferences and spin configurations among the different 3d6 CoIII, 3d7 CoII, and 3d8 CoI oxidation states of the metal, and to the catalytic proton reduction with an evaluation of the pathways for the generation of H2via CoIII-H- or CoII-H- intermediates by mono and bimetallic routes. Metals 187-192 mitochondrially encoded cytochrome c oxidase II Homo sapiens 145-149 26754960-1 2016 The generation, under self-assembly conditions, of coordination polymers on surface based combinations of a terpyridine-antracene-pyridine based tecton and Co(II) or Pd(II) cations is primarily governed by the coordination geometry of the metal center (octahedral and square planar respectively). Metals 239-244 mitochondrially encoded cytochrome c oxidase II Homo sapiens 156-162 26716610-1 2016 Paramagnetic Fe(II) and Co(II) complexes are utilized as the first transition metal examples of (1)H NMR shift agents (paraSHIFT) for thermometry applications using Magnetic Resonance Spectroscopy (MRS). Metals 78-83 mitochondrially encoded cytochrome c oxidase II Homo sapiens 24-30 26716933-10 2016 Metal-centered oxidations were exhibited for all of the Co(II) porphyrins and an M(II)/M(III) process was also observed to occur for NiOPP(R) (R = CH2OH, H, CHO, and NO2) and CuOPP(NO2)(CN)2. Metals 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 56-61 26454381-5 2016 The addition of Co(II) and Cu(II) solutions to the l-Tyr AgNPs also induces a paramagnetic quenching of the fluorescence in the PL spectra and the related Stern Volmer plots highlight a linear correlation over the whole concentration range for both metal ions, with a more pronounced effect for the copper(II) ion. Metals 249-254 mitochondrially encoded cytochrome c oxidase II Homo sapiens 16-22 26509841-1 2015 Subcomponent self-assembly of two isomeric bis(3-aminophenyl)pyrenes, 2-formylpyridine and the metal ions Fe(II), Co(II), and Zn(II) led to the formation of two previously unidentified structure types: a C2-symmetric M(II)4L6 assembly with meridionally coordinated metal centers, and a C3-symmetric self-included M(II)4L6 assembly with facially coordinated metal centers. Metals 265-270 mitochondrially encoded cytochrome c oxidase II Homo sapiens 114-119 26509841-1 2015 Subcomponent self-assembly of two isomeric bis(3-aminophenyl)pyrenes, 2-formylpyridine and the metal ions Fe(II), Co(II), and Zn(II) led to the formation of two previously unidentified structure types: a C2-symmetric M(II)4L6 assembly with meridionally coordinated metal centers, and a C3-symmetric self-included M(II)4L6 assembly with facially coordinated metal centers. Metals 265-270 mitochondrially encoded cytochrome c oxidase II Homo sapiens 114-119 26406288-5 2015 All four cages have been structurally characterised: in the Ru(ii)/Cd(ii) cage (reported in a recent communication) the Ru(ii) and Cd(ii) ions are crystallographically distinct; in the other three cages [Ru(ii)/Co(ii), Os(ii)/Cd(ii) and Os(ii)/Co(ii), reported here] the ions are disordered around the periphery such that every metal site refines as a 50 : 50 mixture of the two metal atom types. Metals 328-333 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-72 26406288-5 2015 All four cages have been structurally characterised: in the Ru(ii)/Cd(ii) cage (reported in a recent communication) the Ru(ii) and Cd(ii) ions are crystallographically distinct; in the other three cages [Ru(ii)/Co(ii), Os(ii)/Cd(ii) and Os(ii)/Co(ii), reported here] the ions are disordered around the periphery such that every metal site refines as a 50 : 50 mixture of the two metal atom types. Metals 328-333 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-72 26406288-5 2015 All four cages have been structurally characterised: in the Ru(ii)/Cd(ii) cage (reported in a recent communication) the Ru(ii) and Cd(ii) ions are crystallographically distinct; in the other three cages [Ru(ii)/Co(ii), Os(ii)/Cd(ii) and Os(ii)/Co(ii), reported here] the ions are disordered around the periphery such that every metal site refines as a 50 : 50 mixture of the two metal atom types. Metals 328-333 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-72 26406288-5 2015 All four cages have been structurally characterised: in the Ru(ii)/Cd(ii) cage (reported in a recent communication) the Ru(ii) and Cd(ii) ions are crystallographically distinct; in the other three cages [Ru(ii)/Co(ii), Os(ii)/Cd(ii) and Os(ii)/Co(ii), reported here] the ions are disordered around the periphery such that every metal site refines as a 50 : 50 mixture of the two metal atom types. Metals 328-333 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-72 26406288-5 2015 All four cages have been structurally characterised: in the Ru(ii)/Cd(ii) cage (reported in a recent communication) the Ru(ii) and Cd(ii) ions are crystallographically distinct; in the other three cages [Ru(ii)/Co(ii), Os(ii)/Cd(ii) and Os(ii)/Co(ii), reported here] the ions are disordered around the periphery such that every metal site refines as a 50 : 50 mixture of the two metal atom types. Metals 328-333 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-72 26406288-5 2015 All four cages have been structurally characterised: in the Ru(ii)/Cd(ii) cage (reported in a recent communication) the Ru(ii) and Cd(ii) ions are crystallographically distinct; in the other three cages [Ru(ii)/Co(ii), Os(ii)/Cd(ii) and Os(ii)/Co(ii), reported here] the ions are disordered around the periphery such that every metal site refines as a 50 : 50 mixture of the two metal atom types. Metals 328-333 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-72 26406288-5 2015 All four cages have been structurally characterised: in the Ru(ii)/Cd(ii) cage (reported in a recent communication) the Ru(ii) and Cd(ii) ions are crystallographically distinct; in the other three cages [Ru(ii)/Co(ii), Os(ii)/Cd(ii) and Os(ii)/Co(ii), reported here] the ions are disordered around the periphery such that every metal site refines as a 50 : 50 mixture of the two metal atom types. Metals 328-333 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-72 26406288-5 2015 All four cages have been structurally characterised: in the Ru(ii)/Cd(ii) cage (reported in a recent communication) the Ru(ii) and Cd(ii) ions are crystallographically distinct; in the other three cages [Ru(ii)/Co(ii), Os(ii)/Cd(ii) and Os(ii)/Co(ii), reported here] the ions are disordered around the periphery such that every metal site refines as a 50 : 50 mixture of the two metal atom types. Metals 379-384 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-72 26406288-5 2015 All four cages have been structurally characterised: in the Ru(ii)/Cd(ii) cage (reported in a recent communication) the Ru(ii) and Cd(ii) ions are crystallographically distinct; in the other three cages [Ru(ii)/Co(ii), Os(ii)/Cd(ii) and Os(ii)/Co(ii), reported here] the ions are disordered around the periphery such that every metal site refines as a 50 : 50 mixture of the two metal atom types. Metals 379-384 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-72 26406288-5 2015 All four cages have been structurally characterised: in the Ru(ii)/Cd(ii) cage (reported in a recent communication) the Ru(ii) and Cd(ii) ions are crystallographically distinct; in the other three cages [Ru(ii)/Co(ii), Os(ii)/Cd(ii) and Os(ii)/Co(ii), reported here] the ions are disordered around the periphery such that every metal site refines as a 50 : 50 mixture of the two metal atom types. Metals 379-384 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-72 26406288-5 2015 All four cages have been structurally characterised: in the Ru(ii)/Cd(ii) cage (reported in a recent communication) the Ru(ii) and Cd(ii) ions are crystallographically distinct; in the other three cages [Ru(ii)/Co(ii), Os(ii)/Cd(ii) and Os(ii)/Co(ii), reported here] the ions are disordered around the periphery such that every metal site refines as a 50 : 50 mixture of the two metal atom types. Metals 379-384 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-72 26406288-5 2015 All four cages have been structurally characterised: in the Ru(ii)/Cd(ii) cage (reported in a recent communication) the Ru(ii) and Cd(ii) ions are crystallographically distinct; in the other three cages [Ru(ii)/Co(ii), Os(ii)/Cd(ii) and Os(ii)/Co(ii), reported here] the ions are disordered around the periphery such that every metal site refines as a 50 : 50 mixture of the two metal atom types. Metals 379-384 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-72 26406288-5 2015 All four cages have been structurally characterised: in the Ru(ii)/Cd(ii) cage (reported in a recent communication) the Ru(ii) and Cd(ii) ions are crystallographically distinct; in the other three cages [Ru(ii)/Co(ii), Os(ii)/Cd(ii) and Os(ii)/Co(ii), reported here] the ions are disordered around the periphery such that every metal site refines as a 50 : 50 mixture of the two metal atom types. Metals 379-384 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-72 26406288-5 2015 All four cages have been structurally characterised: in the Ru(ii)/Cd(ii) cage (reported in a recent communication) the Ru(ii) and Cd(ii) ions are crystallographically distinct; in the other three cages [Ru(ii)/Co(ii), Os(ii)/Cd(ii) and Os(ii)/Co(ii), reported here] the ions are disordered around the periphery such that every metal site refines as a 50 : 50 mixture of the two metal atom types. Metals 379-384 mitochondrially encoded cytochrome c oxidase II Homo sapiens 70-72 26406288-6 2015 The incorporation of Os(ii) units into the cages results in both redox activity [a reversible Os(ii)/Os(iii) couple for all four metal ions simultaneously, at a modest potential] and luminescence [the Os(ii) units have luminescent (3)MLCT excited states which will be good photo-electron donors] being incorporated into the cage superstructure. Metals 129-134 mitochondrially encoded cytochrome c oxidase II Homo sapiens 24-26 26406288-6 2015 The incorporation of Os(ii) units into the cages results in both redox activity [a reversible Os(ii)/Os(iii) couple for all four metal ions simultaneously, at a modest potential] and luminescence [the Os(ii) units have luminescent (3)MLCT excited states which will be good photo-electron donors] being incorporated into the cage superstructure. Metals 129-134 mitochondrially encoded cytochrome c oxidase II Homo sapiens 97-99 26406288-6 2015 The incorporation of Os(ii) units into the cages results in both redox activity [a reversible Os(ii)/Os(iii) couple for all four metal ions simultaneously, at a modest potential] and luminescence [the Os(ii) units have luminescent (3)MLCT excited states which will be good photo-electron donors] being incorporated into the cage superstructure. Metals 129-134 mitochondrially encoded cytochrome c oxidase II Homo sapiens 97-99 26225623-3 2015 With such simple fabricating means to form good-quality films, polyCo films show stable switching at the central metal ion of the Co(II)/Co(I) redox reaction when immersed in aqueous solution. Metals 113-118 mitochondrially encoded cytochrome c oxidase II Homo sapiens 130-136 26056978-2 2015 In this work benzimidazole based metal organic thin films of dichlorobis (1H-Benzimidazole) Co(II) and dichlorobis (1H-Benzimidazole) Cu(II) were deposited by chemical bath deposition method. Metals 33-38 mitochondrially encoded cytochrome c oxidase II Homo sapiens 92-98 26324662-1 2015 A new type of homochiral metal-organic nanotubular structures based on metal phosphonates are reported, namely, (R)- or (S)-[M(pemp)(H2O)2][M = Co(II) (1), Ni(II) (2)] [pemp(2-) = (R)- or (S)-(1-phenylethylamino)methylphosphonate]. Metals 25-30 mitochondrially encoded cytochrome c oxidase II Homo sapiens 144-150 26279265-0 2015 Spontaneous symmetry breaking of Co(II) metal-organic frameworks from achiral precursors via asymmetrical crystallization. Metals 40-45 mitochondrially encoded cytochrome c oxidase II Homo sapiens 33-39 33435084-4 2015 It was confirmed that both Co(II) and Cr(III) ions, and their combination, at concentrations relevant for the metal release situation, resulted in protein aggregation and its concomitant precipitation, which increased the friction coefficient. Metals 110-115 mitochondrially encoded cytochrome c oxidase II Homo sapiens 27-33 25706679-2 2015 The synthesized Schiff bases were used for complexation with different metal ions like Co(II), Ni(II) and Cu(II) by using a molar ratio of ligand: metal as 2:1. Metals 71-76 mitochondrially encoded cytochrome c oxidase II Homo sapiens 87-93 25841152-3 2015 The thermal activation energies of decomposition (Ea) of HL and its metal complexes with Cu(II), Co(II) and Ni(II) are found to be 48.76, 36.83, 30.59 and 40.45 kJ/mol, respectively. Metals 68-73 mitochondrially encoded cytochrome c oxidase II Homo sapiens 97-103 26018933-4 2015 The mutants allow us to demonstrate convincingly the preparation of a mixed-metal analogue, Co(C)Zn(S)-MMP-1, with Zn(II) in the structural site and Co(II) in the catalytic site. Metals 76-81 mitochondrially encoded cytochrome c oxidase II Homo sapiens 149-155 25706679-2 2015 The synthesized Schiff bases were used for complexation with different metal ions like Co(II), Ni(II) and Cu(II) by using a molar ratio of ligand: metal as 2:1. Metals 147-152 mitochondrially encoded cytochrome c oxidase II Homo sapiens 87-93 25623286-0 2015 Inter-ligand azo (N=N) unit formation and stabilization of a Co(II)-diradical complex via metal-to-ligand dpi-ppi* back donation: synthesis, characterization, and theoretical study. Metals 90-95 mitochondrially encoded cytochrome c oxidase II Homo sapiens 61-67 25743249-1 2015 A pair of supramolecular isomers of Co(II)-based metal-organic frameworks can be directionally constructed in virtue of solvent templates, which show diverse bilayer networks and lattice packing with the same Co3 SBUs and organic linkers. Metals 49-54 mitochondrially encoded cytochrome c oxidase II Homo sapiens 36-41 25804832-9 2015 The nanosensor exhibits high selectivity toward Co(II) ions in comparison with common metal ions. Metals 86-91 mitochondrially encoded cytochrome c oxidase II Homo sapiens 48-54 25666328-3 2015 Metal complexes are like [M(AMTA)2], [M(ATA)2] type, where M=Mn(II), Co(II) and Cu(II). Metals 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 69-75 25686861-5 2015 The detection of H-bonding (OH O) in the [M(LH)2] metal complexes by IR spectra supported the square-planar MN4 coordination of Ni(II), Cu(II) and Co(II) complexes. Metals 50-55 mitochondrially encoded cytochrome c oxidase II Homo sapiens 147-153 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. Metals 4-9 mitochondrially encoded cytochrome c oxidase II Homo sapiens 96-102 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. Metals 77-82 mitochondrially encoded cytochrome c oxidase II Homo sapiens 96-102 25490374-2 2015 Subsequently metal complexes of the type [MLX2] and [CuL]X2; (M=Mn(II), Co(II), Ni(II) and Zn(II); X=Cl or NO3) were synthesized by the reaction of the free macrocyclic ligand (L) with the corresponding metal salts in 1:1 molar ratio. Metals 13-18 mitochondrially encoded cytochrome c oxidase II Homo sapiens 72-78 25064505-1 2015 Metal complexes of the chloride, nitrate and acetate salts of Co(II), Ni(II) Cu(II), Zn(II), Cd(II) or Hg(II) with 2,3-butanedione bis(isonicotinylhydrazone) [BBINH] have been synthesized and structurally characterized. Metals 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 62-68 25531180-2 2015 The list of metal ions studied here includes Zn(II), Cd(II), Ni(II), Co(II), and Cu(I). Metals 12-17 mitochondrially encoded cytochrome c oxidase II Homo sapiens 69-74 25494338-1 2015 The possibility of employing the mechanism of intramolecular electron transfer between metal and ligand centers in the valence tautomeric complexes formed as electrically neutral 2 : 1 adducts of Co(II) diketonates and redox-active tetradentate di-o-quinones, for quantum information processing, has been computationally studied using the DFT B3LYP*/6-311++G(d,p) method. Metals 87-92 mitochondrially encoded cytochrome c oxidase II Homo sapiens 196-201 26163785-1 2015 Mononuclear transition metal complexes of Mn(II), Co(II), Ni(II), Cu(II), Zn(II) and Cd(II) with a new hydrazone ligand derived from pyrazine-2-carbohydrazide and 2-hydroxyacetophenone have been synthesized. Metals 23-28 mitochondrially encoded cytochrome c oxidase II Homo sapiens 50-56 25472020-1 2014 Five novel metal organic frameworks were obtained by hydro-solvothermal reactions using the hexafluorisopropylidenebis(benzoic) acid (H2hfipbb) as linker and Co(II) or Mn(II) ions as connectors. Metals 11-16 mitochondrially encoded cytochrome c oxidase II Homo sapiens 158-164 25356958-1 2014 This study examines metal binding to metallo-beta-lactamase VIM-2, demonstrating the first successful preparation of a Co(II)-substituted VIM-2 analogue. Metals 20-25 mitochondrially encoded cytochrome c oxidase II Homo sapiens 119-125 25356958-2 2014 Spectroscopic studies of the half- and fully metal loaded enzymes show that both Zn(II) and Co(II) bind cooperatively, where the major species present, regardless of stoichiometry, are apo- and di-Zn (or di-Co) enzymes. Metals 45-50 mitochondrially encoded cytochrome c oxidase II Homo sapiens 92-98 25034144-8 2014 Immobilized- Cr(III) and Co(II) affinity chromatography indicated that metal ions can also directly bind to several metallo and non-metalloproteins and, as demonstrated for aldolase and catalase, induce loss of their biological function. Metals 71-76 mitochondrially encoded cytochrome c oxidase II Homo sapiens 25-31 25148569-0 2014 Cooperative metal-ligand assisted E/Z isomerization and cyano activation at Cu(II) and Co(II) complexes of arylhydrazones of active methylene nitriles. Metals 12-17 mitochondrially encoded cytochrome c oxidase II Homo sapiens 87-93 24815057-1 2014 The novel metal-based molecular entities {Cu(II), Ni(II) and Co(II)} 1-3, respectively were synthesized and characterized by elemental analysis and spectroscopic methods (IR, (1)H and (13)C NMR, EPR, UV-vis, ESI-MS and XRPD). Metals 10-15 mitochondrially encoded cytochrome c oxidase II Homo sapiens 61-67 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). Metals 128-133 mitochondrially encoded cytochrome c oxidase II Homo sapiens 12-18 24815057-0 2014 Synthesis and characterization of new transition metal {Cu(II), Ni(II) and Co(II)} L-phenylalanine-DACH conjugate complexes: in vitro DNA binding, cleavage and molecular docking studies. Metals 49-54 mitochondrially encoded cytochrome c oxidase II Homo sapiens 75-81 24507930-4 2014 Each compound can undergo two metal-centered one-electron reductions leading to formation of Co(II) and Co(I) derivatives in CH2Cl2 or pyridine containing 0.1 M tetra-n-butylammonium perchlorate (TBAP). Metals 30-35 mitochondrially encoded cytochrome c oxidase II Homo sapiens 93-99 24754678-3 2014 This marks the first preparation of a metallo-beta-lactamase selectively substituted with a paramagnetic metal ion, Co(II), either in the Zn1 (CoCd-NDM-1) or in the Zn2 site (ZnCo-NDM-1), as well as both (CoCo-NDM-1). Metals 38-43 mitochondrially encoded cytochrome c oxidase II Homo sapiens 116-122 24162794-0 2014 An unprecedented Co(II) cuboctahedron as the secondary building unit in a Co-based metal-organic framework. Metals 83-88 mitochondrially encoded cytochrome c oxidase II Homo sapiens 17-23 24601533-2 2014 The metal center Co(II) ion in each complex shows a similar distorted octahedral geometry. Metals 4-9 mitochondrially encoded cytochrome c oxidase II Homo sapiens 17-23 24611507-1 2014 We report the synthesis, structure, and sorption properties of a family of eight diamondoid (dia) metal-organic materials (MOMs) that are sustained by Co(II) or Zn(II) cations linked by one of three rigid ligands: 4-(2-(4-pyridyl)ethenyl)benzoate (1), 4-(pyridin-4-yl)benzoate (2), and 4-(pyridin-4-yl)acrylate (3). Metals 98-103 mitochondrially encoded cytochrome c oxidase II Homo sapiens 151-157 24604763-4 2014 The initially formed states of 1 a and 3 a are considered to result from metal-to-polyoxometalate charge transfer (MPCT) from Co(II) to W, while the longer-lived excited state of 1 a is tentatively assigned to a localized intermediate MPCT state. Metals 73-78 mitochondrially encoded cytochrome c oxidase II Homo sapiens 126-132 24125042-1 2014 A multidentate ligand platform is introduced that enables the isolation of both homo- and heterobimetallic complexes of divalent first-row transition metal ions such as Mn(II), Fe(II), and Co(II). Metals 98-103 mitochondrially encoded cytochrome c oxidase II Homo sapiens 189-195 24437997-0 2014 High nuclearity (octa-, dodeca-, and pentadecanuclear) metal (M = Co(II), Ni(II)) phosphonate cages: synthesis, structure, and magnetic behavior. Metals 55-60 mitochondrially encoded cytochrome c oxidase II Homo sapiens 66-72 24695963-2 2014 Individual members of this large family of repressors coordinate Cu(I) or Ni(II)/Co(II) or perform cysteine sulfur chemistry in mitigating the effects of metal or metabolite toxicity, respectively. Metals 154-159 mitochondrially encoded cytochrome c oxidase II Homo sapiens 81-87 24592203-2 2014 Metal complexes of the Schiff base were prepared from their chloride salts of Co(II), Ni(II), Cu(II), Cd(II), and Hg(II) in ethanol. Metals 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 78-84 24394438-6 2014 The UV-visible-near IR spectroscopies and magnetic moment data for the Co(II) and Ni(II) complexes indicated a tetragonal distorted coordination geometry for both metal centres. Metals 163-168 mitochondrially encoded cytochrome c oxidase II Homo sapiens 71-88 25371658-5 2014 Metal-ligand stability constants fall in the order of Cu(II) > Co(II) > Ni(II) which is in agreement with those reported by Irving stability order. Metals 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 66-72 23897214-2 2013 The isolation and characterization of four coordination polymers obtained by direct reactions of metal ion salts of Cu(II), Co(II) and Fe(II) with pyrazine (pyz) and benzoic/benzoate (Bz) ligands under hydrothermal or hydrothermal microwave conditions are described. Metals 97-102 mitochondrially encoded cytochrome c oxidase II Homo sapiens 124-130 24176919-8 2014 Conditional complex stability constant determinations for Dp44mT with Cu(II), Co(II), Fe(II), Ni(II) and Zn(II) revealed that the metal-to-ligand ratio is 1:1 in [Cu(II)Dp44mT] complex, while for Co(II), Fe(II) and Ni(II) is 1:2. Metals 130-135 mitochondrially encoded cytochrome c oxidase II Homo sapiens 196-202 24231744-5 2014 Among all the metal ions investigated, only Co(II) ions gives sharp colour change from ruby red to blue and is easily detectable by naked-eye. Metals 14-19 mitochondrially encoded cytochrome c oxidase II Homo sapiens 44-50 24068677-12 2013 Thus, carcinogenicity of soluble Co(II) could be related to high survival of metal-loaded cells, which permits accumulation of genetic and epigenetic abnormalities. Metals 77-82 mitochondrially encoded cytochrome c oxidase II Homo sapiens 33-39 23508380-3 2013 Attempts to prepare Co(II) dibenzyl complexes with bulky IPr coligands led to metal reduction to Co(I) and aromatic C-H activation and C-C coupling between the benzyl groups. Metals 78-83 mitochondrially encoded cytochrome c oxidase II Homo sapiens 20-26 23807426-0 2013 Unusual composition dependence of magnetic relaxation for Co(II)(1-x)Ni(II)(x) chain-based metal-organic frameworks. Metals 91-96 mitochondrially encoded cytochrome c oxidase II Homo sapiens 58-64 23454738-1 2013 In this work, based on electronic spinning resonance and chemiluminescence (CL) measurements, it is found that the reaction kinetics of Co(II)-triggered Fenton-like reaction is much faster than those of other transition metal ions, which facilitates the observation of the strong CL signals from Co(II). Metals 220-225 mitochondrially encoded cytochrome c oxidase II Homo sapiens 136-141 23454738-1 2013 In this work, based on electronic spinning resonance and chemiluminescence (CL) measurements, it is found that the reaction kinetics of Co(II)-triggered Fenton-like reaction is much faster than those of other transition metal ions, which facilitates the observation of the strong CL signals from Co(II). Metals 220-225 mitochondrially encoded cytochrome c oxidase II Homo sapiens 136-142 23535906-1 2013 The dinucleating ligand L (1,3-bis[bis(pyridin-2-ylmethyl)amino]propan-2-ol) combined with metal ions efficiently cleaves DNA when M : L is 1 : 1 (M = Co(II) or Fe(III)) at pH 5.5-7.0, with free L being more active at acidic pH than when bound to Zn(II), Cu(II) or Ni(II) at neutral pH. Metals 91-96 mitochondrially encoded cytochrome c oxidase II Homo sapiens 151-157 23631353-2 2013 Previous studies mainly focused on the development of highly efficient catalysts, while rare reports concerned the mechanistic understanding of metal valence change, associated with the formation of inactive Co(II)-Salen complex. Metals 144-149 mitochondrially encoded cytochrome c oxidase II Homo sapiens 208-214 23508268-3 2013 Structural analysis shows that in 1 the capped-octahedral environment around the Co(II) centers is highly distorted with rather long bonds between the metal and donor atoms. Metals 151-156 mitochondrially encoded cytochrome c oxidase II Homo sapiens 81-87 23001132-8 2012 Time resolved spectroscopic measurements were performed on compound 6, which proved an intramolecular electron transfer from an excited Ru(II) metal centre to the Co(II) metal centre via the bridging L-pyr ligand. Metals 143-148 mitochondrially encoded cytochrome c oxidase II Homo sapiens 163-169 22715144-6 2013 Under optimized conditions, the calibration curve of metal ions was linear over the range of 2.0 x 10(-8) to 2.0 x 10(-5) M for Co(II), 1.0 x 10(-7) to 2.0 x 10(-5) M for Fe (II) and 2.0 x 10(-7) to 1.0 x 10(-4) M for Cr(III). Metals 53-58 mitochondrially encoded cytochrome c oxidase II Homo sapiens 128-133 23243667-4 2013 The Me2Cyclen base is always involved in the coordination of the transition metal cation with the four amine functions; both side-arms bind Co(II) while only one of them binds Cu(II). Metals 76-81 mitochondrially encoded cytochrome c oxidase II Homo sapiens 140-146 23266605-3 2013 The metal complexes with Cr(III), Mn(II), Fe(III), Co(II), Ni(II), Cu(II), Zn(II) and Th(IV) have been prepared and characterized by elemental analyses, IR and (1)H-NMR spectroscopy, thermal and magnetic measurements. Metals 4-9 mitochondrially encoded cytochrome c oxidase II Homo sapiens 51-57 23317083-6 2013 Cyclic voltammetry studies reveal that the reduction of the complex bound Mn(II), Co(II), and Zn(II) ions is a ligand-centered process whereas the first oxidation step depends on the metal ion present. Metals 183-188 mitochondrially encoded cytochrome c oxidase II Homo sapiens 82-87 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. Metals 2-7 mitochondrially encoded cytochrome c oxidase II Homo sapiens 44-50 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. Metals 196-201 mitochondrially encoded cytochrome c oxidase II Homo sapiens 213-219 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. Metals 340-345 mitochondrially encoded cytochrome c oxidase II Homo sapiens 213-219 23165737-0 2013 Bipyridine and phenanthroline IR-spectral bands as indicators of metal spin state in hexacoordinated complexes of Fe(II), Ni(II) and Co(II). Metals 65-70 mitochondrially encoded cytochrome c oxidase II Homo sapiens 133-139 23172152-1 2013 We report a catalytic eight-cobalt-capped alpha-Keggin polyoxoazocobaltite with a highly symmetric structure completely constructed from the late transition-metal Co(II) as a poly atom, [Co(20)(OH)(24)(MMT)(12)(SO(4))](NO(3))(2) 6H(2)O (1) (MMT: 2-mercapto-5-methyl-1,3,4-thiadiazole). Metals 157-162 mitochondrially encoded cytochrome c oxidase II Homo sapiens 163-168 23749135-5 2013 The metal ions were extracted through complexation with 8-hydroxyquinoline in the organic-rich phase with distribution constants and extraction percentage values, respectively, of 0.47 and 74 for Fe(III), 0.15 and 47 for Co(II), and 0.08 and 32 for Ni(II). Metals 4-9 mitochondrially encoded cytochrome c oxidase II Homo sapiens 221-226 23007663-1 2012 Reaction of imidazole aldehydes with dihydrazino derivatives of 2-phenylpyrimidine provides a family of bis(acylhydrazone) ligands which form [2 x 2] metallogrid complexes with transition metal ions including Fe(II), Co(II), Cu(II) and Zn(II). Metals 150-155 mitochondrially encoded cytochrome c oxidase II Homo sapiens 217-223 22960784-8 2012 The cyclic voltammogram (CV) displays two one-electron metal based processes: a quasi-reversible Co(III)/Co(II) oxidation wave at E(1/2) = -0.5 V vs. Fc(+)/Fc and a quasi-reversible Co(II)/Co(I) reduction wave at E(1/2) = -1.7 V. 1 reacts with CH(3)I, generating the mono S-methylated complex, [CoL(Me)I] (1(Me)). Metals 55-60 mitochondrially encoded cytochrome c oxidase II Homo sapiens 97-102 22960784-8 2012 The cyclic voltammogram (CV) displays two one-electron metal based processes: a quasi-reversible Co(III)/Co(II) oxidation wave at E(1/2) = -0.5 V vs. Fc(+)/Fc and a quasi-reversible Co(II)/Co(I) reduction wave at E(1/2) = -1.7 V. 1 reacts with CH(3)I, generating the mono S-methylated complex, [CoL(Me)I] (1(Me)). Metals 55-60 mitochondrially encoded cytochrome c oxidase II Homo sapiens 105-111 22998407-6 2012 [Co(II)(mu-OH(2))CaOH(2)](+) contained two aquo ligands, one bonded to the Ca(II) ion and one bridging between the two metal ions, and thus represents an unusual example of a heterobimetallic complex containing two aquo ligands spanning different metal ions. Metals 119-124 mitochondrially encoded cytochrome c oxidase II Homo sapiens 1-7 22998407-6 2012 [Co(II)(mu-OH(2))CaOH(2)](+) contained two aquo ligands, one bonded to the Ca(II) ion and one bridging between the two metal ions, and thus represents an unusual example of a heterobimetallic complex containing two aquo ligands spanning different metal ions. Metals 183-188 mitochondrially encoded cytochrome c oxidase II Homo sapiens 1-7 22491744-1 2012 The redox-active fac-[Mo(V)(mp)(3)](-) (mp: o-mercaptophenolato) bearing asymmetric O- and S-cation binding sites can bind with several kinds of metal ions such as Na(+), Mn(II), Fe(II), Co(II), Ni(II), and Cu(I). Metals 145-150 mitochondrially encoded cytochrome c oxidase II Homo sapiens 187-193 22935596-1 2012 Schiff base ligand, 1,4-bis[(2-hydroxybenzaldehyde)propyl]piperazine (BHPP), and its Cu(II), Ni(II) and Co(II) metal complexes were synthesized and characterized by elemental analysis, magnetic susceptibility, molar conductance and spectral (IR and UV-vis) studies. Metals 111-116 mitochondrially encoded cytochrome c oxidase II Homo sapiens 104-110 22935596-3 2012 Metal complexes are formed in the 1:1 (M:L) ratio as found from the elemental analysis and found to have the general formula [ML] nH(2)O, where M=Co(II), Ni(II) and Cu(II), L=BHPP. Metals 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 146-152 22639389-5 2012 The fluorescence properties of the isostructural capsules were strongly dependent on the identity of the metal species: the Zn(II) capsule emitted strong blue fluorescence with a high quantum yield (Phi=0.8), in sharp contrast to the weakly emissive Ni(II) and Mn(II) capsules and the completely non-emissive Pd(II), Pt(II), and Co(II) capsules. Metals 105-110 mitochondrially encoded cytochrome c oxidase II Homo sapiens 329-335 22450432-2 2012 The complexes are essentially isostructural and isomorphous, allowing the Co(II) and Cu(II) complexes to co-crystallize in mixed-metal solid solutions with the formula [Co(x)Cu(1-x)(DDOP)(NO(3))(H(2)O)](NO(3)), where x = 0.4 (4), 0.1 (5), and 0.7 (6). Metals 129-134 mitochondrially encoded cytochrome c oxidase II Homo sapiens 74-80 22536852-14 2012 Notably, the observed k(2) values (M(-1) s(-1)) for Mn(II) (2a, 0.152), Co(II) (3a, 0.208), and Zn(II) (4a, 0.230) complexes (1a, 0.058; already reported) linearly correlate with Z(eff)/r values of the metal ion. Metals 202-207 mitochondrially encoded cytochrome c oxidase II Homo sapiens 72-78 22505053-1 2012 Trapped in a noble cube: A novel family of noble metalates has been discovered in which a 3d metal ion M (M = Mn(II), Fe(III), Co(II), Cu(II), Zn(II)) is encapsulated by a 12 palladium-oxo cage {Pd(12)O(32)}, which is capped by eight phosphate groups. Metals 49-54 mitochondrially encoded cytochrome c oxidase II Homo sapiens 127-133 22411760-0 2012 Noble metal-free oxidative electrocatalysts: polyaniline and Co(II)-polyaniline nanostructures hosted in nanoporous silica. Metals 6-11 mitochondrially encoded cytochrome c oxidase II Homo sapiens 61-67 22411760-3 2012 Both the metal-free (SBA-15/PANI) and the Co(II)-doped SBA-15/PANI nanocomposite materials showed high electrocatalytic activity for oxidation of L-ascorbic acid, with very low overpotential and high current density. Metals 9-14 mitochondrially encoded cytochrome c oxidase II Homo sapiens 42-48 22342562-3 2012 Those which were most affected by the addition of this metal ion were lactate > formate histidinate > succinate, this order reflecting the ability of these complexants to compete for the available Co(II) in terms of (1) thermodynamic equilibrium constants for the formation of their complexes and (2) their HSS concentrations. Metals 55-60 mitochondrially encoded cytochrome c oxidase II Homo sapiens 204-210 22428925-0 2012 Combination of magnetic susceptibility and electron paramagnetic resonance to monitor the 1D to 2D solid state transformation in flexible metal-organic frameworks of Co(II) and Zn(II) with 1,4-bis(triazol-1-ylmethyl)benzene. Metals 138-143 mitochondrially encoded cytochrome c oxidase II Homo sapiens 166-172 22611346-2 2012 It has been found that the Schiff bases with Cu(II) or Co(II) ion forming binuclear complexes on (1 : 1) "metal : ligand" stoichiometry. Metals 106-111 mitochondrially encoded cytochrome c oxidase II Homo sapiens 55-61 22179398-1 2012 Postsynthetic metal ion exchange in a benzotriazolate-based MFU-4l(arge) framework leads to a Co(II)-containing framework with open metal sites showing reversible gas-phase oxidation properties. Metals 14-19 mitochondrially encoded cytochrome c oxidase II Homo sapiens 94-99 22179398-1 2012 Postsynthetic metal ion exchange in a benzotriazolate-based MFU-4l(arge) framework leads to a Co(II)-containing framework with open metal sites showing reversible gas-phase oxidation properties. Metals 132-137 mitochondrially encoded cytochrome c oxidase II Homo sapiens 94-99 22400016-1 2012 Metal complexes of (Z)-2-(pyrrolidin-2-ylidene)hydrazinecarbothioamide (L) with Cu(II), Co(II), and Ni(II) chlorides were tested against selected types of fungi and were found to have significant antifungal activities. Metals 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 88-93 22076957-0 2011 Exploring the effect of metal ions and counteranions on the structure and magnetic properties of five dodecanuclear Co(II) and Ni(II) clusters. Metals 24-29 mitochondrially encoded cytochrome c oxidase II Homo sapiens 116-122 21796789-7 2011 Metal ions, i.e. Co(II), Cu(II), Ni(II), Al(III), and Fe(III), as models were injected into the present TRDC system. Metals 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 17-23 21835544-2 2011 The selectivity order of the resin towards some metal ions follows the order Pb(II) > Cu(II)> Zn(II), Ni(II), Co(II). Metals 48-53 mitochondrially encoded cytochrome c oxidase II Homo sapiens 116-122 21882826-1 2011 We fabricated a vertically and unidirectionally oriented metal coordinated alpha-helical peptide monolayer, Leu(2)Ala(Pyri)(Co(II))Leu(6)Ala(4-Pyri)(Co(II))Leu(6), by stepwise polymerization on a mixed self-assembled monolayer consisting of amino-alkanethiol, dialkyl disulfide, and ferrocenyl alkanethiol acted as a photoresponsive electron donor. Metals 57-62 mitochondrially encoded cytochrome c oxidase II Homo sapiens 124-130 21882826-1 2011 We fabricated a vertically and unidirectionally oriented metal coordinated alpha-helical peptide monolayer, Leu(2)Ala(Pyri)(Co(II))Leu(6)Ala(4-Pyri)(Co(II))Leu(6), by stepwise polymerization on a mixed self-assembled monolayer consisting of amino-alkanethiol, dialkyl disulfide, and ferrocenyl alkanethiol acted as a photoresponsive electron donor. Metals 57-62 mitochondrially encoded cytochrome c oxidase II Homo sapiens 149-155 21796789-9 2011 The elution times of the metal ions were examined based on their absorption behavior; Co(II), Ni(II), Al(III), Fe(III), and Cu(II) were eluted in this order over the elution times of 4.7-6.8 min. Metals 25-30 mitochondrially encoded cytochrome c oxidase II Homo sapiens 86-92 22121779-9 2011 Metal ions Co(II) and Ni(II) can mediate RT-HSA interaction, making the binding of the drug to protein stronger, which indicates that Co(II) and Ni(II) can enhance rhaponticin"s medical efficacy under physiological conditions. Metals 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 11-17 22121779-9 2011 Metal ions Co(II) and Ni(II) can mediate RT-HSA interaction, making the binding of the drug to protein stronger, which indicates that Co(II) and Ni(II) can enhance rhaponticin"s medical efficacy under physiological conditions. Metals 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 134-140 21265566-4 2011 Co 2p(3/2) absorption edge signals were used to determine the spatial distributions of the metal species in the Co(II)-doped cement. Metals 91-96 mitochondrially encoded cytochrome c oxidase II Homo sapiens 112-118 21688331-1 2011 Crystal structures of two metal-organic frameworks (MFU-1 and MFU-2) are presented, both of which contain redox-active Co(II) centres coordinated by linear 1,4-bis[(3,5-dimethyl)pyrazol-4-yl] ligands. Metals 26-31 mitochondrially encoded cytochrome c oxidase II Homo sapiens 119-125 20939764-4 2011 Metal complexes are [M(LH)Cl(2)] and [M(LH)(2)Cl(2)] type, where M = Fe(III), Co(II), and Cu(II) and LH = IPMCHTSC and IPMCHPhTSC. Metals 0-5 mitochondrially encoded cytochrome c oxidase II Homo sapiens 78-83 20821809-8 2011 The height and area showed linear dependences with the Co(II) concentration, which were used to quantify the heavy metal, with recoveries up to 95%. Metals 115-120 mitochondrially encoded cytochrome c oxidase II Homo sapiens 55-61 20567791-2 2010 The bis-gamma-pyrone forms stable metal complexes with Li, Mg, Cu(II), Ni(II), Zn, Fe(II), Co(II) and Ba perchlorates whose crystal structures reveal that the ligand possesses significant bispyrylium character while the metal is coordinated at the negatively charged edge of the structure. Metals 34-39 mitochondrially encoded cytochrome c oxidase II Homo sapiens 91-97 20945441-3 2010 The irregular coordination of the carbonate ions to the metal centers results in a combination of coordination numbers (CNs) of the Co(II) ions of five and six. Metals 56-61 mitochondrially encoded cytochrome c oxidase II Homo sapiens 132-138 21082809-2 2010 d-(-)-quinic acid is a cellular alpha-hydroxycarboxylate metal ion binder, which reacts with Co(II) and Zn(II) under pH-specific hydrothermal conditions, leading to the isolation of two new species [Co(2)(C(7)H(11)O(6))(4)](n) nH(2)O (1) and [Zn(3)(C(7)H(11)O(6))(6)](n) nH(2)O (2). Metals 57-62 mitochondrially encoded cytochrome c oxidase II Homo sapiens 93-99 20810212-0 2010 Preparation and characterization of chelating fibers based on natural wool for removal of Hg(II), Cu(II) and Co(II) metal ions from aqueous solutions. Metals 116-121 mitochondrially encoded cytochrome c oxidase II Homo sapiens 109-115 20537435-0 2010 Chiral preference of L-tryptophan derived metal-based antitumor agent of late 3d-metal ions (Co(II), Cu(II) and Zn(II)) in comparison to D- and DL-tryptophan analogues: their in vitro reactivity towards CT DNA, 5"-GMP and 5"-TMP. Metals 42-47 mitochondrially encoded cytochrome c oxidase II Homo sapiens 93-98 20537435-0 2010 Chiral preference of L-tryptophan derived metal-based antitumor agent of late 3d-metal ions (Co(II), Cu(II) and Zn(II)) in comparison to D- and DL-tryptophan analogues: their in vitro reactivity towards CT DNA, 5"-GMP and 5"-TMP. Metals 81-86 mitochondrially encoded cytochrome c oxidase II Homo sapiens 93-98