PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9784594-1	1998	Protoporphyria (PP) is caused by a deficiency of ferrochelatase (FC) activity, which catalyzes the final step in the heme biosynthesis pathway.	Heme	117-121	FECH	Bos taurus	65-67	
3986176-1	1985	Spectrofluorometric techniques have been employed to examine the active site of the terminal enzyme of the heme biosynthetic pathway, ferrochelatase (protoheme ferrolyase, EC 4.99.1.1).	Heme	107-111	FECH	Bos taurus	134-148	
1761561-1	1991	Ferrochelatase (EC 4.99.1.1) catalyzes the final step of heme biosynthesis, the insertion of iron(II) into protoporphyrin.	Heme	57-61	FECH	Bos taurus	0-14	
3091080-6	1986	When purified ferrochelatase was incubated with the low molecular weight form of NADH dehydrogenase prepared from Complex I, heme synthesis from ferric ion occurred by the addition of NADH.	Heme	125-129	FECH	Bos taurus	14-28	
3091080-8	1986	These results indicate that ferrous ion is produced by NADH oxidation in Complex I and is then utilized for heme synthesis by ferrochelatase.	Heme	108-112	FECH	Bos taurus	126-140	
3884041-1	1985	The orientation of ferrochelatase (protoheme ferro-lyase, EC 4.99.1.1), the terminal enzyme of the heme biosynthetic pathway, was examined in bovine liver mitochondria.	Heme	40-44	FECH	Bos taurus	19-33	
6688622-12	1983	These findings lead to a sequential Bi Bi kinetic model for ferrochelatase with iron binding occurring prior to porphyrin binding and heme being released prior to the release of two protons.	Heme	134-138	FECH	Bos taurus	60-74	
6698990-1	1984	The role of sulfhydryl groups in the activity of the terminal enzyme of the heme biosynthetic pathway, ferrochelatase (protoheme ferrolyase, EC 4.99.1.1), has been examined by using a variety of sulfhydryl group-specific reagents.	Heme	76-80	FECH	Bos taurus	103-117	
6688622-2	1983	The terminal enzyme of the heme biosynthetic pathway, ferrochelatase (protoheme ferrolyase EC 4.99.1.1), has been purified to apparent homogeneity from bovine liver mitochondria using a scheme similar to that reported by Taketani and Tokunaga (Taketani, S. and Tokunaga, R. (1981) J. Biol.	Heme	27-31	FECH	Bos taurus	54-68