PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24300990-10 2014 While additions of THF and I2/I(-) both result in the formation of five-coordinate complexes, Co(II) is oxidized to Co(III) in the case of the latter. co(iii) 116-123 mitochondrially encoded cytochrome c oxidase II Homo sapiens 94-100 24300990-11 2014 However, additions of 1-methylimidazole, pyridine and pyrazine as axial ligands result in the formation of a six-coordinate complex in which Co(II) is spontaneously oxidized to Co(III) in air. co(iii) 177-184 mitochondrially encoded cytochrome c oxidase II Homo sapiens 141-147 22764083-3 2012 The reaction occurs through a single-electron transfer from the doublet Co(II) catalyst to the epoxide and forms a doublet Co(III)-carbon radical intermediate. co(iii) 123-130 mitochondrially encoded cytochrome c oxidase II Homo sapiens 72-78 24044879-0 2013 Tuning transverse anisotropy in Co(III)-Co(II)-Co(III) mixed-valence complex toward slow magnetic relaxation. co(iii) 32-39 mitochondrially encoded cytochrome c oxidase II Homo sapiens 40-46 24044879-0 2013 Tuning transverse anisotropy in Co(III)-Co(II)-Co(III) mixed-valence complex toward slow magnetic relaxation. co(iii) 47-54 mitochondrially encoded cytochrome c oxidase II Homo sapiens 40-46 23557586-1 2013 The reaction of the multisite coordination ligand (LH4) with CoX2 nH2O in the presence of tetrabutylammonium hydroxide affords a series of homometallic dinuclear mixed-valence complexes, [Co(III)Co(II)(LH2)2(X)(H2O)](H2O)m (1, X = Cl and m = 4; 2, X = Br and m = 4; 3, X = NO3 and m = 3). co(iii) 188-195 mitochondrially encoded cytochrome c oxidase II Homo sapiens 61-65 23343346-4 2013 The detailed kinetic studies have revealed that the rate-determining step in the catalytic cycle is the proton-coupled electron transfer reduction of O(2) with the protonated Co(II)(Ch) ([Co(II)(ChH)](+)) that is produced by facile electron-transfer reduction of [Co(III)(ChH)](2+) by ferrocene derivative in the presence of HClO(4). co(iii) 264-271 mitochondrially encoded cytochrome c oxidase II Homo sapiens 175-185 23343346-4 2013 The detailed kinetic studies have revealed that the rate-determining step in the catalytic cycle is the proton-coupled electron transfer reduction of O(2) with the protonated Co(II)(Ch) ([Co(II)(ChH)](+)) that is produced by facile electron-transfer reduction of [Co(III)(ChH)](2+) by ferrocene derivative in the presence of HClO(4). co(iii) 264-271 mitochondrially encoded cytochrome c oxidase II Homo sapiens 175-181 23343346-6 2013 Such a positive shift of [Co(III)(Ch)](+) by protonation resulted in enhancement of the catalytic reactivity of [Co(III)(ChH)](2+) for the two-electron reduction of O(2) with a lower overpotential as compared with that of [Co(III)(OEP)](+). co(iii) 26-33 mitochondrially encoded cytochrome c oxidase II Homo sapiens 231-234 23343346-6 2013 Such a positive shift of [Co(III)(Ch)](+) by protonation resulted in enhancement of the catalytic reactivity of [Co(III)(ChH)](2+) for the two-electron reduction of O(2) with a lower overpotential as compared with that of [Co(III)(OEP)](+). co(iii) 113-120 mitochondrially encoded cytochrome c oxidase II Homo sapiens 231-234 23343346-6 2013 Such a positive shift of [Co(III)(Ch)](+) by protonation resulted in enhancement of the catalytic reactivity of [Co(III)(ChH)](2+) for the two-electron reduction of O(2) with a lower overpotential as compared with that of [Co(III)(OEP)](+). co(iii) 113-120 mitochondrially encoded cytochrome c oxidase II Homo sapiens 231-234 23092306-7 2012 XPS determined binding energies were interpreted to imply that after oxidation in an oxygen/argon mixture of the grafted sample both Pd(II) and Co(II) were oxidized to produce PdO(2) (337.5 eV) and Co(III)(2)O(3) (781.1 eV) which most probably interacts with the silicon surface via Pd(IV)-O-Si and Co(III)-O-Si bonds. co(iii) 198-205 mitochondrially encoded cytochrome c oxidase II Homo sapiens 144-150 11944671-8 2002 The extent of the Co(ll) sorption reduction in Co(III)/Se(IV) bisorbate systems compared to the corresponding single-sorbate systems increased with increasing Co(II) surface coverage. co(iii) 47-54 mitochondrially encoded cytochrome c oxidase II Homo sapiens 159-165 22418687-5 2012 The utilisation of other Co(II) salt precursors gives rise to entirely different species including the mononuclear and trinuclear complexes [Co(II)(L(2))(2)] (5) and [Co(III)(2)Na(I)(1)(L(3))(6)](BF(4)) (6) (where L(3)H = 2-iminomethyl-4-bromo-6-methoxyphenol). co(iii) 167-174 mitochondrially encoded cytochrome c oxidase II Homo sapiens 25-31 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). co(iii) 71-78 mitochondrially encoded cytochrome c oxidase II Homo sapiens 86-92 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). co(iii) 102-109 mitochondrially encoded cytochrome c oxidase II Homo sapiens 86-92 21265566-6 2011 On the basis of the shape of the absorption spectra, it was found that Co(II) is partly oxidized to Co(III). co(iii) 100-107 mitochondrially encoded cytochrome c oxidase II Homo sapiens 71-77 21265566-8 2011 Thus, this study suggests that thermodynamic calculations of Co(II)-immobilization by cementitious systems should take into consideration not only the solubility of Co(II)-hydroxides but also Co(III) phases. co(iii) 192-199 mitochondrially encoded cytochrome c oxidase II Homo sapiens 61-67 19624164-5 2009 This analysis demonstrated that the formed carboxylate intermediate helped to stabilize the active Co(III) species against decomposition to inactive Co(II) by reversibly intramolecular Co-O bond formation and dissociation. co(iii) 99-106 mitochondrially encoded cytochrome c oxidase II Homo sapiens 149-155 19358538-10 2009 The first three correspond to [Co(II)DBQ(2-)Co(II)](2+) reduction to [Co(II)DBQ(*3-)Co(II)](+), and oxidation to [Co(III)DBQ(*3-)Co(III)](3+) and [Co(III)DBQ(2-)Co(III)](4+), respectively. co(iii) 129-136 mitochondrially encoded cytochrome c oxidase II Homo sapiens 44-50 18985241-2 2008 Crystal structural analysis revealed that two Co(III) ions were linked to a central triangular Co(II) core through HL(3-) and H2L(2-) hydroxyl groups. co(iii) 46-53 mitochondrially encoded cytochrome c oxidase II Homo sapiens 95-101 17054329-3 2006 The result is that sequential switching from high-spin Co(II) to low-spin Co(III) of one center, followed by the onset of switching of the other center at lower temperature, is observed in a solid amorphous thin film by IR absorption spectroscopy. co(iii) 74-81 mitochondrially encoded cytochrome c oxidase II Homo sapiens 55-61 22998407-10 2012 Allowing [Co(III)(mu-OH)Ca(II)](+) to react with diphenylhydrazine afforded [Co(II)(mu-OH(2))Ca(II)OH(2)](+) and azobenzene. co(iii) 10-17 mitochondrially encoded cytochrome c oxidase II Homo sapiens 77-83 22175783-2 2012 Upon O(2) binding to the high-spin Co(II) (S = (3)/(2)) enzyme-substrate complex, an S = (1)/(2) EPR signal exhibiting (59)Co hyperfine splitting (A = 24 G) typical of a low-spin Co(III)-superoxide complex was observed. co(iii) 179-186 mitochondrially encoded cytochrome c oxidase II Homo sapiens 35-41 19358538-4 2009 Valence ambiguous 1(3+) forms via redox-induced electron transfer, whereby the one-electron oxidation of the [Co(II)(DBQ(2-))Co(II)](2+) core forms [Co(III)(DBQ(*3-))Co(III)](3+), and it also exhibits spin crossover behavior to the core [Co(III)(DBQ(2-))Co(II)](3+) above room temperature. co(iii) 149-156 mitochondrially encoded cytochrome c oxidase II Homo sapiens 110-116 19358538-4 2009 Valence ambiguous 1(3+) forms via redox-induced electron transfer, whereby the one-electron oxidation of the [Co(II)(DBQ(2-))Co(II)](2+) core forms [Co(III)(DBQ(*3-))Co(III)](3+), and it also exhibits spin crossover behavior to the core [Co(III)(DBQ(2-))Co(II)](3+) above room temperature. co(iii) 149-156 mitochondrially encoded cytochrome c oxidase II Homo sapiens 125-131 19358538-4 2009 Valence ambiguous 1(3+) forms via redox-induced electron transfer, whereby the one-electron oxidation of the [Co(II)(DBQ(2-))Co(II)](2+) core forms [Co(III)(DBQ(*3-))Co(III)](3+), and it also exhibits spin crossover behavior to the core [Co(III)(DBQ(2-))Co(II)](3+) above room temperature. co(iii) 149-156 mitochondrially encoded cytochrome c oxidase II Homo sapiens 125-131 19358538-4 2009 Valence ambiguous 1(3+) forms via redox-induced electron transfer, whereby the one-electron oxidation of the [Co(II)(DBQ(2-))Co(II)](2+) core forms [Co(III)(DBQ(*3-))Co(III)](3+), and it also exhibits spin crossover behavior to the core [Co(III)(DBQ(2-))Co(II)](3+) above room temperature. co(iii) 166-173 mitochondrially encoded cytochrome c oxidase II Homo sapiens 110-116 19358538-4 2009 Valence ambiguous 1(3+) forms via redox-induced electron transfer, whereby the one-electron oxidation of the [Co(II)(DBQ(2-))Co(II)](2+) core forms [Co(III)(DBQ(*3-))Co(III)](3+), and it also exhibits spin crossover behavior to the core [Co(III)(DBQ(2-))Co(II)](3+) above room temperature. co(iii) 166-173 mitochondrially encoded cytochrome c oxidase II Homo sapiens 125-131 19358538-4 2009 Valence ambiguous 1(3+) forms via redox-induced electron transfer, whereby the one-electron oxidation of the [Co(II)(DBQ(2-))Co(II)](2+) core forms [Co(III)(DBQ(*3-))Co(III)](3+), and it also exhibits spin crossover behavior to the core [Co(III)(DBQ(2-))Co(II)](3+) above room temperature. co(iii) 166-173 mitochondrially encoded cytochrome c oxidase II Homo sapiens 125-131 19358538-10 2009 The first three correspond to [Co(II)DBQ(2-)Co(II)](2+) reduction to [Co(II)DBQ(*3-)Co(II)](+), and oxidation to [Co(III)DBQ(*3-)Co(III)](3+) and [Co(III)DBQ(2-)Co(III)](4+), respectively. co(iii) 129-136 mitochondrially encoded cytochrome c oxidase II Homo sapiens 31-37 19358538-10 2009 The first three correspond to [Co(II)DBQ(2-)Co(II)](2+) reduction to [Co(II)DBQ(*3-)Co(II)](+), and oxidation to [Co(III)DBQ(*3-)Co(III)](3+) and [Co(III)DBQ(2-)Co(III)](4+), respectively. co(iii) 129-136 mitochondrially encoded cytochrome c oxidase II Homo sapiens 44-50 19358538-10 2009 The first three correspond to [Co(II)DBQ(2-)Co(II)](2+) reduction to [Co(II)DBQ(*3-)Co(II)](+), and oxidation to [Co(III)DBQ(*3-)Co(III)](3+) and [Co(III)DBQ(2-)Co(III)](4+), respectively. co(iii) 129-136 mitochondrially encoded cytochrome c oxidase II Homo sapiens 31-37 19308980-7 2009 The reversal of relative effective OMRP rate constants k(eff) (4>1 in the absence of external donors, 4<1 in their presence) is rationalized through competitive steric effects on Co(III)-C and Co(II)-L bond strengths. co(iii) 185-192 mitochondrially encoded cytochrome c oxidase II Homo sapiens 199-205 15010798-0 2004 A novel mixed-valence complex containing Co(II)(2)Co(III)(2) molecular squares with 4,5-imidazoledicarboxylate bridges. co(iii) 50-57 mitochondrially encoded cytochrome c oxidase II Homo sapiens 41-47 11681893-1 2001 The electro-oxidation of cobalt (II) octaethylporphyrin adsorbed on graphite electrodes, Co(II)(OEP)(ads") to Co(III)(OEP)(ads)(+), in the presence of aqueous solutions of CO leads to catalytic oxidation of CO to CO(2). co(iii) 110-117 mitochondrially encoded cytochrome c oxidase II Homo sapiens 89-95 11681893-1 2001 The electro-oxidation of cobalt (II) octaethylporphyrin adsorbed on graphite electrodes, Co(II)(OEP)(ads") to Co(III)(OEP)(ads)(+), in the presence of aqueous solutions of CO leads to catalytic oxidation of CO to CO(2). co(iii) 110-117 mitochondrially encoded cytochrome c oxidase II Homo sapiens 96-99 11681893-1 2001 The electro-oxidation of cobalt (II) octaethylporphyrin adsorbed on graphite electrodes, Co(II)(OEP)(ads") to Co(III)(OEP)(ads)(+), in the presence of aqueous solutions of CO leads to catalytic oxidation of CO to CO(2). co(iii) 110-117 mitochondrially encoded cytochrome c oxidase II Homo sapiens 118-121 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. co(iii) 224-231 mitochondrially encoded cytochrome c oxidase II Homo sapiens 217-223 33819782-8 2021 Co(II) Co(III) Co(II) redox reaction cycle was constructed due to the different redox potential of Co(II)/Co(III), HSO5-/SO4 -, and HSO5-/SO5 -. co(iii) 7-14 mitochondrially encoded cytochrome c oxidase II Homo sapiens 15-21 33819782-8 2021 Co(II) Co(III) Co(II) redox reaction cycle was constructed due to the different redox potential of Co(II)/Co(III), HSO5-/SO4 -, and HSO5-/SO5 -. co(iii) 7-14 mitochondrially encoded cytochrome c oxidase II Homo sapiens 15-21 33819782-8 2021 Co(II) Co(III) Co(II) redox reaction cycle was constructed due to the different redox potential of Co(II)/Co(III), HSO5-/SO4 -, and HSO5-/SO5 -. co(iii) 106-113 mitochondrially encoded cytochrome c oxidase II Homo sapiens 15-21 33819782-8 2021 Co(II) Co(III) Co(II) redox reaction cycle was constructed due to the different redox potential of Co(II)/Co(III), HSO5-/SO4 -, and HSO5-/SO5 -. co(iii) 106-113 mitochondrially encoded cytochrome c oxidase II Homo sapiens 15-21 34862103-5 2022 Meanwhile, cobalt doping promotes H2O2 decomposition by accelerated Fe(II)/Fe(III) cycle and Co(II)/Co(III) redox. co(iii) 100-107 mitochondrially encoded cytochrome c oxidase II Homo sapiens 93-99 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. co(iii) 55-62 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. co(iii) 101-108 mitochondrially encoded cytochrome c oxidase II Homo sapiens 94-100 34548209-4 2021 HCbl is known to be a transient species where the oxidation state of the Co is variable; Co(I)-H+ Co(II)-H Co(III)-H-. co(iii) 111-118 mitochondrially encoded cytochrome c oxidase II Homo sapiens 100-106 6186274-2 1982 Co(II) interacts with bleomycin in aqueous solution, in the presence of air, to give a short-lived mononuclear superoxo Co(III) complex (I). co(iii) 120-127 mitochondrially encoded cytochrome c oxidase II Homo sapiens 0-6 35395537-6 2022 Simultaneously, the internal electron exchange occurs between Co(II)/Co(III) and V(IV)/V(V), which stabilizes the content of Co(II) and V(IV). co(iii) 69-76 mitochondrially encoded cytochrome c oxidase II Homo sapiens 62-68 35395537-6 2022 Simultaneously, the internal electron exchange occurs between Co(II)/Co(III) and V(IV)/V(V), which stabilizes the content of Co(II) and V(IV). co(iii) 69-76 mitochondrially encoded cytochrome c oxidase II Homo sapiens 125-131 35476545-2 2022 The triple catalysis realizes three key elementary steps in a single catalytic cycle: (1) Co(III) hydride generation by photochemical reduction of Co(II) followed by protonation, (2) metal hydride hydrogen atom transfer (MHAT) of alkenes by Co(III) hydride, and (3) oxidation of the alkyl Co(III) complex to alkyl Co(IV). co(iii) 90-97 mitochondrially encoded cytochrome c oxidase II Homo sapiens 147-153 35476545-2 2022 The triple catalysis realizes three key elementary steps in a single catalytic cycle: (1) Co(III) hydride generation by photochemical reduction of Co(II) followed by protonation, (2) metal hydride hydrogen atom transfer (MHAT) of alkenes by Co(III) hydride, and (3) oxidation of the alkyl Co(III) complex to alkyl Co(IV). co(iii) 289-296 mitochondrially encoded cytochrome c oxidase II Homo sapiens 147-153 35172100-3 2022 An experimental study of the catalyst showed that the increase in the acetic acid concentration triggers catalytic current and reduction of Co(II) to Co(I), and protonation occurred, yielding a Co(III)-H intermediate. co(iii) 194-201 mitochondrially encoded cytochrome c oxidase II Homo sapiens 140-146 35424567-9 2022 Proposed radical and redox mechanisms are presented for H2O2 decomposition where the redox mechanism is suggested to predominate via a Co(ii)/Co(iii) redox consecutive cyclic process. co(iii) 142-149 mitochondrially encoded cytochrome c oxidase II Homo sapiens 135-141 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. co(iii) 208-215 mitochondrially encoded cytochrome c oxidase II Homo sapiens 201-207 35049285-0 2022 Facile Transformations of a Binuclear Cp*Co(II) Diamidonaphthalene Complex to Mixed-Valent Co(II)Co(III), Co(III)(mu-H)Co(III), and Co(III)(mu-OH)Co(III) Derivatives. co(iii) 97-104 mitochondrially encoded cytochrome c oxidase II Homo sapiens 41-47 35049285-0 2022 Facile Transformations of a Binuclear Cp*Co(II) Diamidonaphthalene Complex to Mixed-Valent Co(II)Co(III), Co(III)(mu-H)Co(III), and Co(III)(mu-OH)Co(III) Derivatives. co(iii) 119-126 mitochondrially encoded cytochrome c oxidase II Homo sapiens 41-47 35049285-0 2022 Facile Transformations of a Binuclear Cp*Co(II) Diamidonaphthalene Complex to Mixed-Valent Co(II)Co(III), Co(III)(mu-H)Co(III), and Co(III)(mu-OH)Co(III) Derivatives. co(iii) 146-153 mitochondrially encoded cytochrome c oxidase II Homo sapiens 41-47 31339119-6 2019 Interestingly, the Co(ii)/Co(iii) mixed-valence complex 6 resulted from the treatment of 1 with silver perchlorate (1.0 equiv.) co(iii) 26-33 mitochondrially encoded cytochrome c oxidase II Homo sapiens 19-25 33621088-8 2021 Together, these experiments reveal the details of the reaction mechanism: reduction of the Co(III) species is followed by dissociation of the bound acetonitrile ligand, subsequent reduction of the unligated Co(II) species to form a Co(I) species is followed by protonation, which occurs at the Cp ring, followed by tautomerization to generate the stable Co(III)-hydride product [HCoCp(dxpe)]+. co(iii) 91-98 mitochondrially encoded cytochrome c oxidase II Homo sapiens 207-213 31393480-5 2019 The complexes displayed a quasi-reversible Co(i)/Co(ii) redox couple at ~-1.1 V and an irreversible Co(ii)/Co(iii) couple at ~1.3 V vs. Ag/AgCl in DMF-0.1 M [Bun4N](ClO4). co(iii) 107-114 mitochondrially encoded cytochrome c oxidase II Homo sapiens 100-106 182215-6 1976 The quaternary adducts formed by H2O2 oxidation in the presence of aspartokinase, Co(II), ATP, aspartate, and threonine comprised a mixture of both ezyme-Co(III)-ATP-aspartate and enzyme-Co(III)-ATP-threonine adducts. co(iii) 154-161 mitochondrially encoded cytochrome c oxidase II Homo sapiens 82-87 182215-6 1976 The quaternary adducts formed by H2O2 oxidation in the presence of aspartokinase, Co(II), ATP, aspartate, and threonine comprised a mixture of both ezyme-Co(III)-ATP-aspartate and enzyme-Co(III)-ATP-threonine adducts. co(iii) 187-194 mitochondrially encoded cytochrome c oxidase II Homo sapiens 82-87 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. co(iii) 91-98 mitochondrially encoded cytochrome c oxidase II Homo sapiens 84-90 32814135-5 2021 Based on the characterization results, the sulfate radicals and hydroxyl radicals were considered to be the main free radicals which were involved into the circulation of Co(II)-Co(III)-Co(II) as well as the oxidation of Fe(II), which was responsible for the remarkable catalytic efficiency. co(iii) 178-185 mitochondrially encoded cytochrome c oxidase II Homo sapiens 171-177 32814135-5 2021 Based on the characterization results, the sulfate radicals and hydroxyl radicals were considered to be the main free radicals which were involved into the circulation of Co(II)-Co(III)-Co(II) as well as the oxidation of Fe(II), which was responsible for the remarkable catalytic efficiency. co(iii) 178-185 mitochondrially encoded cytochrome c oxidase II Homo sapiens 186-192 32947702-7 2020 Mechanism investigation suggested that the oxygen vacancies, redox cycles of Co(II)/Co(III) and S22-/(S2- and sulfate species) on the surface of 0.2CoAl-LDH@CoSx were crucial for PMS activation. co(iii) 84-91 mitochondrially encoded cytochrome c oxidase II Homo sapiens 77-83 32464763-8 2020 It was suspected that O2 - and H2O2 played important roles in the formation of OH and the cycle of Co(II)/Co(III) and Ni(II)/Ni(III). co(iii) 107-114 mitochondrially encoded cytochrome c oxidase II Homo sapiens 100-106 30962670-6 2019 Monitoring the addition of HBPin to [(iPrPNP)Co(N2)]+ provided evidence for a transient Co(III) oxidative addition product that likely undergoes comproportionation with the cobalt(I) starting material to generate the observed Co(II) products. co(iii) 88-95 mitochondrially encoded cytochrome c oxidase II Homo sapiens 226-232 29850706-6 2018 The electrochemical properties of complex 5 were investigated in DMF, and the Co(ii)/Co(iii) redox couple was found to be negatively shifted compared to that of complex 1, while the ligand-based processes became irreversible. co(iii) 85-92 mitochondrially encoded cytochrome c oxidase II Homo sapiens 78-84 28347141-3 2017 Here we demonstrate that elemental halogens quantitatively oxidize coordinatively unsaturated Co(II) ions in a robust azolate metal-organic framework (MOF) to produce stable and safe-to-handle Co(III) materials featuring terminal Co(III)-halogen bonds. co(iii) 193-200 mitochondrially encoded cytochrome c oxidase II Homo sapiens 94-100 28347141-3 2017 Here we demonstrate that elemental halogens quantitatively oxidize coordinatively unsaturated Co(II) ions in a robust azolate metal-organic framework (MOF) to produce stable and safe-to-handle Co(III) materials featuring terminal Co(III)-halogen bonds. co(iii) 230-237 mitochondrially encoded cytochrome c oxidase II Homo sapiens 94-100 26538114-2 2015 Cyclic voltammetry (CV) investigations revealed that Co(II)-Co(III) oxidation is a diffusion controlled electron transfer process. co(iii) 60-67 mitochondrially encoded cytochrome c oxidase II Homo sapiens 53-59 26820843-6 2016 The subsequent oxidation of the Co(II) ions inside the macrocycle into Co(III) ions made the metal-ligand bonds almost inert, thus affording a kinetically locked 4 : 4 metallomacrocycle. co(iii) 71-78 mitochondrially encoded cytochrome c oxidase II Homo sapiens 32-38 26323791-2 2015 [Co(III)(Ch)](+) was reduced by ascorbate to reproduce Co(II)(Ch). co(iii) 1-8 mitochondrially encoded cytochrome c oxidase II Homo sapiens 55-61 24802678-9 2014 Marcus diagram is derived for the electron transfer reaction Co(II) + D35(+) Co(III) + D35 using the Co-N bond length as a reaction coordinate. co(iii) 78-85 mitochondrially encoded cytochrome c oxidase II Homo sapiens 61-67 25537966-1 2015 We are reporting two new mixed valent Co(ii)/Co(iii) polynuclear complexes, {Co(II)6Co(III)3} and {Co(II)Co(III)4}, bearing different amount of Co(ii) ions in their cores, through the employment of the multidentate triethanolamine (teaH3) ligand in different stoichiometric ratios. co(iii) 45-52 mitochondrially encoded cytochrome c oxidase II Homo sapiens 38-44 25537966-1 2015 We are reporting two new mixed valent Co(ii)/Co(iii) polynuclear complexes, {Co(II)6Co(III)3} and {Co(II)Co(III)4}, bearing different amount of Co(ii) ions in their cores, through the employment of the multidentate triethanolamine (teaH3) ligand in different stoichiometric ratios. co(iii) 45-52 mitochondrially encoded cytochrome c oxidase II Homo sapiens 80-82 25537966-1 2015 We are reporting two new mixed valent Co(ii)/Co(iii) polynuclear complexes, {Co(II)6Co(III)3} and {Co(II)Co(III)4}, bearing different amount of Co(ii) ions in their cores, through the employment of the multidentate triethanolamine (teaH3) ligand in different stoichiometric ratios. co(iii) 45-52 mitochondrially encoded cytochrome c oxidase II Homo sapiens 87-89 25537966-1 2015 We are reporting two new mixed valent Co(ii)/Co(iii) polynuclear complexes, {Co(II)6Co(III)3} and {Co(II)Co(III)4}, bearing different amount of Co(ii) ions in their cores, through the employment of the multidentate triethanolamine (teaH3) ligand in different stoichiometric ratios. co(iii) 45-52 mitochondrially encoded cytochrome c oxidase II Homo sapiens 144-150