PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	119-125	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
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	
12240429-1	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	
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	
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