PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 III Homo sapiens 104-111 32412246-1 2020 Bis(dioxolene)-bridged dinuclear cobalt compounds provide an avenue toward controlled two-step valence tautomeric (VT) interconversions of the form {CoIII-cat-cat-CoIII} {CoIII-cat-SQ-CoII} {CoII-SQ-SQ-CoII} (cat2- = catecholate, SQ - = semiquinonate). Cobalt 33-39 mitochondrially encoded cytochrome c oxidase III Homo sapiens 149-154 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 III Homo sapiens 214-219 32412246-1 2020 Bis(dioxolene)-bridged dinuclear cobalt compounds provide an avenue toward controlled two-step valence tautomeric (VT) interconversions of the form {CoIII-cat-cat-CoIII} {CoIII-cat-SQ-CoII} {CoII-SQ-SQ-CoII} (cat2- = catecholate, SQ - = semiquinonate). Cobalt 33-39 mitochondrially encoded cytochrome c oxidase III Homo sapiens 163-168 32412246-1 2020 Bis(dioxolene)-bridged dinuclear cobalt compounds provide an avenue toward controlled two-step valence tautomeric (VT) interconversions of the form {CoIII-cat-cat-CoIII} {CoIII-cat-SQ-CoII} {CoII-SQ-SQ-CoII} (cat2- = catecholate, SQ - = semiquinonate). Cobalt 33-39 mitochondrially encoded cytochrome c oxidase III Homo sapiens 163-168 32412246-3 2020 Complementary structural, magnetic, spectroscopic and DFT computational studies reveal different electronic structures and VT behavior for the four cobalt complexes; one-step partial VT, two-step VT, incomplete VT, and temperature-invariant {CoIII-cat-cat-CoIII} states are observed. Cobalt 148-154 mitochondrially encoded cytochrome c oxidase III Homo sapiens 242-247 31779326-1 2019 Strong spin-dependent delocalization (double exchange) was previously demonstrated for the complexes, NN-Bridge-SQ-Coiii(py)2Cat-Bridge-NN (where NN = S = 12 nitronylnitroxide, Bridge = 1,4-phenylene and single bond, SQ = S = 12 orthobenzosemiquinone, Coiii = low-spin d6 cobalt 3+, and Cat = diamagnetic catecholate). Cobalt 272-281 mitochondrially encoded cytochrome c oxidase III Homo sapiens 115-120 32279486-3 2020 Density functional theory supports a CoIII=N=CoIII canonical form with significant pi-bonding between the cobalt centers and the nitride atom. Cobalt 106-112 mitochondrially encoded cytochrome c oxidase III Homo sapiens 37-42 32279486-3 2020 Density functional theory supports a CoIII=N=CoIII canonical form with significant pi-bonding between the cobalt centers and the nitride atom. Cobalt 106-112 mitochondrially encoded cytochrome c oxidase III Homo sapiens 45-50 31910972-1 2020 A biomimetic assembly of per-O-methylated-cyclodextrin dimer with cobalt proto-porphyrin (CoIII-PPIX@Py2CD) was achieved via covalent linkage between CoIII of CoIII-PPIX and pyridine N of Py2CD (primarily synthesized by the acyl chlorination reaction of two beta-CDs monomers with 3,5-bis (bromomethyl) pyridine). Cobalt 66-72 mitochondrially encoded cytochrome c oxidase III Homo sapiens 90-95 31910972-1 2020 A biomimetic assembly of per-O-methylated-cyclodextrin dimer with cobalt proto-porphyrin (CoIII-PPIX@Py2CD) was achieved via covalent linkage between CoIII of CoIII-PPIX and pyridine N of Py2CD (primarily synthesized by the acyl chlorination reaction of two beta-CDs monomers with 3,5-bis (bromomethyl) pyridine). Cobalt 66-72 mitochondrially encoded cytochrome c oxidase III Homo sapiens 150-155 31910972-1 2020 A biomimetic assembly of per-O-methylated-cyclodextrin dimer with cobalt proto-porphyrin (CoIII-PPIX@Py2CD) was achieved via covalent linkage between CoIII of CoIII-PPIX and pyridine N of Py2CD (primarily synthesized by the acyl chlorination reaction of two beta-CDs monomers with 3,5-bis (bromomethyl) pyridine). Cobalt 66-72 mitochondrially encoded cytochrome c oxidase III Homo sapiens 150-155 32120161-7 2020 Coupling of N-terminal peptides with the cobalt complexes, possessing a carboxylic group on the tetradentate Schiff base ligand, afforded Co(III)-peptide bioconjugates, which were purified by semi-preparative HPLC and characterized by analytical HPLC and mass spectrometry. Cobalt 41-47 mitochondrially encoded cytochrome c oxidase III Homo sapiens 138-145 31621305-3 2019 First, a novel oxamato-based tetranuclear cobalt(III) compound with a tetrahedron-shaped geometry is used, for the first time, as the metalloligand toward calcium(II) metal ions to lead to a diamagnetic CaII-CoIII three-dimensional (3D) MOF (1). Cobalt 42-53 mitochondrially encoded cytochrome c oxidase III Homo sapiens 208-213 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 III Homo sapiens 220-223 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 III Homo sapiens 139-145 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 III Homo sapiens 108-113 30964644-1 2019 Organocobalt(III) complexes (R-CoIII), defined as cobalt complexes featuring a carbon-cobalt bond, are largely used to produce carbon-centered radicals by homolytic cleavage of their C-Co bond under mild conditions. Cobalt 6-12 mitochondrially encoded cytochrome c oxidase III Homo sapiens 31-36 30964644-1 2019 Organocobalt(III) complexes (R-CoIII), defined as cobalt complexes featuring a carbon-cobalt bond, are largely used to produce carbon-centered radicals by homolytic cleavage of their C-Co bond under mild conditions. Cobalt 50-56 mitochondrially encoded cytochrome c oxidase III Homo sapiens 31-36 27475779-1 2016 Cobalt(III) complexes (1-3) such as [Co(acac)(bpy)(N3)2 H2O] 1, [Co(acac)(en)(N3)2] 2, and [Co(acac)(2-pic)(N3)2] 3 (where, acac=acetylacetone, bpy=2.2"-bipyridine, en=ethylenediamine, 2-pic=2-picolylamine and NaN3=sodium azide) were synthesized and characterized. Cobalt 0-6 mitochondrially encoded cytochrome c oxidase III Homo sapiens 7-10 29969023-8 2018 The basicity of cobalt center along with thermodynamic stability of putative CoIII/II-H species is essentially a prime factor in deciding the most favorable pathway for hydrogen evolution. Cobalt 16-22 mitochondrially encoded cytochrome c oxidase III Homo sapiens 77-82 28926691-7 2017 Dissolution of CP 3 in DMSO favors Co-S bond heterolysis, yielding the diamagnetic six-coordinate purple N-bound CoIII(TPP)(N-py-DTDA-)(O SMe2) complex (lambdamax, 436 nm). Cobalt 35-39 mitochondrially encoded cytochrome c oxidase III Homo sapiens 113-118 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 III Homo sapiens 213-218 27723326-0 2016 Isolation of Key Organometallic Aryl-Co(III) Intermediates in Cobalt-Catalyzed C(sp2)-H Functionalizations and New Insights into Alkyne Annulation Reaction Mechanisms. Cobalt 62-68 mitochondrially encoded cytochrome c oxidase III Homo sapiens 40-43 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 III Homo sapiens 160-167 29039921-4 2017 A linear correlation is observed between log(TOF) vs E1/2(CoIII/II) for the different cobalt complexes (TOF = turnover frequency). Cobalt 86-92 mitochondrially encoded cytochrome c oxidase III Homo sapiens 58-63 27533922-0 2016 Cobalt Kbeta valence-to-core X-ray emission spectroscopy: a study of low-spin octahedral cobalt(iii) complexes. Cobalt 0-6 mitochondrially encoded cytochrome c oxidase III Homo sapiens 96-99 27452370-1 2016 X-ray transient absorption spectroscopy (X-TAS) has been used to study the light-induced hydrogen evolution reaction catalyzed by a tetradentate macrocyclic cobalt complex with the formula [LCo(III)Cl2](+) (L = macrocyclic ligand), [Ru(bpy)3](2+) photosensitizer, and an equimolar mixture of sodium ascorbate/ascorbic acid electron donor in pure water. Cobalt 157-163 mitochondrially encoded cytochrome c oxidase III Homo sapiens 194-197 24826941-2 2014 The synthesis, structure and magnetic properties are reported of two disklike mixed-valence cobalt clusters [Co(III)Co(II)6(thmp)2(acac)6(ada)3] (1) and [Co(III)2Co(II)11(thmp)4(Me3CCOO)4(acac)6(OH)4(H2O)4](Me3CCOO)2 H2O (2). Cobalt 92-98 mitochondrially encoded cytochrome c oxidase III Homo sapiens 112-115 27555929-0 2016 Crystal structure of bis-{4-bromo-2-[(carb-amim-id-amido-imino)-meth-yl]phenolato-kappa(3) N,N",O}cobalt(III) nitrate di-methyl-formamide monosolvate. Cobalt 98-104 mitochondrially encoded cytochrome c oxidase III Homo sapiens 105-108 25529387-1 2015 The local electronic structure of the cobalt centre-ion of Co(III) protoporphyrin IX chloride dissolved in dimethyl sulfoxide (DMSO) liquid solution is studied by resonant inelastic X-ray scattering (RIXS) spectroscopy at the cobalt L-edge. Cobalt 38-44 mitochondrially encoded cytochrome c oxidase III Homo sapiens 59-66 25529387-1 2015 The local electronic structure of the cobalt centre-ion of Co(III) protoporphyrin IX chloride dissolved in dimethyl sulfoxide (DMSO) liquid solution is studied by resonant inelastic X-ray scattering (RIXS) spectroscopy at the cobalt L-edge. Cobalt 226-232 mitochondrially encoded cytochrome c oxidase III Homo sapiens 59-66 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 III Homo sapiens 61-68 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 III Homo sapiens 106-113 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 III Homo sapiens 220-227 24721109-9 2014 The log K values for [H2O-DPTC-Co] correlate reasonably well with those for H2OCbl(+); therefore, Co(III) displays a similar behavior toward these ligands irrespective of whether the equatorial ligand is a corrole or a corrin. Cobalt 31-33 mitochondrially encoded cytochrome c oxidase III Homo sapiens 98-104 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 III Homo sapiens 19-26 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 III Homo sapiens 34-41 24764829-0 2014 Tris(2,6-dibenzoyl-4-methyl-phenolato-kappa(2) O (1),O (2))cobalt(III). Cobalt 59-65 mitochondrially encoded cytochrome c oxidase III Homo sapiens 66-69 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 III Homo sapiens 58-65 22719350-0 2012 Tris(2-{[2-(4-meth-oxy-phen-yl)eth-yl]imino-meth-yl}phenolato-kappa(2)N,O(1))cobalt(III). Cobalt 77-83 mitochondrially encoded cytochrome c oxidase III Homo sapiens 84-87 22904723-0 2012 Tris[2,4-dichloro-6-(ethyl-imino-meth-yl)phenolato-kappa(2)N,O]cobalt(III). Cobalt 63-69 mitochondrially encoded cytochrome c oxidase III Homo sapiens 70-73 21963172-4 2011 The hydroxyl groups on the surface of Co-containing birnessites gradually decreased with an increase of Co/Mn molar ratio owing to the occupance of Co(III) into vacancies and the location of large amounts of Co(2+/3+) and Mn(2+/3+) above/below the vacant sites. Cobalt 38-40 mitochondrially encoded cytochrome c oxidase III Homo sapiens 148-155 21963172-4 2011 The hydroxyl groups on the surface of Co-containing birnessites gradually decreased with an increase of Co/Mn molar ratio owing to the occupance of Co(III) into vacancies and the location of large amounts of Co(2+/3+) and Mn(2+/3+) above/below the vacant sites. Cobalt 104-106 mitochondrially encoded cytochrome c oxidase III Homo sapiens 148-155 21942543-14 2011 On the basis of the electrostatic work term associated with bringing the two cobalt complexes together in solution, the preferred bimetallic pathway involves the reaction of two Co(III)H complexes to produce H(2). Cobalt 77-83 mitochondrially encoded cytochrome c oxidase III Homo sapiens 181-184 22219826-0 2011 fac-Tris(pyridine-2-carboxyl-ato-kappaN,O)cobalt(III). Cobalt 42-48 mitochondrially encoded cytochrome c oxidase III Homo sapiens 49-52 20729276-10 2010 Cobalt(III)hexamine contains high- and low-affinity sites in tRNA with K(1) = 3.2 x 10(5) M(-1) and K(2) = 1.7 x 10(5) M(-1), that have been attributed to the interactions with guanine-N7 sites and the backbone PO(2) group, respectively. Cobalt 0-6 mitochondrially encoded cytochrome c oxidase III Homo sapiens 7-10 22090917-1 2011 In the title complex, [Co(C(22)H(18)N(2)O(4))(CN)(H(2)O)] CH(3)CN, the Co(III) ion is six-coordinated in a distorted octa-hedral environment defined by two N atoms and two O atoms from a salen ligand in the equatorial plane and one O atom from a water mol-ecule and one C atom from a cyanide group at the axial positions. Cobalt 23-25 mitochondrially encoded cytochrome c oxidase III Homo sapiens 71-78 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 III Homo sapiens 158-165 20721276-1 2010 The use of 2-pyridinealdoxime (paoH)/N,N"-donor ligand (L-L) "blend" in cobalt chemistry has afforded two cationic mononuclear cobalt(III) complexes of the general type [Co(pao)(2)(L-L)](+), where L-L = 1,10-phenanthroline (phen) and 2,2"-bipyridine (bpy). Cobalt 72-78 mitochondrially encoded cytochrome c oxidase III Homo sapiens 134-137 20721276-1 2010 The use of 2-pyridinealdoxime (paoH)/N,N"-donor ligand (L-L) "blend" in cobalt chemistry has afforded two cationic mononuclear cobalt(III) complexes of the general type [Co(pao)(2)(L-L)](+), where L-L = 1,10-phenanthroline (phen) and 2,2"-bipyridine (bpy). Cobalt 127-133 mitochondrially encoded cytochrome c oxidase III Homo sapiens 134-137 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 III Homo sapiens 118-124 18717564-9 2008 The strong ferromagnetic interaction between distant cobalt ions arises as a result of low electron-promotion energies in the exchange bridges containing Co(III) ions. Cobalt 53-59 mitochondrially encoded cytochrome c oxidase III Homo sapiens 154-161 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 III Homo sapiens 121-124 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 III Homo sapiens 187-190 17949016-1 2007 We have shown that copper and cobalt metallosurfactants derived from Cu(II) and Co(III) complexes of a macrobicyclic hexamine ("cage") can form wormlike micelles in aqueous solution that may coexist with or easily interconvert with vesicle structures. Cobalt 30-36 mitochondrially encoded cytochrome c oxidase III Homo sapiens 80-87 17048265-0 2007 1H, 13C and 15N NMR coordination shifts in gold(III), cobalt(III), rhodium(III) chloride complexes with pyridine, 2,2"-bipyridine and 1,10-phenanthroline. Cobalt 54-60 mitochondrially encoded cytochrome c oxidase III Homo sapiens 61-64 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 III Homo sapiens 133-140 17048265-0 2007 1H, 13C and 15N NMR coordination shifts in gold(III), cobalt(III), rhodium(III) chloride complexes with pyridine, 2,2"-bipyridine and 1,10-phenanthroline. Cobalt 54-60 mitochondrially encoded cytochrome c oxidase III Homo sapiens 61-64 16456280-0 2006 A cobalt(III) compound of a 13-membered cyclic tetraamine: trans-(12,12-dimethyl-1,4,7,10-tetraazacyclotetradecane)diisothiocyanatocobalt(III) tetraisothiocyanatozinc(II) ethanol solvate. Cobalt 2-8 mitochondrially encoded cytochrome c oxidase III Homo sapiens 9-12 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 III Homo sapiens 10-17 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 III Homo sapiens 18-25 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 III Homo sapiens 18-25 16456280-0 2006 A cobalt(III) compound of a 13-membered cyclic tetraamine: trans-(12,12-dimethyl-1,4,7,10-tetraazacyclotetradecane)diisothiocyanatocobalt(III) tetraisothiocyanatozinc(II) ethanol solvate. Cobalt 2-8 mitochondrially encoded cytochrome c oxidase III Homo sapiens 138-141 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 III Homo sapiens 207-212 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 III Homo sapiens 151-158 15540136-1 2004 A series of novel half-sandwich M(I) and M(III) complexes (M = Co, Rh) bearing the N-heterocyclic carbene ligand 1,3-dimesitylimidazol-2-ylidene (IMes) have been prepared and characterized. Cobalt 63-65 mitochondrially encoded cytochrome c oxidase III Homo sapiens 43-46 15600324-0 2004 Terminal cobalt(III) imido complexes supported by tris(carbene) ligands: imido insertion into the cobalt-carbene bond. Cobalt 9-15 mitochondrially encoded cytochrome c oxidase III Homo sapiens 16-19 12400832-7 2002 At higher pH, Co was transported primarily as Co(II)NTA and the Co(III) species Co(III)(HNTA)2 and Co(III)(IDA)2. Cobalt 14-16 mitochondrially encoded cytochrome c oxidase III Homo sapiens 64-71 12950226-16 2003 The required presence of a Cys-sulfinic residue and one water molecule at the Co(III) site of Co-NHase as well as the optimal pH of the enzyme near 7 suggests that (i) modulation of the pK(a) of the bound water molecule at the active site of the enzyme could be one role of the oxidized Cys-S residue(s) and (ii) a cobalt-bound hydroxide could be responsible for the hydrolysis of nitriles by Co-NHase. Cobalt 315-321 mitochondrially encoded cytochrome c oxidase III Homo sapiens 81-84 12603151-13 2003 The slow self-exchange rates for the cobalt complexes are apparently due to their interconverting high-spin [Co(II)(H(2)bim)(3)](2+) with low-spin Co(III) derivatives. Cobalt 37-43 mitochondrially encoded cytochrome c oxidase III Homo sapiens 147-154 12400832-7 2002 At higher pH, Co was transported primarily as Co(II)NTA and the Co(III) species Co(III)(HNTA)2 and Co(III)(IDA)2. Cobalt 14-16 mitochondrially encoded cytochrome c oxidase III Homo sapiens 67-70 12400832-7 2002 At higher pH, Co was transported primarily as Co(II)NTA and the Co(III) species Co(III)(HNTA)2 and Co(III)(IDA)2. Cobalt 14-16 mitochondrially encoded cytochrome c oxidase III Homo sapiens 83-86 12121784-0 2002 Structures of HO(2)-Co(III)bleomycin A(2) bound to d(GAGCTC)(2) and d(GGAAGCTTCC)(2): structure-reactivity relationships of Co and Fe bleomycins. Cobalt 20-22 mitochondrially encoded cytochrome c oxidase III Homo sapiens 23-26 12224970-0 2002 Substituted polypyridine complexes of cobalt(II/III) as efficient electron-transfer mediators in dye-sensitized solar cells. Cobalt 38-44 mitochondrially encoded cytochrome c oxidase III Homo sapiens 48-51 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 III Homo sapiens 181-186 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 III Homo sapiens 226-233 11421673-20 2001 Importantly, this is the first computational rationalization of the (59)Co NMR spectra of Co(III) porphyrins. Cobalt 72-74 mitochondrially encoded cytochrome c oxidase III Homo sapiens 90-97 11456548-6 2001 Complex 2 is a six-coordinate Co(III) complex containing cis-thiolates and imine nitrogens, and has properties similar to the cobalt center of Co NHase. Cobalt 126-132 mitochondrially encoded cytochrome c oxidase III Homo sapiens 33-36 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 III Homo sapiens 19-26 10572911-5 1999 In contrast, high leukocyte and erythrocyte labelling efficiencies (> 90%) were obtained with 57Co(III) tropolonate containing cobalt carrier and the elution in cell-free plasma over 4 h was < 8%. Cobalt 130-136 mitochondrially encoded cytochrome c oxidase III Homo sapiens 102-105 11670645-2 1998 The synthesis of monometallic cobalt(III) and -(I) complexes of ((dimethylamino)ethyl)cyclopentadienyl are reported. Cobalt 30-36 mitochondrially encoded cytochrome c oxidase III Homo sapiens 37-40 26236964-0 2015 Time-Resolved Investigation of Cobalt Oxidation by Mn(III)-Rich delta-MnO2 Using Quick X-ray Absorption Spectroscopy. Cobalt 31-37 mitochondrially encoded cytochrome c oxidase III Homo sapiens 54-57 34951771-5 2022 The cobalt-based catalyst was characterized by several methods and is suggested to be Co(III) (hydr)oxide. Cobalt 4-10 mitochondrially encoded cytochrome c oxidase III Homo sapiens 86-93 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 III Homo sapiens 211-216 210789-2 1978 Co(III)-carboxypeptidase A, isolated by affinity gel filtration chromatography, has the same amino acid composition and molecular weight as the starting material and contains 0.95 g-atom/mol of cobalt and 0.01 g-atom/mol of zinc. Cobalt 194-200 mitochondrially encoded cytochrome c oxidase III Homo sapiens 3-6 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 III Homo sapiens 143-150 18967335-2 1998 The cobalt ion released by the oxidative decomposition of inert bis[2-(5-bromo-2-pyridylazo)-5-(N-propyl-N-sulfopropyl-amino-phenolato] cobaltate (Co(III)-5-Br-PAPS) with peroxomonosulfate acts as a catalyst for the oxidative degradation of the complex. Cobalt 4-10 mitochondrially encoded cytochrome c oxidase III Homo sapiens 150-153 34499506-11 2021 We thus demonstrate that high-performance cobalt-based OER catalysts indeed emerge effortlessly from a self-optimization process favoring the formation of Co(III) centers in all-octahedral environments. Cobalt 42-48 mitochondrially encoded cytochrome c oxidase III Homo sapiens 155-162 34397061-3 2021 Herein, we report the preparation of one such cobalt(iii) hydride: (Cp*CoIII(P2BCy4)(H))BPh4 (Cp* = C5Me5-, P2BCy4 = 1,2-bis(di(3-dicyclohexylborane)propylphosphino)ethane) that is encircled by a boron-based Lewis-acidic secondary coordination sphere. Cobalt 46-65 mitochondrially encoded cytochrome c oxidase III Homo sapiens 71-76 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 III Homo sapiens 100-107 33847448-1 2021 Reaction of the cobalt(I) complex [(TIMMN mes )Co I ](BPh 4 ) ( 2 ) (TIMMN mes = t ris -[2-(3-mesityl- im idazolin-2-ylidene)- m ethyl]-ami n e) with 1-adamantyl azide yields the cobalt(III) imido complex [(TIMMN mes )Co III (NAd)](BPh 4 ) ( 3 ) with concomitant release of dinitro-gen. Cobalt 16-25 mitochondrially encoded cytochrome c oxidase III Homo sapiens 218-224 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 III Homo sapiens 103-106 32810326-1 2021 The cobalt species PPh 4 [Co III (TAML red )] is a competent and stable catalyst for the sulfimidation of (aryl)(alkyl)-substituted sulfides with iminoiodinanes reaching turnover numbers up to 900 and turnover frequencies of 640 min -1 under mild and aerobic conditions. Cobalt 4-10 mitochondrially encoded cytochrome c oxidase III Homo sapiens 26-32 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 III Homo sapiens 62-67 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 III Homo sapiens 73-78 32239007-1 2020 Cobalt complexes have been demonstrated to target zinc fingers, as shown by investigations of Doxovir, the trade name of the [CoIII(acacen)(2-Me-Imz)2]+ drug in clinical trials. Cobalt 0-6 mitochondrially encoded cytochrome c oxidase III Homo sapiens 126-131