PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
34110158-2	2021	Here, we report biochemical, biophysical, and computational analyses revealing that 1H-indazole-4-amines inhibit both hIDO1 and hTDO by a mechanism involving direct coordination with the heme ferrous and ferric states.	Ferric enterobactin ion	204-210	indoleamine 2,3-dioxygenase 1	Homo sapiens	118-123	
31436417-3	2019	These consequential effects are regulated through redox changes in the heme cofactor of IDO1, which autoxidizes to the inactive ferric state during turnover.	Ferric enterobactin ion	128-134	indoleamine 2,3-dioxygenase 1	Homo sapiens	88-92	
21517759-4	2011	The active IDO conformer exists only in the presence of reducing cofactors (such as cytochrome b(5)), requiring the single electron reduction of ferric-to-ferrous iron (Fe(3+) Fe(2+)), which facilitates binding of L-Trp and O(2) to the enzyme active site.	Ferric enterobactin ion	145-151	indoleamine 2,3-dioxygenase 1	Homo sapiens	11-14