PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 16385994-0 2005 Determination of trace amounts of cobalt using 1-(5-bromo-2-pyridylazo)-2-naphthol-6-sulfonic acid-Cu(II)-Co(II) competitive replacement complexation. Cobalt 34-40 mitochondrially encoded cytochrome c oxidase II Homo sapiens 106-112 16363471-0 2005 Cu(II)-3-(5-chlor-2-hydroxy-3-sulfophenylazo)-6-(2,4,6-tribromophenylazo)-4,5-dihydroxynaphthalene-2,7-disulfonic Acid-Co(II) binuclear complexation and its application to the selective determination of cobalt at ng/ml level. Cobalt 203-209 mitochondrially encoded cytochrome c oxidase II Homo sapiens 119-125 16296861-2 2005 In the photostationary state of these four complexes, nearly 50% of the trans-azobenzene moieties of the Co(II) complexes were converted to the cis isomer, and nearly 10% of the trans-azobenzene moieties of the Co(III) complexes isomerized to the cis isomer, implying that the cis isomer ratio in the photostationary state upon irradiation at 365 nm is controlled not by the number of azobenzene moieties in one molecule but rather by the oxidation state of the cobalt ions. Cobalt 462-468 mitochondrially encoded cytochrome c oxidase II Homo sapiens 105-111 16296861-3 2005 The femtosecond transient absorption spectra of the ligands and the complexes suggested that the photoexcited states of the azobenzene moieties in the Co(III) complexes were strongly deactivated by electron transfer from the azobenzene moiety to the cobalt center to form an azobenzene radical cation and a Co(II) center. Cobalt 250-256 mitochondrially encoded cytochrome c oxidase II Homo sapiens 307-313 15783223-7 2005 On the basis of these spectroscopic and theoretical analyses, 1 is best described as containing an intermediate spin FeII ion, whereas for the corresponding cobalt complex, oxidation states describing a d6 (CoIII) or d7 (CoII) electron configuration cannot be unambiguously assigned. Cobalt 157-163 mitochondrially encoded cytochrome c oxidase II Homo sapiens 207-211 16021422-2 2005 These exploit the enhancement of the cobalt peak obtained by using the Co(II)-dimethylglyoxime-cetyltrimethylammonium bromide-piperazine-N,N"-bis(2-ethanesulfonic acid) system. Cobalt 37-43 mitochondrially encoded cytochrome c oxidase II Homo sapiens 71-76 18968778-2 2002 The QADEAB can react with Co(II) in the presence of pH 3.8 acetic acid-sodium acetate buffer solution and cetyl trimethylammonium bromide (CTMAB) medium to form a violet chelate of a molar ratio 1:2 (cobalt to QADEAB). Cobalt 200-206 mitochondrially encoded cytochrome c oxidase II Homo sapiens 26-32 14983832-2 2003 Cobalt impregnated alginate beads are first formed by extrusion of an aqueous suspension of Co3O4 into a Co(II) chloride solution. Cobalt 0-6 mitochondrially encoded cytochrome c oxidase II Homo sapiens 105-111 18968778-0 2002 Study on the solid phase extraction of Co(II)-QADEAB chelate with C(18) disk and its application to the determination of trace cobalt. Cobalt 127-133 mitochondrially encoded cytochrome c oxidase II Homo sapiens 39-45 18969902-2 2005 The method exploits the enhancement of cobalt peak current observed in the system Co(II)-nioxime-cetyltrimethylammonium bromide-piperazine-N,N"-bis(2-ethanesulfonic acid). Cobalt 39-45 mitochondrially encoded cytochrome c oxidase II Homo sapiens 82-88 15243734-2 2004 The procedure exploits the enhancement of the cobalt peak obtained by use of the system Co(II)-dimethylglyoxime-piperazine-1,4-bis(2-ethanesulfonic acid)-cetyltrimethylammonium bromide. Cobalt 46-52 mitochondrially encoded cytochrome c oxidase II Homo sapiens 88-93 12465986-7 2002 This result clearly indicates that the inversion proceeds in the three steps; (i) the Co-C bond was homolytically cleaved by photoirradiation and the 1,2-bis(ethoxycarbonyl)ethyl radical and Co(II) were produced, (ii) the radical rotated by 180 degrees directing the C-D bond to the cobalt atom and the opposite plane of the radical faced to the cobalt atom, and (iii) the radical made a bond with Co(II). Cobalt 86-88 mitochondrially encoded cytochrome c oxidase II Homo sapiens 191-197 12465986-7 2002 This result clearly indicates that the inversion proceeds in the three steps; (i) the Co-C bond was homolytically cleaved by photoirradiation and the 1,2-bis(ethoxycarbonyl)ethyl radical and Co(II) were produced, (ii) the radical rotated by 180 degrees directing the C-D bond to the cobalt atom and the opposite plane of the radical faced to the cobalt atom, and (iii) the radical made a bond with Co(II). Cobalt 86-88 mitochondrially encoded cytochrome c oxidase II Homo sapiens 398-404 12465986-7 2002 This result clearly indicates that the inversion proceeds in the three steps; (i) the Co-C bond was homolytically cleaved by photoirradiation and the 1,2-bis(ethoxycarbonyl)ethyl radical and Co(II) were produced, (ii) the radical rotated by 180 degrees directing the C-D bond to the cobalt atom and the opposite plane of the radical faced to the cobalt atom, and (iii) the radical made a bond with Co(II). Cobalt 283-289 mitochondrially encoded cytochrome c oxidase II Homo sapiens 191-197 12465986-7 2002 This result clearly indicates that the inversion proceeds in the three steps; (i) the Co-C bond was homolytically cleaved by photoirradiation and the 1,2-bis(ethoxycarbonyl)ethyl radical and Co(II) were produced, (ii) the radical rotated by 180 degrees directing the C-D bond to the cobalt atom and the opposite plane of the radical faced to the cobalt atom, and (iii) the radical made a bond with Co(II). Cobalt 346-352 mitochondrially encoded cytochrome c oxidase II Homo sapiens 191-197 11944672-7 2002 The extent of the decrease in cobalt second shell features between single and bisorbate samples with equal Co(II) coverage increased with an increase in the Se:Co surface coverage ratio. Cobalt 30-36 mitochondrially encoded cytochrome c oxidase II Homo sapiens 107-113 12938390-0 2002 [Photometric determination of cobalt by the formation of a multi-ligand complex of Co(II)-C16H16N2S2O2-DEA]. Cobalt 30-36 mitochondrially encoded cytochrome c oxidase II Homo sapiens 83-88 12058909-3 2002 Co(II) was then coordinated to the TACN, followed by cobalt oxidation to make polymer A or followed by N-octyl TACN coordination and cobalt oxidation to make polymer B. Cobalt 53-59 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-6 12058909-3 2002 Co(II) was then coordinated to the TACN, followed by cobalt oxidation to make polymer A or followed by N-octyl TACN coordination and cobalt oxidation to make polymer B. Cobalt 133-139 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-6 11074321-1 2000 We initially observed a phenomenon of reduced in vitro binding of exogenous cobalt [Co(II)] to the N-terminus of human serum albumin (HSA) in emergency chest pain patients with early onset unstable angina and myocardial infarction. Cobalt 76-82 mitochondrially encoded cytochrome c oxidase II Homo sapiens 84-90 12240429-1 2001 The trans/cis ratio of the azobenzene-attached bipyridine ligands in a cobalt complex is reversibly altered by a combination of photoirradiation with a single UV light source and the reversible redox change between Co(II) and Co(III). Cobalt 71-77 mitochondrially encoded cytochrome c oxidase II Homo sapiens 215-221 11456660-8 2001 Electronic and X-ray absorbance results for P-1[Co(II)] and P-1[Co(NO)] show that the coordination geometry of the immobilized cobalt complexes are similar to those of their monomeric analogues and that NO binds directly to the cobalt centers. Cobalt 127-133 mitochondrially encoded cytochrome c oxidase II Homo sapiens 48-54 11599958-6 2001 In contrast Co(II)(OEB-15,19-(CN)(2)), which was obtained by the insertion of Co(II) into the free ligand, is monomeric with a four-coordinate cobalt ion. Cobalt 143-149 mitochondrially encoded cytochrome c oxidase II Homo sapiens 12-18 12240429-0 2001 Reversible trans-cis photoisomerization of azobenzene-attached bipyridine ligands coordinated to cobalt using a single UV light source and the Co(III)/Co(II) redox change. Cobalt 97-103 mitochondrially encoded cytochrome c oxidase II Homo sapiens 143-148 10968618-4 2000 In an effort to unravel the aqueous chemistry of cobalt in the presence of a physiologically relevant ligand, citrate, the first aqueous, soluble, mononuclear complex has been synthesized and isolated from reaction mixtures containing Co(II) and citrate in a 1:2 molar ratio at pH approximately 8. Cobalt 49-55 mitochondrially encoded cytochrome c oxidase II Homo sapiens 235-241 10504238-11 1999 A 14% increase in the isotropic hyperfine coupling of the remote dimethylbenzimidazole (14)N nucleus in enzyme-bound versus free base-on cob(II)alamin shows an enhanced delocalization of unpaired spin density from Co(II) onto the axial ligand, which would contribute to the acceleration of the cobalt-carbon bond cleavage rate in situ. Cobalt 294-300 mitochondrially encoded cytochrome c oxidase II Homo sapiens 214-220 10819461-13 2000 The reduction from Co(III) to Co(II) produces the most significant structural changes: the cobalt coordination number decreases from six to five, and the edge position shifts by 2.4 +/- 0.3 eV. Cobalt 91-97 mitochondrially encoded cytochrome c oxidase II Homo sapiens 30-36 34862103-5 2022 Meanwhile, cobalt doping promotes H2O2 decomposition by accelerated Fe(II)/Fe(III) cycle and Co(II)/Co(III) redox. Cobalt 11-17 mitochondrially encoded cytochrome c oxidase II Homo sapiens 93-99 2247162-3 1990 Here we describe an XAS study of divalent cobalt (Co(II)) complexes sorbed on three different solids, gamma-Al2O3, rutile (TiO2) and kaolinite (Al2Si2O5(OH)4). Cobalt 42-48 mitochondrially encoded cytochrome c oxidase II Homo sapiens 50-56 31769666-6 2019 In particular, the central metal atom adopts a high-spin (S = 2) state in 2-Fe, while the cobalt complex 2-Co represents a rare example of a Co(II) species with a coordination number different from six displaying a low-spin to high-spin spin-crossover (SCO) behavior. Cobalt 90-96 mitochondrially encoded cytochrome c oxidase II Homo sapiens 141-147 1327111-1 1992 A binuclear cobalt derivative of arthropod hemocyanin (Hc) has been prepared by the reaction of apo-Hc with Co(II) in the presence of thiocyanate. Cobalt 12-18 mitochondrially encoded cytochrome c oxidase II Homo sapiens 108-114 1327111-8 1992 The binuclear cobalt derivative cannot be reconstituted to native Hc with Cu(I), indicating the stable loading of Co(II) in the active site. Cobalt 14-20 mitochondrially encoded cytochrome c oxidase II Homo sapiens 114-120 34847327-3 2021 Through an approach that relies on mechanistic insights and systematic examination of ligand and counterion effects, we developed an efficient cobalt-based catalytic system ((P~P)CoX2/Me3Al) (P~P = bisphosphine) to effect the first enantioselective heterodimerization of several types of 1,3-dienes with ethylene. Cobalt 143-149 mitochondrially encoded cytochrome c oxidase II Homo sapiens 179-183 34953459-3 2022 The voltammetry showed that the redox couple of Co(II)/Co(III) and Ni(II)/Ni(III) as the mediator catalytically transferred the electrons of NO2-/NO3-; the Ni site had a relatively high transfer coefficient and diffusive current, while the Co site was better in the capacitive removal of the nitrite and nitrate compounds. Cobalt 240-242 mitochondrially encoded cytochrome c oxidase II Homo sapiens 48-54 34774613-3 2022 The coexistence of Co and Ni in various valence states might accelerate the cyclic process of Co(II)/Co(III) and Ni(II)/Ni(III), thereby improving the catalytic activity. Cobalt 19-21 mitochondrially encoded cytochrome c oxidase II Homo sapiens 94-100 34464118-3 2021 Our experiments and density functional theory calculations indicate that the Co atom fixated into the nitrogen pots of g-C3N4 serves as the main active site, enabling dissociation of the adsorbed PAA and conversion of the coordinated Co(II) to Co(IV) via a unique two-electron transfer mechanism. Cobalt 77-79 mitochondrially encoded cytochrome c oxidase II Homo sapiens 234-240 34272392-6 2021 Mechanistic studies strongly support that the reaction involves direct halogen atom abstraction via single electron transfer to difluoroalkyl bromides from the in situ formed cobalt(I) species, thus realizing a Co(I)/Co(II)/Co(III) catalytic cycle. Cobalt 175-184 mitochondrially encoded cytochrome c oxidase II Homo sapiens 217-223 34352174-2 2021 Herein an unprecedented cobalt-catalyzed highly site-, diastereo-, and enantioselective protocol for stereoselective formation of nucleophilic allyl-Co(II) complexes followed by addition to aldehydes is presented. Cobalt 24-30 mitochondrially encoded cytochrome c oxidase II Homo sapiens 149-155 34085813-4 2021 Such high-yield light-induced VT had never been experimentally observed in molecular crystals of cobalt tautomers, proving that the 450 nm light illumination is triggering a chain of events that leads to the ls-CoIII to hs-CoII interconversion. Cobalt 97-103 mitochondrially encoded cytochrome c oxidase II Homo sapiens 223-227 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). Cobalt 117-123 mitochondrially encoded cytochrome c oxidase II Homo sapiens 149-155 35188161-3 2022 The redox properties of CoIIFeII have been investigated in DMF, revealing that this complex is the easiest to reduce by one-electron among the analogous MFe complexes (M = Ni, Fe, Co). Cobalt 180-182 mitochondrially encoded cytochrome c oxidase II Homo sapiens 24-32 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. Cobalt 154-160 mitochondrially encoded cytochrome c oxidase II Homo sapiens 41-47 35040067-4 2022 The results showed that hollow cobalt-based ferrocenyl metal-organic framework microspheres (Co-Fc-MOFs) exhibited the best catalytic performance, which is closely related to the synergy of Fc/Fc+ and Co(II)/Co(III) cycles in persulfate activation. Cobalt 31-37 mitochondrially encoded cytochrome c oxidase II Homo sapiens 201-207 35172100-1 2022 We performed first principles simulations to explore the water reduction process of the cobalt complex (CoII(bpbH2)Cl2), where bpbH2 = N,N"-bis(2"-pyridine carboxamide)-1,2-benzene. Cobalt 88-94 mitochondrially encoded cytochrome c oxidase II Homo sapiens 104-108 35041773-3 2022 The electrocatalytic H 2 generating capabilities of two Co(II) complexes, (Co(kappa 3 -2,6-{Ph 2 PNR} 2 (NC 5 H 3 ))Br 2 ) R = H ( I) R = Me ( II ) are presented for a variety of proton sources including trifluoroacetic acid (TFA), acetic acid (AA) and trifluoroethanol (TFE). Cobalt 75-77 mitochondrially encoded cytochrome c oxidase II Homo sapiens 56-62 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. Cobalt 119-125 mitochondrially encoded cytochrome c oxidase II Homo sapiens 204-210 35068152-3 2022 In this work, we study the experimentally synthesized Co(II) dimer (Co2(C5NH5)4(mu-PO2(CH2C6H5)2)3) SMM with the goal to control the exchange energy, DeltaEJ, between the Co atoms through tuning of the capping ligands. Cobalt 171-173 mitochondrially encoded cytochrome c oxidase II Homo sapiens 54-60 2840023-4 1988 The electronic state of the Co(II) ion provides a useful probe to estimate how ligation to iron-containing subunits changes the structure of the cobalt-substituted heme vicinity as described previously (T. Inubushi and T. Yonetani (1983) Biochemistry 22, 1894-1900). Cobalt 145-151 mitochondrially encoded cytochrome c oxidase II Homo sapiens 28-34 33497983-6 2021 Quenching reactions and EPR studies revealed the coexistence of sulfate radical (SO4 -), hydroxyl radical ( OH), and singlet oxygen (1O2), which was attributed to the potential in-situ recycling of cobalt and copper species (Co(III) Co(II), Cu(II) Cu(I))). Cobalt 198-204 mitochondrially encoded cytochrome c oxidase II Homo sapiens 233-239 6322852-0 1984 Co(II) derivatives of Cu,Zn-superoxide dismutase with the cobalt bound in the place of copper. Cobalt 58-64 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-6 6322852-2 1984 Co(II) derivatives of Cu,Zn-superoxide dismutase having cobalt substituted for the copper (Co,Zn-superoxide dismutase and Co,Co-superoxide dismutase) were studied by optical and EPR spectroscopy. Cobalt 56-62 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-6 6322852-4 1984 This behaviour suggests that cobalt in Co,Zn-superoxide dismutase is open to solvent access, at variance with the Co(II) of the Cu,Co-superoxide dismutase, which is substituted for the Zn. Cobalt 29-35 mitochondrially encoded cytochrome c oxidase II Homo sapiens 114-120 32991759-2 2021 An appropriately tuned cationic pincer cobalt(I) complex featuring a central silylene donor reacts with CO2 to afford a bimetallic siloxane featuring two Co(II) centers with liberation of CO, and reaction with ethylene yields a similar bimetallic complex with an ethylene bridge. Cobalt 39-48 mitochondrially encoded cytochrome c oxidase II Homo sapiens 154-160 33529486-3 2021 A detailed analysis of the electronic structure of Cobalt dimers of the general formula Co2Cl2Ln (L = NH3 and PH3) demonstrates that electron transfer is triggered by asymetric coordination of amine and phosphine to stabilize a mixed-valence Co(II)-Co(0) dimer. Cobalt 51-57 mitochondrially encoded cytochrome c oxidase II Homo sapiens 244-250 33264886-7 2021 The co-existence of Fe and Co in various valence states in catalyst might improve the conversion of Co(III)/Co(II) and Fe(III)/Fe(II), which would increase the catalytic activity in catalytic ozonation process. Cobalt 27-29 mitochondrially encoded cytochrome c oxidase II Homo sapiens 108-114 33433551-1 2021 We are reporting the synthesis and structural characterization of a new hexanuclear Co(ii)/Co(iii) complex starting from a versatile pivalate cobalt precursor and the racemic mixture of a chelating Schiff base type ligand. Cobalt 142-148 mitochondrially encoded cytochrome c oxidase II Homo sapiens 84-90 33412472-7 2021 Such favorable effect was partially ascribed to the specific ligand structure of six coordination structure between phosphate and cobalt, which facilitated electron transfer in the CoIII/CoII reduction. Cobalt 130-136 mitochondrially encoded cytochrome c oxidase II Homo sapiens 181-185 33023288-7 2020 On the other hand, Cl4QH2 + is deprotonated to produce Cl4QH , which transfers either a hydrogen-atom transfer or a proton-coupled electron transfer to [CoII(dmgH)2pyCl]- to produce a cobalt(III) hydride complex, [CoIII(H)(dmgH)2pyCl]-, which reacts with H+ to evolve H2, accompanied by the regeneration of CoIII(dmgH)2pyCl. Cobalt 184-203 mitochondrially encoded cytochrome c oxidase II Homo sapiens 153-157 33191419-0 2020 Field-induced slow magnetic relaxation from linear trinuclear CoIII-CoII-CoIII to grid [2 x 2] tetranuclear mixed-valence cobalt complexes. Cobalt 122-128 mitochondrially encoded cytochrome c oxidase II Homo sapiens 62-66 32768854-4 2020 The PFRs enabled an efficient transfer electron to both cobalt atom and O2, facilitating the recycle of Co(III)/Co(II), and thereby leaded to an excellent catalytic performance. Cobalt 56-62 mitochondrially encoded cytochrome c oxidase II Homo sapiens 112-118 32485604-1 2020 In this manuscript, we report the development of a rapid and facile optic sensor for highly sensitive and selective detection of cobalt ions (Co(II)). Cobalt 129-135 mitochondrially encoded cytochrome c oxidase II Homo sapiens 142-148 31747078-2 2020 In this work, we precisely anchor catalytic active cobalt porphyrin [TCPP(Co) = (5,10,15,20)-tetrakis(4-carboxyphenyl)porphyrin-Co(II)] onto the water-stable 2-D MOF nanosheets (Zr-BTB) to obtain ultra-thin 2-D MOF nanosheets [TCPP(Co)/Zr-BTB] with accessible catalytic sites for CO2 reduction reaction. Cobalt 51-57 mitochondrially encoded cytochrome c oxidase II Homo sapiens 128-134 32697905-3 2020 Mechanistic studies suggest that the reaction operates through a radical chain process initiated by Co(II)/O2/phenol and quenched by the cobalt-based catalyst. Cobalt 137-143 mitochondrially encoded cytochrome c oxidase II Homo sapiens 100-106 32271545-5 2020 The possible interface mechanism of PMS activation by CuCo-H3 was proposed, wherein unique interconnected meso-macroporous nanosheets structure, strong interaction between copper and cobalt, and cycling of Co(II)/Co(III) and Cu(I)/Cu(II) effectively facilitated PMS activation to generate SO4 - and OH, which contributed to BP-4 degradation. Cobalt 183-189 mitochondrially encoded cytochrome c oxidase II Homo sapiens 206-212 32815718-1 2020 The influence of a redox-active ligand on spin-changing events induced by the coordination of exogenous donors is investigated within the cobalt complex [CoII(DPP 2-)], bearing a redox-active DPP2- ligand (DPP = dipyrrin-bis(o,p-di-tert-butylphenolato) with a pentafluorophenyl moiety on the meso-position. Cobalt 138-144 mitochondrially encoded cytochrome c oxidase II Homo sapiens 154-158 32481699-8 2020 The combined effect of pH, metal complexation capacity, and the presence of Fe and Mn oxides added to wheat straw biochar resulted in an effective reduction of soluble Co (II), showing high efficiency of this material for cobalt sorption in contaminated soils. Cobalt 222-228 mitochondrially encoded cytochrome c oxidase II Homo sapiens 168-175 32186188-3 2020 For the first time, this study determined the reaction rates of PAA with Co(II) (kPAA,Co(II) = 1.70x101 to 6.67x102 M-1 s-1) and Co(III) (kPAA,Co(III) = 3.91x100 to 4.57x102 M-1 s-1) ions over initial pH 3.0-8.2, and evaluated thirty different aromatic organic compounds for degradation by Co/PAA. Cobalt 73-75 mitochondrially encoded cytochrome c oxidase II Homo sapiens 86-92 31725272-3 2019 The crystal structure of Co(II)-TMU-63 is assembled from two types of organic building blocks (mu4-tpa2- and mu-dapz ligands), which arrange the cobalt nodes into a complex layer-pillared net with an unreported 4,4,4,6T14 topology. Cobalt 145-151 mitochondrially encoded cytochrome c oxidase II Homo sapiens 25-38 31521068-1 2019 Cobalt complexes that undergo charge-transfer induced spin-transitions or valence tautomerism from low spin CoIII to high spin (HS) CoII are potential candidates for magneto-optical switches. Cobalt 0-6 mitochondrially encoded cytochrome c oxidase II Homo sapiens 108-112 31264803-3 2019 The paramagnetic nature of all the solids was evidenced by magnetic susceptibility measurements, showing the variation of the oxidation states of two cobalt centers in [1L -nmc ]n+ from CoII 1.00 CoIII 1.00 for X=ClO4 - or NO3 - to CoII 0.67 CoIII 1.33 for X=Cl- , via CoII 0.83 CoIII 1.17 for X=SO4 2- . Cobalt 150-156 mitochondrially encoded cytochrome c oxidase II Homo sapiens 186-190 31432676-6 2019 Whereas for M = Ni (DeltaE = -13 kcal/mol) Ni+III is reduced to Ni+II, for M = Co, Fe, Mn (DeltaE = 1, 10, 6 kcal/mol, respectively) it is Co+III that is reduced to Co+II. Cobalt 79-81 mitochondrially encoded cytochrome c oxidase II Homo sapiens 139-144 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. Cobalt 39-45 mitochondrially encoded cytochrome c oxidase II Homo sapiens 129-135 31005705-1 2019 An efficient method for the consolidation of cobalt (Co(II)) adsorbed calcium hydroxyapatite was investigated to develop a simplified route for decontamination of the coolant system of nuclear power plants and direct immobilization of as-spent adsorbent. Cobalt 45-51 mitochondrially encoded cytochrome c oxidase II Homo sapiens 53-59 30580142-4 2019 Capturing cobalt (Co(II)) from filtered river water doped with competing metals (Cu, As, Ag, Cd, Hg, Tl, and Pb) was most effective from pH 5-8 with binding affinity ranged from IDAA > DE4A > ED3A > Ac-Phos > SH on SAMMS. Cobalt 10-16 mitochondrially encoded cytochrome c oxidase II Homo sapiens 18-24 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. Cobalt 32-34 mitochondrially encoded cytochrome c oxidase II Homo sapiens 83-87 30293044-1 2019 This study analyzes the effect of the addition of acetate, citrate, and nitrilotriacetate anions on the retention of Co(II) cations by the gamma-alumina surface in view of the preparation of alumina supported cobalt catalysts. Cobalt 209-215 mitochondrially encoded cytochrome c oxidase II Homo sapiens 117-123 30177164-2 2018 Obtained Co(II)-RLMP complexes, with cobalt content ~2-8% (AAS), were characterized by UV-Vis spectrophotometry, FTIR spectroscopy (ATR-FTIR, FT-IRIS), MALDI-TOF/TOF MS, and XRD. Cobalt 37-43 mitochondrially encoded cytochrome c oxidase II Homo sapiens 9-15 30462116-1 2018 We report the synthesis, structural characterization and a combined computational and experimental study of the magnetic properties of two pivalate cobalt complexes, a mononuclear Co(ii) one and a tetranuclear Co(ii)3Co(iii) mixed valence polynuclear one. Cobalt 148-154 mitochondrially encoded cytochrome c oxidase II Homo sapiens 183-185 31459006-5 2018 Cobalt nanoparticles were loaded to F-MPM through in situ reduction of coordinated Co(II) ions to produce a monolithic Co heterogeneous catalyst (Co-MPM). Cobalt 0-6 mitochondrially encoded cytochrome c oxidase II Homo sapiens 83-89 30204436-4 2018 The amount of detectable Co(II)aq after 3 h for the six Co-POMs ranges from ~0.25 to ~90% of the total cobalt initially present in the Co-POM. Cobalt 103-109 mitochondrially encoded cytochrome c oxidase II Homo sapiens 25-30 30009517-3 2018 Time-resolved Co K-edge X-ray absorption spectroscopy in the microsecond time range indicates that, for the [CoII (aPPy)] catalyst (aPPy=di([2,2"-bipyridin]-6-yl)(pyridin-2-yl)methanol), the pendant pyridine dissociates from the cobalt in the intermediate CoI state. Cobalt 229-235 mitochondrially encoded cytochrome c oxidase II Homo sapiens 109-113 30094992-2 2018 More interestingly, under the same condition, the assembly of 4-methyl-3,5-di(pyridin-4-yl) benzoic acid (HMDPB) with Co(II) facilitates the formation of a cationic framework, [Co2(MDPB)3(DMF)](NO3) xS (2), with cobalt dimer, [Co2(CO2)3N4], as building blocks. Cobalt 213-219 mitochondrially encoded cytochrome c oxidase II Homo sapiens 118-124 28937969-1 2017 This work presented a facile and eco-friendly method for the determination of cobalt ions (Co(II)) in living cells based on layered double hydroxides (Mg-Al CO3-LDHs) enhanced chemiluminescence (CL) emission of a Co(II)-hydrogen peroxide-sodium hydroxide system. Cobalt 78-84 mitochondrially encoded cytochrome c oxidase II Homo sapiens 91-97 30203727-3 2018 Two groups of cobalt compounds are differentiated on the basis of their mechanisms of toxicity: (1) those essentially involving the solubilization of Co(II) ions, and (2) metallic materials for which both surface corrosion and release of Co(II) ions act in concert. Cobalt 14-20 mitochondrially encoded cytochrome c oxidase II Homo sapiens 150-156 30203727-3 2018 Two groups of cobalt compounds are differentiated on the basis of their mechanisms of toxicity: (1) those essentially involving the solubilization of Co(II) ions, and (2) metallic materials for which both surface corrosion and release of Co(II) ions act in concert. Cobalt 14-20 mitochondrially encoded cytochrome c oxidase II Homo sapiens 238-244 32559940-2 2018 Almost complete dissolution of Li and nearly 90% dissolution of Co occurred in at 80 C for 6 h. The reducing agent, ascorbic acid (AA), converts the dissolved Co(III) to Co(II) thereby selective recovery of Co as Co(II)-oxalate is possible. Cobalt 64-66 mitochondrially encoded cytochrome c oxidase II Homo sapiens 171-177 32559940-2 2018 Almost complete dissolution of Li and nearly 90% dissolution of Co occurred in at 80 C for 6 h. The reducing agent, ascorbic acid (AA), converts the dissolved Co(III) to Co(II) thereby selective recovery of Co as Co(II)-oxalate is possible. Cobalt 160-162 mitochondrially encoded cytochrome c oxidase II Homo sapiens 171-177 32559940-2 2018 Almost complete dissolution of Li and nearly 90% dissolution of Co occurred in at 80 C for 6 h. The reducing agent, ascorbic acid (AA), converts the dissolved Co(III) to Co(II) thereby selective recovery of Co as Co(II)-oxalate is possible. Cobalt 160-162 mitochondrially encoded cytochrome c oxidase II Homo sapiens 214-220 29938022-3 2018 Experimental investigations, supported by electronic structure calculations, reveal that catalysis commences when nitrate binds to the two-electron reduced species CoII(DIM-), where cobalt and the macrocycle are each reduced by a single electron. Cobalt 182-188 mitochondrially encoded cytochrome c oxidase II Homo sapiens 164-168 29334459-6 2018 Lennard-Jones parameters for the cobalt center in the Co(II) and Co(I) states were optimized using a helium atom probe, and partial atomic charges were obtained with a combination of natural population analysis (NPA) and restrained electrostatic potential (RESP) fitting approaches. Cobalt 33-39 mitochondrially encoded cytochrome c oxidase II Homo sapiens 54-60 28846901-1 2018 A novel nitrogen-doped biochar embedded with cobalt (Co-NB) was fabricated via pyrolysis of glucose pretreated with melamine (N donor) and Co(II). Cobalt 45-51 mitochondrially encoded cytochrome c oxidase II Homo sapiens 139-145 28933477-1 2017 We present a new and efficient cobalt precursor, CoII(DMOCHCOCF3)2, to prepare Co3O4 thin films and conformal coatings. Cobalt 31-37 mitochondrially encoded cytochrome c oxidase II Homo sapiens 49-53 29052339-3 2017 For a cobalt complex of the tetradentate methanol-bridged bispyridyl-bipyridyl complex [CoII Br(tpy)]Br, a detailed mechanistic picture is obtained by combining electrochemistry, spectroscopy, and photocatalysis. Cobalt 6-12 mitochondrially encoded cytochrome c oxidase II Homo sapiens 88-92 28937969-1 2017 This work presented a facile and eco-friendly method for the determination of cobalt ions (Co(II)) in living cells based on layered double hydroxides (Mg-Al CO3-LDHs) enhanced chemiluminescence (CL) emission of a Co(II)-hydrogen peroxide-sodium hydroxide system. Cobalt 78-84 mitochondrially encoded cytochrome c oxidase II Homo sapiens 213-219 28503262-1 2017 The cobalt (Co(II)) ion is a main component of alloys and considered to be carcinogenic, especially due to the carcinogenic and toxicological effects in the aquatic environment. Cobalt 4-10 mitochondrially encoded cytochrome c oxidase II Homo sapiens 12-18 29034924-0 2017 Trapping of superoxido cobalt and peroxido dicobalt species formed reversibly from CoII and O2. Cobalt 23-29 mitochondrially encoded cytochrome c oxidase II Homo sapiens 83-87 28409286-2 2017 It is based on cluster and periodic density functional theory modeling for relevant {[Co(II)(NH3)n]-NO} adducts, where Co(II) means a cobalt cation embedded either in a periodic model of chabasite (CHA) zeolite or in model clusters. Cobalt 134-140 mitochondrially encoded cytochrome c oxidase II Homo sapiens 86-92 28409286-2 2017 It is based on cluster and periodic density functional theory modeling for relevant {[Co(II)(NH3)n]-NO} adducts, where Co(II) means a cobalt cation embedded either in a periodic model of chabasite (CHA) zeolite or in model clusters. Cobalt 134-140 mitochondrially encoded cytochrome c oxidase II Homo sapiens 119-125 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. Cobalt 37-43 mitochondrially encoded cytochrome c oxidase II Homo sapiens 143-149 27320443-1 2016 By introducing photoactive fac-tris(2-phenylpyridine)iridium moieties as a ligand backbone to constrain the coordination geometry of cobalt ions, a multifunctional Ir2Co3-type capsule was achieved and showed induced-fit capsule-capsule conversion by cooperative binding one carbonate anion with the equatorial Co(ii) centers. Cobalt 133-139 mitochondrially encoded cytochrome c oxidase II Homo sapiens 310-316 28035824-3 2017 A comparison of their Kbeta XES spectra with the spectra of cobalt coordination complexes with known oxidation and spin states demonstrates that the low-temperature valence tautomer can be described as a low-spin CoIII configuration and the high-temperature valence tautomer as a high-spin CoII configuration. Cobalt 60-66 mitochondrially encoded cytochrome c oxidase II Homo sapiens 213-217 27384529-6 2016 Our data support binding of a serine residue from the reductive-activator protein (RACo) of CoFeSP to the cobalt ion in the CoFeSP-RACo protein complex that stabilizes Co(II). Cobalt 106-112 mitochondrially encoded cytochrome c oxidase II Homo sapiens 168-174 27022316-3 2016 The specific configuration of the alpha-amino acid group affects the eg (1) electron of Co(II) transfer to the pi (*) orbit of O2; this phenomenon also favors the reversible formation and dissociation of Co-O2 bond when O2 coordinates with Co(II) complexes. Cobalt 88-90 mitochondrially encoded cytochrome c oxidase II Homo sapiens 240-246 25907670-3 2015 Owing to the different orientations of the carboxylate groups, the benzenedicarboxylates adopt various bridging modes to connect the Co(II) ions into a series of 1D carboxylate cobalt architectures based on the 1D chain, binuclear and single-ion magnetic units, respectively. Cobalt 177-183 mitochondrially encoded cytochrome c oxidase II Homo sapiens 133-139 26245626-2 2016 Cobalt oxido catalyst (Co-OECs) films deposited from buffered Co(II) solutions have emerged as arguably the most studied class of heterogeneous oxygen evolution catalysts. Cobalt 0-6 mitochondrially encoded cytochrome c oxidase II Homo sapiens 62-68 26509213-4 2015 In situ spectroelectrochemical measurements provided insights into the cobalt oxidation state during the course of reaction and showed that the majority of catalytic centers in this MOF are redox-accessible where Co(II) is reduced to Co(I) during catalysis. Cobalt 71-77 mitochondrially encoded cytochrome c oxidase II Homo sapiens 213-219 25469667-0 2015 Co(II)-mediated effects of plain and plasma immersion ion implanted cobalt-chromium alloys on the osteogenic differentiation of human mesenchymal stem cells. Cobalt 68-74 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-5 25854540-11 2015 Most of these transformations proceed through low-valent cobalt complexes, which are conveniently generated in situ from air-stable Co(II) salts by Zn- or Mn-mediated reduction. Cobalt 57-63 mitochondrially encoded cytochrome c oxidase II Homo sapiens 132-138 25544494-2 2015 In this study, we investigated the underlying mechanisms and transformation pathways of atrazine degradation by cobalt catalyzed peroxymonosulfate (Co(II)/PMS). Cobalt 112-118 mitochondrially encoded cytochrome c oxidase II Homo sapiens 148-154 25464507-4 2014 The analytical parameters of prepared NCs were also calculated for a selective detection of divalent cobalt [Co(II)] prior to its determination by inductively coupled plasma-optical emission spectrometry (ICP-OES). Cobalt 101-107 mitochondrially encoded cytochrome c oxidase II Homo sapiens 109-115 25494642-4 2015 The composite shows good performance in multiple cycle testing and the turnover number (TON vs Co(II)) of this hybrid material for hydrogen evolution reaction (754 after 5 h) is considerably higher than previously reported dye-sensitized cobalt-based catalysts. Cobalt 238-244 mitochondrially encoded cytochrome c oxidase II Homo sapiens 95-101 25632988-3 2015 With M = Fe, Co, or Ni, electrochemical formation of the Ta-Ta bonds is accompanied by a partial reduction of the Fe(II), Co(II), or Ni(II) to Fe(0), Co(0), or Ni(0). Cobalt 13-15 mitochondrially encoded cytochrome c oxidase II Homo sapiens 122-128 25135438-2 2014 Bond Valence Sum (BVS) calculations and bond lengths indicate the presence of mixed valent Co (Co(II), Co(III)) centres in compounds and and only Co(III) centres in and as required for the charge balances and supported by the magnetic measurements. Cobalt 91-93 mitochondrially encoded cytochrome c oxidase II Homo sapiens 95-101 25243488-5 2014 In addition to the unusual reactivity of the nitride 2, the resulting divalent cobalt complex 3 is a rare example of a trigonal pyramidal complex with four different donor ligands of a tetradentate chelate-an N-heterocyclic carbene, a phenolate, an imine, and an amine-binding to a high-spin Co(II) ion. Cobalt 79-85 mitochondrially encoded cytochrome c oxidase II Homo sapiens 292-298 24788679-1 2014 A significant improvement in the long-term stability for cobalt-based dye-sensitized solar cells (DSCs) under light-soaking conditions has been achieved by optimization of the composition of tris(2,2"-bipyridine) Co(ii)/Co(iii) electrolytes. Cobalt 57-63 mitochondrially encoded cytochrome c oxidase II Homo sapiens 213-219 25275501-1 2014 Two new cobalt precursors, Co(II)(PyCHCOCF3)2(DMAP)2 (1) and Co(III)(PyCHCOCF3)3 (2), based on Co(II) and Co(III) centers were synthesized using a redox active ligand system. Cobalt 8-14 mitochondrially encoded cytochrome c oxidase II Homo sapiens 27-52 25275501-1 2014 Two new cobalt precursors, Co(II)(PyCHCOCF3)2(DMAP)2 (1) and Co(III)(PyCHCOCF3)3 (2), based on Co(II) and Co(III) centers were synthesized using a redox active ligand system. Cobalt 8-14 mitochondrially encoded cytochrome c oxidase II Homo sapiens 27-33 24998701-5 2014 Since the distance between the cobalt ions is quite large (11.59 A), this is attributed in a first instance to the intrinsic properties of each Co(II) center (single-ion magnet behavior). Cobalt 31-37 mitochondrially encoded cytochrome c oxidase II Homo sapiens 144-150 24819564-1 2014 A homogeneous solution of Co(II) in acetate buffer at pH 7 is found to be an efficient water oxidation catalyst (WOC) showing significantly greater current density than Co(II) in phosphate buffer (Co-Pi) under identical conditions owing to the higher solubility of the former. Cobalt 26-28 mitochondrially encoded cytochrome c oxidase II Homo sapiens 169-175 24206708-2 2014 In this study, cobalt containing compounds, namely Co(II), cyanocobalamin (CN-Cbl) and hydroxylcobalamin (OH-Cbl), were well separated by reversed phase HPLC with a C8-HPLC column as the stationary phase and 8 mmol L(-1) ammonium acetate in 22%v/v methanol solution (pH 4) as the mobile phase using isocratic elution. Cobalt 15-21 mitochondrially encoded cytochrome c oxidase II Homo sapiens 51-57 24525159-7 2014 Membrane filtration experiments revealed that the removal capabilities of the materials for cobalt ions depended on the membrane"s thickness, flow rate and initial concentration of Co(II) ions. Cobalt 92-98 mitochondrially encoded cytochrome c oxidase II Homo sapiens 181-187 24589710-1 2014 Linear trimetallic Co(III)/Co(II)/Co(III) cobalt complexes with bridging acyl-alkoxy ligands are electrocatalysts for the reduction of tosic acid in acetonitrile. Cobalt 42-48 mitochondrially encoded cytochrome c oxidase II Homo sapiens 27-33 25325542-1 2014 Based on the sensitive reaction of Co(II) and salicyl fluorone with the presence of cetylpyridinium bromide in basic solution, a new method of flow injection micelle-solubilized spectrophotometry was developed for the determination of cobalt. Cobalt 235-241 mitochondrially encoded cytochrome c oxidase II Homo sapiens 35-41 24044777-5 2013 The combined experimental and theoretical charge density study identifies the different characters of two types of cobalt ions; more pronounced charge concentration and depletion features in the valence shell charge concentration (VSCC) are found in the Co(III) ion than in the Co(II) ion, and d-orbital populations also show the difference. Cobalt 115-121 mitochondrially encoded cytochrome c oxidase II Homo sapiens 278-284 23357750-4 2013 In the interference study, Co(II) was selectivity extracted in the top phase in the presence of Ni(II) and Cd(II) in a concentration of up to 20 times the cobalt level in the system. Cobalt 155-161 mitochondrially encoded cytochrome c oxidase II Homo sapiens 27-33 23732516-2 2013 Compound 1 was formed by the cleavage of Co-Cl bonds, the reduction of Co(II) to Co(I) and by the coordination of a toluene molecule. Cobalt 0-2 mitochondrially encoded cytochrome c oxidase II Homo sapiens 71-77 23411617-3 2013 In 1, the central rhombic core Co2O2 is occupied by two Co(III) ions while the external cobalt atoms display Co(II) oxidation states; meanwhile 2 and 3 exhibit a reversal in their Co(II)2Co(III)2 oxidation state distribution. Cobalt 88-94 mitochondrially encoded cytochrome c oxidase II Homo sapiens 109-115 23656559-6 2013 Based on the available information, most people with clearly elevated serum Co, like supplement users and hip implant patients, have >90% of Co as albumin-bound, with considerable excess binding capacity to sequester Co(II) ions. Cobalt 76-78 mitochondrially encoded cytochrome c oxidase II Homo sapiens 220-226 23783365-7 2013 X-ray photoelectron spectroscopy (XPS) data displayed the valence state of the cobalt element as Co(ii) or Co(iii) oxide species. Cobalt 79-85 mitochondrially encoded cytochrome c oxidase II Homo sapiens 97-103 23788486-5 2013 Upon changing the I(-) /I3 (-) electrolyte to the Co(II) /Co(III) redox couple, the cell gave rise to a significantly improved conversion efficiency of 10.02% with the multifunctional HC-A, which is one of the highest values reported for DSSCs with a cobalt-based electrolyte. Cobalt 251-257 mitochondrially encoded cytochrome c oxidase II Homo sapiens 50-56 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). Cobalt 28-34 mitochondrially encoded cytochrome c oxidase II Homo sapiens 163-168 22047035-2 2011 The metric parameters about the metal center and the pre-edge region of the Co K-edge X-ray absorption spectrum were reproduced by density functional theory (DFT), providing a qualitative description of the Co-NO bonding interaction as a Co(II) (S(Co) = 3/2) metal center, antiferromagnetically coupled to a triplet NO(-) anion (S(NO) = 1), an interpretation of the electronic structure that was validated by ab initio multireference methods (CASSCF/MRCI). Cobalt 248-251 mitochondrially encoded cytochrome c oxidase II Homo sapiens 238-244 22395577-3 2012 Assembling Cu(II), M(II) (M = Ni and Co), azido and nicotinic acid in hydrothermal condition, two novel isomorphic 3D heterometallic 3d-3d azido complexes, [CuM(N(3))(2)(nicotinate)(2)]( ) (M = Ni(II) for 1 and Co(II) for 2) were obtained. Cobalt 37-39 mitochondrially encoded cytochrome c oxidase II Homo sapiens 211-217 22931576-7 2012 Immunofluorescence showed dark and uniform COX-2 stain in Ni-Cr and Co-Cr alloy groups, while in pure Ti group, Au alloy group, and negative control group shallow and uneven distribution of COX-2 stain were observed. Cobalt 68-70 mitochondrially encoded cytochrome c oxidase II Homo sapiens 43-48 22134498-2 2012 Speciation of cobalt active sites into Co(II), mono- and polynuclear oxo-cobalt species as well as CoO clusters was quantified by IR using CO and NO as probe molecules. Cobalt 14-20 mitochondrially encoded cytochrome c oxidase II Homo sapiens 39-45 23232244-2 2012 The ATPS-MSFA method was applied for the determination of cobalt, based on the reaction between Co(II) and KSCN, which produces a metallic complex that spontaneously partitions to the top phase of the ATPS composed of poly(ethylene oxide), ammonium sulfate and water. Cobalt 58-64 mitochondrially encoded cytochrome c oxidase II Homo sapiens 96-111 21736310-2 2011 The networks here generally consist of (1) the persistent core component (denoted as CoTCPSB) of linear Co(II) aqua clusters (Co-O-Co-O-Co) integrated into 2D grids by 4,4"-bipyridine and TCPSB and (2) ancillary ligands (AL) on the two terminal Co(II) ions-these include DMF (N,N"-dimethylformamide), DMA (N,N"-dimethylacetamide), CH(3)CN, and water. Cobalt 85-87 mitochondrially encoded cytochrome c oxidase II Homo sapiens 104-110 21265566-1 2011 Scanning transmission X-ray microscopy was used to investigate the speciation and spatial distribution of Co in a Co(II)-doped cement matrix. Cobalt 106-108 mitochondrially encoded cytochrome c oxidase II Homo sapiens 114-120 21523305-9 2011 6 is a mixed-valence trinuclear cobalt complex, which is formulated as Co(III)(S = 0)-Co(II)(S = 3/2)-Co(III)(S = 0). Cobalt 32-38 mitochondrially encoded cytochrome c oxidase II Homo sapiens 86-92 21522824-1 2011 In the title coordination polymer, [Co(C(14)H(16)O(6))(H(2)O)(2)](n), the Co(II) ion, situated on a twofold rotation axis, is coordinated by four O atoms from two 4,4"-[1,4-phenyl-enebis(-oxy)]dibutano-ate (L) ligands and two water mol-ecules in a highly distorted octa-hedral geometry. Cobalt 36-38 mitochondrially encoded cytochrome c oxidase II Homo sapiens 74-80 21522293-1 2011 In the title diaqua-cobalt complex, [Co(C(8)H(11)NO(5)PS)(2)(H(2)O)(2)], the Co(II) atom is surrounded by six O atoms belonging to the phosphoryl and sulfonyl groups of two deprotonated chelate ligands and two additional O atoms from water mol-ecules which are in cis positions with respect to one another. Cobalt 20-26 mitochondrially encoded cytochrome c oxidase II Homo sapiens 77-83 20540554-5 2010 At lower temperatures, the Co(II) ion undergoes a spin transition to the low spin form (S(Co) = 1/2) and antiferromagnetic coupling gives rise to the observed diamagnetic ground state. Cobalt 90-93 mitochondrially encoded cytochrome c oxidase II Homo sapiens 27-33 20821809-1 2011 INTRODUCTION: The cobalt is an essential element for leguminous plants but may be harmful for other species; for that reason determination of Co(II) is very important for the management of polluted areas and for discover plants with capacity for the hyperaccumulation of heavy metals, which has produced a growing necessity of fast, sensitive and selective analytical techniques. Cobalt 18-24 mitochondrially encoded cytochrome c oxidase II Homo sapiens 142-148 20820611-3 2010 With LiOMe/pyridine as base in MeOH a dinuclear cobalt cage, [Co(2)(SbAr)(4)O(4)(O(3)PPh)(4)(OMe)(4)py(2)] 3, is formed, with four Sb(ii) and two Co(ii) centres bridged by mu(3)-oxides and phosphonates. Cobalt 48-54 mitochondrially encoded cytochrome c oxidase II Homo sapiens 134-136 20820611-3 2010 With LiOMe/pyridine as base in MeOH a dinuclear cobalt cage, [Co(2)(SbAr)(4)O(4)(O(3)PPh)(4)(OMe)(4)py(2)] 3, is formed, with four Sb(ii) and two Co(ii) centres bridged by mu(3)-oxides and phosphonates. Cobalt 48-54 mitochondrially encoded cytochrome c oxidase II Homo sapiens 146-152 20820611-7 2010 With Et(3)N/pyridine as base in MeCN a tetranuclear cobalt cage, [Co(4)(SbAr)(5)O(9)(O(3)PPh)(6)(py)(4)] 13, with five Sb(ii) centres forming a "bowtie" and bridging to four Co(ii) centres by phosphonates and mu(3)-oxides, is formed. Cobalt 52-58 mitochondrially encoded cytochrome c oxidase II Homo sapiens 122-124 20820611-7 2010 With Et(3)N/pyridine as base in MeCN a tetranuclear cobalt cage, [Co(4)(SbAr)(5)O(9)(O(3)PPh)(6)(py)(4)] 13, with five Sb(ii) centres forming a "bowtie" and bridging to four Co(ii) centres by phosphonates and mu(3)-oxides, is formed. Cobalt 52-58 mitochondrially encoded cytochrome c oxidase II Homo sapiens 174-180 20657935-1 2010 The systematic immobilization of cobalt(II) Schiff base complexes on SBA-15 mesoporous silica via copper catalyzed [3 + 2] azide-alkyne cycloaddition (CuAAC) "click reaction" involving either step-wise synthesis of silica-bound Schiff base ligand followed by its subsequent complexation with cobalt ions, or by the direct immobilization of preformed Co(II) Schiff base complex to the silica support is described. Cobalt 33-39 mitochondrially encoded cytochrome c oxidase II Homo sapiens 350-355 21588110-1 2010 In the title complex, [Co(C(22)H(15)O(5))(2)(C(2)H(5)OH)(2)], the Co(II) atom (site symmetry ) is coordinated by two O,O"-bidentate 4-(2-benzoyl-1-oxidoethen-yl)-3-hy-droxy-phenyl benzoate anions and two ethanol O atoms, resulting in a slightly distorted CoO(6) octa-hedral coordination. Cobalt 23-25 mitochondrially encoded cytochrome c oxidase II Homo sapiens 66-72 20227425-0 2010 The genotoxicity of physiological concentrations of chromium (Cr(III) and Cr(VI)) and cobalt (Co(II)): an in vitro study. Cobalt 86-92 mitochondrially encoded cytochrome c oxidase II Homo sapiens 94-100 20334891-4 2010 Cobalt chemistry is dominated by the Co(II) oxidation state in the aqueous phase of terrestrial environments primarily due to the extremely low solubility of Co(III). Cobalt 0-6 mitochondrially encoded cytochrome c oxidase II Homo sapiens 37-42 18854902-3 2008 In the presence of the other complexes, some damage occurred only in the presence of high sulfite concentrations (0.1-2.0 mM) after incubation for 4 h. In the presence of GGH, Co(II) and dissolved O2, DNA damage must involve a reactive high-valent cobalt complex. Cobalt 248-254 mitochondrially encoded cytochrome c oxidase II Homo sapiens 176-182 20092265-1 2010 A Co(II)-salen based fluorescent sensor (1.Co) that can selectively recognize cyanide anions in 1:2 binding stoichiometry over other anions has been developed. Cobalt 43-46 mitochondrially encoded cytochrome c oxidase II Homo sapiens 2-8 21582700-1 2009 In the title complex, [Co(C(22)H(24)N(2)O(4))] H(2)O, the Co(II) atom is in an almost square-planar coordination environment involv-ing two O and two N atoms from the Schiff base ligand. Cobalt 23-25 mitochondrially encoded cytochrome c oxidase II Homo sapiens 58-64 19436090-1 2009 Cobalt nanostructures have been prepared by a chemical route based on the Co(II) reduction in the confined space of cobalt bis(2-ethylhexyl)sulfosuccinate (Co(DEHSS)(2)) reverse micelles dispersed in n-heptane. Cobalt 0-6 mitochondrially encoded cytochrome c oxidase II Homo sapiens 74-80 19265384-6 2009 Modification of ZnO NCs with Co(II) resulted in the transfer of photoexcited electrons to the cobalt center where consequent nonradiative recombination, at energies lower than required for PC, was observed via a comparable decrease in both PL and PC activity. Cobalt 94-100 mitochondrially encoded cytochrome c oxidase II Homo sapiens 29-35 19735721-9 2010 The underlying mechanism of cobalt toxicity is not clearly established, but our results seem to indicate that the toxicity of Co(II) and of irradiation arises from production of reactive oxygen species. Cobalt 28-34 mitochondrially encoded cytochrome c oxidase II Homo sapiens 126-132 19846791-6 2009 The structure supports earlier suggestions that the enzyme acts to lower the reduction potential of the Co(II)/Co(I) couple by elongating the bond between the cobalt and its upper axial water ligand, effectively making the cobalt 4-coordinate, and illuminates the role of Tyr-1139 in the stabilization of this 4-coordinate state. Cobalt 159-165 mitochondrially encoded cytochrome c oxidase II Homo sapiens 104-110 19846791-6 2009 The structure supports earlier suggestions that the enzyme acts to lower the reduction potential of the Co(II)/Co(I) couple by elongating the bond between the cobalt and its upper axial water ligand, effectively making the cobalt 4-coordinate, and illuminates the role of Tyr-1139 in the stabilization of this 4-coordinate state. Cobalt 223-229 mitochondrially encoded cytochrome c oxidase II Homo sapiens 104-110 19775723-0 2009 Application of a peroxymonosulfate/cobalt (PMS/Co(II)) system to treat diesel-contaminated soil. Cobalt 35-41 mitochondrially encoded cytochrome c oxidase II Homo sapiens 47-53 18854902-6 2008 The results indicate that Co(II) binds O2 in the presence of GGH, and leads to the formation of a DMPO-HO adduct without first forming free superoxide or hydroxyl radical, supporting the participation of a reactive high-valent cobalt complex. Cobalt 227-233 mitochondrially encoded cytochrome c oxidase II Homo sapiens 26-32 18350888-3 2008 A potential risk in quantifying exchangeable Co in soils using isotope dilution techniques is the possible presence of two species of Co in soil solution and adsorbed on soil solid phases [Co(II) and Co(III)], coupled with the possibility that when an isotope of Co is added it may undergo a change in oxidation state during the measurement phase. Cobalt 134-136 mitochondrially encoded cytochrome c oxidase II Homo sapiens 189-195 18445468-2 2008 Attempts to prepare Co(II)-substituted L1 using biological incorporation resulted in an enzyme that contained only 1 Eq of cobalt and exhibited no catalytic activity. Cobalt 123-129 mitochondrially encoded cytochrome c oxidase II Homo sapiens 20-26 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. Cobalt 139-145 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-6 18350888-3 2008 A potential risk in quantifying exchangeable Co in soils using isotope dilution techniques is the possible presence of two species of Co in soil solution and adsorbed on soil solid phases [Co(II) and Co(III)], coupled with the possibility that when an isotope of Co is added it may undergo a change in oxidation state during the measurement phase. Cobalt 134-136 mitochondrially encoded cytochrome c oxidase II Homo sapiens 189-195 18076158-5 2008 Iron and cobalt complexation reactions are complicated by redox processes, which lead to mixed-oxidation-state Co(II)/Co(III) systems when starting with Co(II) salts, and reduction of Fe(III) to Fe(II) when starting with Fe(III). Cobalt 9-15 mitochondrially encoded cytochrome c oxidase II Homo sapiens 111-117 18076158-5 2008 Iron and cobalt complexation reactions are complicated by redox processes, which lead to mixed-oxidation-state Co(II)/Co(III) systems when starting with Co(II) salts, and reduction of Fe(III) to Fe(II) when starting with Fe(III). Cobalt 9-15 mitochondrially encoded cytochrome c oxidase II Homo sapiens 153-159 17822232-0 2007 Determination of cobalt at ng ml(-1) level in water using the electrophilic substiution complexation between co(II) and chlorophosphonazo-p-CL-Cu(II) complex. Cobalt 17-23 mitochondrially encoded cytochrome c oxidase II Homo sapiens 109-115 18217608-1 2007 The syntheses and structural elucidations of three different cobalt complexes of m-benziphthalocyanine are reported; both Co(II) and Co(III) complexes can be generated, and the ring undergoes partial oxidation upon metalation with Co(OAc)2x4H2O. Cobalt 61-67 mitochondrially encoded cytochrome c oxidase II Homo sapiens 122-128 17404646-2 2007 Glycoligands using various monosaccharide platforms functionalised by three 2-picolyl groups and coordinated to Co(II) through the bidentate 2-picolyl ether moieties are interesting ligands as they efficiently induce chirality at the cobalt with a fine control of the structure through the central sugar scaffold. Cobalt 234-240 mitochondrially encoded cytochrome c oxidase II Homo sapiens 112-118 17047739-0 2006 Dinuclear Co(III)/Co(III) and Co(II)/Co(III) mixed-valent complexes: synthetic control of the cobalt oxidation level. Cobalt 94-100 mitochondrially encoded cytochrome c oxidase II Homo sapiens 30-36 16023340-2 2006 Eleven out of total 38 isolated fungi which tolerated > 6.0 mM Co(II) were evaluated for cobalt biosorption using dried mycelial biomass. Cobalt 92-98 mitochondrially encoded cytochrome c oxidase II Homo sapiens 66-72 16023340-3 2006 Maximum Co(II)-loading (1036.5 microM/g, 60 min) was achieved with Mortierella SPS 403 biomass, which removed almost 50% of 4.0 mM cobalt from the aqueous solution. Cobalt 131-137 mitochondrially encoded cytochrome c oxidase II Homo sapiens 8-14 17274600-0 2007 Evidence that the principal CoII-binding site in human serum albumin is not at the N-terminus: implication on the albumin cobalt binding test for detecting myocardial ischemia. Cobalt 122-128 mitochondrially encoded cytochrome c oxidase II Homo sapiens 28-32 17274600-3 2007 Recently, binding of CoII to HSA has attracted much interest due to the so-called albumin cobalt binding (ACB) test approved by the Food and Drug Administration for evaluation of myocardial ischemia. Cobalt 90-96 mitochondrially encoded cytochrome c oxidase II Homo sapiens 21-25 17073484-9 2006 The results implied that electron transfer through cobalt clay layers was possible via mediation by Co(II) ions in a clay sheet. Cobalt 51-57 mitochondrially encoded cytochrome c oxidase II Homo sapiens 100-106