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