PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 34380313-2 2021 We recently reported a Co(III)-N2O2 complex with a 2,2"-bipyridine-based ligand backbone which showed alternative selectivity: H2O was observed as the primary reduction product from O2 (71 +- 5%) with decamethylferrocene as a chemical reductant and acetic acid as a proton donor in methanol solution. Methanol 282-290 mitochondrially encoded cytochrome c oxidase III Homo sapiens 23-30 21836833-1 2011 The title mononuclear cobalt(III) complex, [Co(C(14)H(19)N(2)O(2))(C(8)H(7)O(2))(NCS)], was obtained by the reaction of 2-acetyl-phenol, 2-(morpholin-4-yl)ethyl-amine, ammonium thio-cyan-ate and cobalt nitrate in methanol. Methanol 213-221 mitochondrially encoded cytochrome c oxidase III Homo sapiens 29-32 26143270-6 2015 The contribution of Co(III) to the bromate formation was verified with the addition of methanol and EDTA, a radical scavenger and a Co(III) ligand, respectively. Methanol 87-95 mitochondrially encoded cytochrome c oxidase III Homo sapiens 20-26 26143270-6 2015 The contribution of Co(III) to the bromate formation was verified with the addition of methanol and EDTA, a radical scavenger and a Co(III) ligand, respectively. Methanol 87-95 mitochondrially encoded cytochrome c oxidase III Homo sapiens 23-26 26143270-7 2015 In the presence of methanol, free bromine formation increased with increasing Co(II) dosage but no bromate was detected, indicating that Co(III) oxidized bromide to form free bromine but not bromate. Methanol 19-27 mitochondrially encoded cytochrome c oxidase III Homo sapiens 137-143 26143270-8 2015 In the presence of both EDTA and methanol, no free bromine or bromate was detected, as Co(III) was stabilized by EDTA to form the Co(III)EDTA(-) complex, which could not oxidize bromide. Methanol 33-41 mitochondrially encoded cytochrome c oxidase III Homo sapiens 87-94 26143270-8 2015 In the presence of both EDTA and methanol, no free bromine or bromate was detected, as Co(III) was stabilized by EDTA to form the Co(III)EDTA(-) complex, which could not oxidize bromide. Methanol 33-41 mitochondrially encoded cytochrome c oxidase III Homo sapiens 90-93 25604356-2 2015 These complexes are described as [Co(III)(L(X))MeOH], where X indicates the presence of chloro (), bromo (), iodo (), or tert-butyl () substituents in the 3(rd) and 5(th) positions of each phenolate ring. Methanol 47-51 mitochondrially encoded cytochrome c oxidase III Homo sapiens 34-41 21639107-4 2011 In addition, dinuclear and trinuclear mu-hydroxo Co(III) complexes have been obtained in the presence of phosphate anions and absence of methanol, respectively, suggesting that an additional bridging ligand is needed to stabilize the Co(III)bis(mu-hydroxo)Co(III) fragment. Methanol 137-145 mitochondrially encoded cytochrome c oxidase III Homo sapiens 49-56 21639107-4 2011 In addition, dinuclear and trinuclear mu-hydroxo Co(III) complexes have been obtained in the presence of phosphate anions and absence of methanol, respectively, suggesting that an additional bridging ligand is needed to stabilize the Co(III)bis(mu-hydroxo)Co(III) fragment. Methanol 137-145 mitochondrially encoded cytochrome c oxidase III Homo sapiens 52-55 33877179-5 2021 The reaction conditions will determine the pathway followed and all pathways are initiated through the initial formation of a superoxo complex, CoIII(salen)(O2 )(MeOH) (EPR: g = 2.025, A = 19 G). Methanol 162-166 mitochondrially encoded cytochrome c oxidase III Homo sapiens 144-149 21578144-2 2009 The Co(III) cation has site symmetry m, and is coordinated by four oxygen atoms from four bridging pivalate groups, one central O anion and a methanol oxygen atom, forming a distorted octa-hedral geometry. Methanol 142-150 mitochondrially encoded cytochrome c oxidase III Homo sapiens 4-11 20179854-2 2010 The coordination sphere around Co(III) in 2 [or Ga(III) in 3.0.5CHCl(3).MeOH] is described as five-coordinate distorted trigonal bipyramid (DTBP) with O(1), N(1) and N(3) [or O(2), N(1), N(3)] lying in the equatorial plane for 2 [or 3.0.5CHCl(3).MeOH]. Methanol 72-76 mitochondrially encoded cytochrome c oxidase III Homo sapiens 31-38 20179854-2 2010 The coordination sphere around Co(III) in 2 [or Ga(III) in 3.0.5CHCl(3).MeOH] is described as five-coordinate distorted trigonal bipyramid (DTBP) with O(1), N(1) and N(3) [or O(2), N(1), N(3)] lying in the equatorial plane for 2 [or 3.0.5CHCl(3).MeOH]. Methanol 72-76 mitochondrially encoded cytochrome c oxidase III Homo sapiens 34-37 20179854-2 2010 The coordination sphere around Co(III) in 2 [or Ga(III) in 3.0.5CHCl(3).MeOH] is described as five-coordinate distorted trigonal bipyramid (DTBP) with O(1), N(1) and N(3) [or O(2), N(1), N(3)] lying in the equatorial plane for 2 [or 3.0.5CHCl(3).MeOH]. Methanol 246-250 mitochondrially encoded cytochrome c oxidase III Homo sapiens 31-38 20179854-2 2010 The coordination sphere around Co(III) in 2 [or Ga(III) in 3.0.5CHCl(3).MeOH] is described as five-coordinate distorted trigonal bipyramid (DTBP) with O(1), N(1) and N(3) [or O(2), N(1), N(3)] lying in the equatorial plane for 2 [or 3.0.5CHCl(3).MeOH]. Methanol 246-250 mitochondrially encoded cytochrome c oxidase III Homo sapiens 34-37 20721276-2 2010 The CoCl(2)/paoH/L-L (1 : 2 : 1) reaction system in MeOH gives complexes [Co(III)(pao)(2)(phen)]Cl.2H(2)O (1.2H(2)O) and [Co(III)(pao)(2)(bpy)]Cl.1.5MeOH (2.1.5MeOH). Methanol 52-56 mitochondrially encoded cytochrome c oxidase III Homo sapiens 74-81 20721276-2 2010 The CoCl(2)/paoH/L-L (1 : 2 : 1) reaction system in MeOH gives complexes [Co(III)(pao)(2)(phen)]Cl.2H(2)O (1.2H(2)O) and [Co(III)(pao)(2)(bpy)]Cl.1.5MeOH (2.1.5MeOH). Methanol 52-56 mitochondrially encoded cytochrome c oxidase III Homo sapiens 122-129 20023998-3 2010 The Co(III) complexes were tested in the hydrolytic kinetic resolution of (rac)-1,2-epoxyhexane and epoxide ring opening reactions using methanol as the nucleophile. Methanol 137-145 mitochondrially encoded cytochrome c oxidase III Homo sapiens 4-11 19665800-3 2009 Electrochemical data in methanol revealed that the Co(III)-->Co(II) reduction of 1 (-0.84V vs. normal hydrogen electrode - NHE) is more positive than 2 (-1.13V vs. NHE), while it was expected to be more negative due to better sigma-donor ability of imidazole ring in HL1, compared to pyridine in HL2. Methanol 24-32 mitochondrially encoded cytochrome c oxidase III Homo sapiens 54-57 18097493-11 2008 Cyclic voltammetry experiments in MeCN-CH2Cl2 reveal facile metal-centred reversible-to-quasireversible CoIV-CoIII (or a ligand-centred redox process; 2a), CoIII-CoII (1a, 1b.MeOH, 2a, 2b and 3), CoII-CoI (1a, 1b.MeOH, 2aand 2b), and CoI-Co0 (1a, 1b.MeOH and 2b) redox processes. Methanol 213-217 mitochondrially encoded cytochrome c oxidase III Homo sapiens 109-114 18097493-11 2008 Cyclic voltammetry experiments in MeCN-CH2Cl2 reveal facile metal-centred reversible-to-quasireversible CoIV-CoIII (or a ligand-centred redox process; 2a), CoIII-CoII (1a, 1b.MeOH, 2a, 2b and 3), CoII-CoI (1a, 1b.MeOH, 2aand 2b), and CoI-Co0 (1a, 1b.MeOH and 2b) redox processes. Methanol 213-217 mitochondrially encoded cytochrome c oxidase III Homo sapiens 156-161 21202483-0 2008 (Amino-acetato-kappaO,N)bis-(quinolin-8-olato-kappaO,N)cobalt(III) methanol solvate. Methanol 67-75 mitochondrially encoded cytochrome c oxidase III Homo sapiens 62-65 18097493-5 2008 Interestingly, 1b.MeOH undergoes facile metal-centred oxidation by aerial O2-H2O2-[Fe(eta5-C5H5)2][PF6], which led to the isolation of the corresponding cobalt(iii) complex [CoIII(L2)][ClO4] (2b). Methanol 18-22 mitochondrially encoded cytochrome c oxidase III Homo sapiens 174-179 18097493-11 2008 Cyclic voltammetry experiments in MeCN-CH2Cl2 reveal facile metal-centred reversible-to-quasireversible CoIV-CoIII (or a ligand-centred redox process; 2a), CoIII-CoII (1a, 1b.MeOH, 2a, 2b and 3), CoII-CoI (1a, 1b.MeOH, 2aand 2b), and CoI-Co0 (1a, 1b.MeOH and 2b) redox processes. Methanol 175-179 mitochondrially encoded cytochrome c oxidase III Homo sapiens 109-114 18097493-11 2008 Cyclic voltammetry experiments in MeCN-CH2Cl2 reveal facile metal-centred reversible-to-quasireversible CoIV-CoIII (or a ligand-centred redox process; 2a), CoIII-CoII (1a, 1b.MeOH, 2a, 2b and 3), CoII-CoI (1a, 1b.MeOH, 2aand 2b), and CoI-Co0 (1a, 1b.MeOH and 2b) redox processes. Methanol 175-179 mitochondrially encoded cytochrome c oxidase III Homo sapiens 156-161 18097493-11 2008 Cyclic voltammetry experiments in MeCN-CH2Cl2 reveal facile metal-centred reversible-to-quasireversible CoIV-CoIII (or a ligand-centred redox process; 2a), CoIII-CoII (1a, 1b.MeOH, 2a, 2b and 3), CoII-CoI (1a, 1b.MeOH, 2aand 2b), and CoI-Co0 (1a, 1b.MeOH and 2b) redox processes. Methanol 213-217 mitochondrially encoded cytochrome c oxidase III Homo sapiens 109-114 18097493-11 2008 Cyclic voltammetry experiments in MeCN-CH2Cl2 reveal facile metal-centred reversible-to-quasireversible CoIV-CoIII (or a ligand-centred redox process; 2a), CoIII-CoII (1a, 1b.MeOH, 2a, 2b and 3), CoII-CoI (1a, 1b.MeOH, 2aand 2b), and CoI-Co0 (1a, 1b.MeOH and 2b) redox processes. Methanol 213-217 mitochondrially encoded cytochrome c oxidase III Homo sapiens 156-161 17047739-2 2006 Accordingly, the interaction of cobalt(II) acetate with H(3)L in methanol gives rise to the discrete complex [Co(III)(2)L(OAc)(2)(OMe)]*1.5H(2)O.MeOH, 1. Methanol 65-73 mitochondrially encoded cytochrome c oxidase III Homo sapiens 110-117 17047739-2 2006 Accordingly, the interaction of cobalt(II) acetate with H(3)L in methanol gives rise to the discrete complex [Co(III)(2)L(OAc)(2)(OMe)]*1.5H(2)O.MeOH, 1. Methanol 145-149 mitochondrially encoded cytochrome c oxidase III Homo sapiens 110-117 17047739-5 2006 Decreasing the pH of the medium, by addition of a second mol of dicarboxylic acid, leads to [Co(II/III)(2)L(O(2)CCH(2)CO(2))(MeOH)]*2MeOH, 4, while the reaction with terephthalic acid does not proceed. Methanol 125-130 mitochondrially encoded cytochrome c oxidase III Homo sapiens 99-102 16201387-1 2005 Four new complexes of Ni(II), Cu(II), Zn(II) and Co(III) with HL (HL= N,N"-di-beta-D-glucosylethylenediamine) have been synthesized in methanol solutions. Methanol 135-143 mitochondrially encoded cytochrome c oxidase III Homo sapiens 49-56