PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32108445-3 2020 Electrochemically induced hydrogen evolution catalysis studies at pH 4 invoke a mechanism, in which the rate determining step is the protonation of the reduced CoI species that gives a cobalt hydride (CoIII-H), a key intermediate towards the H-H bond formation. Cobalt 185-199 mitochondrially encoded cytochrome c oxidase I Homo sapiens 160-163 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 I Homo sapiens 109-112 30600680-3 2019 Also, the more electron-rich cobalt center of the Co(-I) catalyst was found to contribute higher reactivity for alkene hydrogenation. Cobalt 29-35 mitochondrially encoded cytochrome c oxidase I Homo sapiens 50-55 31698896-1 2019 The oxidative addition of organic electrophiles into electrochemically generated Co(I) complexes has been widely utilized as a strategy to produce carbon-centered radicals when cobalt is ligated by a polydentate ligand. Cobalt 177-183 mitochondrially encoded cytochrome c oxidase I Homo sapiens 81-86 31020835-0 2019 Cationic Co(I)-Intermediates for Hydrofunctionalization Reactions: Regio- and Enantioselective Cobalt-Catalyzed 1,2-Hydroboration of 1,3-Dienes. Cobalt 95-101 mitochondrially encoded cytochrome c oxidase I Homo sapiens 9-28 30095842-4 2018 The selectivity correlates well with the CoI/II redox potential within the same cobalt catalyst series (span 240 mV (1R) and 290 mV (2R)), with electron donating ligands favoring ketone reduction over H2 evolution. Cobalt 80-86 mitochondrially encoded cytochrome c oxidase I Homo sapiens 41-44 30040391-6 2018 Further reduction of the Co(I) complex was found to generate a pincer-based pi-radical anion that demonstrated well-resolved EPR features to the four hydrogen atoms and lone nitrogen atom of the ligand with minor contributions from cobalt and coordinated N2. Cobalt 232-238 mitochondrially encoded cytochrome c oxidase I Homo sapiens 25-30 28453294-1 2017 Vitamin B12 is a natural cobalt complex that, while reduced to the "supernucleophilic" Co(I) form, can easily react with electrophiles via an SN2 mechanism. Cobalt 25-31 mitochondrially encoded cytochrome c oxidase I Homo sapiens 87-92 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 I Homo sapiens 65-70 27936666-3 2016 The spin transition realized above 150 K is accompanied by a cobalt-to-fullerene charge transfer that forms a quintet excited state with a high spin CoI (S = 1) and C60 - (S = 1/2). Cobalt 61-67 mitochondrially encoded cytochrome c oxidase I Homo sapiens 149-152 27978654-0 2016 Co(I)-Mediated Removal of Addends on the C60 Cage and Formation of the Monovalent Cobalt Complex CpCo(CO)(eta2-C60). Cobalt 82-88 mitochondrially encoded cytochrome c oxidase I Homo sapiens 0-5 24044877-6 2013 Furthermore, the central intermediate of the solution-phase cobalt-catalyzed Diels-Alder reaction, [Co(I)(dppe)(isoprene)(phenylacetylene)](+), could be generated via IMR and examined in the gas phase. Cobalt 60-66 mitochondrially encoded cytochrome c oxidase I Homo sapiens 100-104 27973864-3 2016 To the best of our knowledge, this is the first example of capturing the penta-coordinated Co(I) intermediate in operando with bond contraction by XTA, thereby providing new insights for fundamental understanding of structure-function relationship of cobalt-based molecular catalysts. Cobalt 251-257 mitochondrially encoded cytochrome c oxidase I Homo sapiens 91-96 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 I Homo sapiens 234-239 24044877-9 2013 The results constitute strong analytical evidence for the formation and importance of different cobalt(I) species in regioselective Diels-Alder reactions of unactivated substrates and identify [Co(I)(dppe)](+) as the active Diels-Alder catalyst. Cobalt 96-105 mitochondrially encoded cytochrome c oxidase I Homo sapiens 194-198 23945020-2 2013 Coordination of these ligands to cobalt affords the complexes [Co(II)(L2)(CH3CN)](2+) and [Co(II)(L3)(CH3CN)](2+), which are reduced by KC8 to afford [Co(I)(L2)(CH3CN)](+) and [Co(I)(L3)(CH3CN)](+). Cobalt 33-39 mitochondrially encoded cytochrome c oxidase I Homo sapiens 151-156 23945020-2 2013 Coordination of these ligands to cobalt affords the complexes [Co(II)(L2)(CH3CN)](2+) and [Co(II)(L3)(CH3CN)](2+), which are reduced by KC8 to afford [Co(I)(L2)(CH3CN)](+) and [Co(I)(L3)(CH3CN)](+). Cobalt 33-39 mitochondrially encoded cytochrome c oxidase I Homo sapiens 177-182 16619328-0 2006 A Co2N2 diamond-core resting state of cobalt(I): a three-coordinate CoI synthon invoking an unusual pincer-type rearrangement. Cobalt 38-47 mitochondrially encoded cytochrome c oxidase I Homo sapiens 68-71 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 I Homo sapiens 211-216 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 I Homo sapiens 81-86 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 I Homo sapiens 111-116 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 I Homo sapiens 111-116 32523222-0 1970 A Theoretical Investigation of the Configurations (3d + 4s)8 4p in Neutral Cobalt (Co I). Cobalt 75-81 mitochondrially encoded cytochrome c oxidase I Homo sapiens 83-87 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 I Homo sapiens 47-51