PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 27064169-4 2016 Detailed mechanistic studies show that while the complexes retain the monodentate X ligand upon electrochemical reduction to Co(II) species in MeCN solution, in aqueous solution, upon reduction by ascorbate (photocatalytic conditions), [Co(II)(N4Py)(HA)](+) is formed in all cases and is the precursor to the Co(I) species which presumably reacts with a proton. histidinoalanine 250-253 mitochondrially encoded cytochrome c oxidase II Homo sapiens 125-131 27064169-4 2016 Detailed mechanistic studies show that while the complexes retain the monodentate X ligand upon electrochemical reduction to Co(II) species in MeCN solution, in aqueous solution, upon reduction by ascorbate (photocatalytic conditions), [Co(II)(N4Py)(HA)](+) is formed in all cases and is the precursor to the Co(I) species which presumably reacts with a proton. histidinoalanine 250-253 mitochondrially encoded cytochrome c oxidase II Homo sapiens 237-243