PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12526463-0 2000 Kinetics of manganese(III) acetate in acetic acid: generation of Mn(III) with Co(III), Ce(IV), and dibromide radicals; reactions of Mn(III) with Mn(II), Co(II), hydrogen bromide, and alkali bromides. Acetic Acid 38-49 mitochondrially encoded cytochrome c oxidase II Homo sapiens 153-159 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). Acetic Acid 232-243 mitochondrially encoded cytochrome c oxidase II Homo sapiens 56-62 35172100-0 2022 Catalytic Mechanism of Competing Proton Transfer Events from Water and Acetic Acid by (CoII(bpbH2)Cl2) for Water Splitting Processes. Acetic Acid 71-82 mitochondrially encoded cytochrome c oxidase II Homo sapiens 87-91 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. Acetic Acid 70-81 mitochondrially encoded cytochrome c oxidase II Homo sapiens 140-146 35172100-8 2022 The second proton transfer from water to the CoII-H moiety requires less free energy than acetic acid and is the rate-limiting step. Acetic Acid 90-101 mitochondrially encoded cytochrome c oxidase II Homo sapiens 45-49 33260955-5 2020 Finally, the [P44414]Cl + CH3COOH system was applied to the treatment of real waste, NiMH battery black mass, being shown that it allows an efficient separation of Co(II) from Ni(II), Fe(III) and the lanthanides in a single leaching and separation step. Acetic Acid 26-33 mitochondrially encoded cytochrome c oxidase II Homo sapiens 164-170 22830538-1 2012 The interactions of a weak organic acid (acetic acid, HOAc) with a toluene solution of the Co(II)-Schiff base type complex, (R,R")-N,N"-bis(3,5-di-tert-butylsalicylidene)-1,2-cyclohexane-diamino Co(II) (labeled [Co(1)]), was investigated using EPR, HYSCORE, and DFT computations. Acetic Acid 41-52 mitochondrially encoded cytochrome c oxidase II Homo sapiens 91-97 22830538-1 2012 The interactions of a weak organic acid (acetic acid, HOAc) with a toluene solution of the Co(II)-Schiff base type complex, (R,R")-N,N"-bis(3,5-di-tert-butylsalicylidene)-1,2-cyclohexane-diamino Co(II) (labeled [Co(1)]), was investigated using EPR, HYSCORE, and DFT computations. Acetic Acid 54-58 mitochondrially encoded cytochrome c oxidase II Homo sapiens 91-97 22830538-1 2012 The interactions of a weak organic acid (acetic acid, HOAc) with a toluene solution of the Co(II)-Schiff base type complex, (R,R")-N,N"-bis(3,5-di-tert-butylsalicylidene)-1,2-cyclohexane-diamino Co(II) (labeled [Co(1)]), was investigated using EPR, HYSCORE, and DFT computations. Acetic Acid 54-58 mitochondrially encoded cytochrome c oxidase II Homo sapiens 195-201 22830538-4 2012 The newly formed LS state is assigned to the coordinated [Co(II)(1)]-(HOAc) complex, possessing a z(2), (2)A(1)) ground state (species A; g(x) = 2.42, g(y) = 2.28, g(z) = 2.02, A(x) = 100, A(y) = 120, A(z) = 310 MHz). Acetic Acid 70-75 mitochondrially encoded cytochrome c oxidase II Homo sapiens 58-64 22830538-8 2012 This complex is tentatively assigned to a paramagnetic superoxo bridged dimer (AcO(-))[Co(II)(1) O(2)(-)Co(III)(1)](HOAc), as distinct from the more common diamagnetic peroxo bridged dimers. Acetic Acid 118-122 mitochondrially encoded cytochrome c oxidase II Homo sapiens 87-93 22830538-9 2012 Species C is characterized by a very broad HS EPR signal (g(x) = 5.1, g(y) = 3.9, g(z) = 2.1) and is reversibly formed by oxygenation of the LS [Co(II)(1)]-(HOAc) complex to the superoxo complex [Co(III)(1)O(2)(-)](HOAc), which subsequently forms the association complex C by interaction with the HS [Co(II)(1)](OAc(-)) species. Acetic Acid 157-161 mitochondrially encoded cytochrome c oxidase II Homo sapiens 145-151 22830538-9 2012 Species C is characterized by a very broad HS EPR signal (g(x) = 5.1, g(y) = 3.9, g(z) = 2.1) and is reversibly formed by oxygenation of the LS [Co(II)(1)]-(HOAc) complex to the superoxo complex [Co(III)(1)O(2)(-)](HOAc), which subsequently forms the association complex C by interaction with the HS [Co(II)(1)](OAc(-)) species. Acetic Acid 215-219 mitochondrially encoded cytochrome c oxidase II Homo sapiens 145-151 22830538-12 2012 Overall, it appears that a facile interconversion of the [Co(1)] complex, possessing a LS ground state, occurs in the presence of acetic acid, producing both HS and LS Co(II) states, prior to formation of the oxidized active form of the catalyst, [Co(III)(1)](OAc(-)). Acetic Acid 130-141 mitochondrially encoded cytochrome c oxidase II Homo sapiens 168-174 20121216-1 2010 The activation of N,N"-bis(3,5-di-tert-butylsalicylidene)-1,2-cyclohexane-diamino Co(II), [Co(II)(1)], by the addition of acetic acid under aerobic conditions has been investigated by a range of spectroscopic techniques including continuous-wave EPR, HYSCORE, pulsed ENDOR, and resonance Raman. Acetic Acid 122-133 mitochondrially encoded cytochrome c oxidase II Homo sapiens 82-89 12772922-1 2003 In the chiral Co(III)(salen)-catalysed HKR of racemic epoxides, in the presence of ionic liquids, Co(II)(salen) complex is oxidised without acetic acid to catalytically active Co(III)(salen) complex during reaction and, moreover, this oxidation state is stabilised against reduction to Co(II) complex which enables the reuse of the recovered catalyst for consecutive reactions without extra reoxidation. Acetic Acid 140-151 mitochondrially encoded cytochrome c oxidase II Homo sapiens 98-104