PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21615132-1	2011	Phenylalanine hydroxylase (PheH) is an iron(II)-dependent enzyme that catalyzes the hydroxylation of aromatic amino acid l-phenylalanine (L-Phe) to l-tyrosine (L-Tyr).	ammonium ferrous sulfate	39-47	phenylalanine hydroxylase	Homo sapiens	0-25	
21615132-1	2011	Phenylalanine hydroxylase (PheH) is an iron(II)-dependent enzyme that catalyzes the hydroxylation of aromatic amino acid l-phenylalanine (L-Phe) to l-tyrosine (L-Tyr).	ammonium ferrous sulfate	39-47	phenylalanine hydroxylase	Homo sapiens	27-31	
12009881-1	2002	Previous studies of ferrous wild-type phenylalanine hydroxylase, [Fe(2+)]PAH(T)[], have shown the active site to be a six-coordinate distorted octahedral site.	ammonium ferrous sulfate	66-72	phenylalanine hydroxylase	Homo sapiens	38-63	
19489646-2	2009	We have previously shown that the Fe(II) site in phenylalanine hydroxylase (PAH) converts from six-coordinate (6C) to five-coordinate (5C) only when both substrate + cofactor are bound.	ammonium ferrous sulfate	34-40	phenylalanine hydroxylase	Homo sapiens	49-74	
19489646-2	2009	We have previously shown that the Fe(II) site in phenylalanine hydroxylase (PAH) converts from six-coordinate (6C) to five-coordinate (5C) only when both substrate + cofactor are bound.	ammonium ferrous sulfate	34-40	phenylalanine hydroxylase	Homo sapiens	76-79	
12733906-8	2003	These results provide insight into the PAH reaction and disease mechanism at a molecular level, indicating that the first step of the mechanism is formation of a peroxy-pterin species, which subsequently reacts with the Fe(II) site if the pterin is properly oriented for formation of an Fe-OO-pterin bridge and an open coordination position is available on the Fe(II).	ammonium ferrous sulfate	220-226	phenylalanine hydroxylase	Homo sapiens	39-42	
12733906-8	2003	These results provide insight into the PAH reaction and disease mechanism at a molecular level, indicating that the first step of the mechanism is formation of a peroxy-pterin species, which subsequently reacts with the Fe(II) site if the pterin is properly oriented for formation of an Fe-OO-pterin bridge and an open coordination position is available on the Fe(II).	ammonium ferrous sulfate	361-367	phenylalanine hydroxylase	Homo sapiens	39-42	
11718561-0	2001	High resolution crystal structures of the catalytic domain of human phenylalanine hydroxylase in its catalytically active Fe(II) form and binary complex with tetrahydrobiopterin.	ammonium ferrous sulfate	122-128	phenylalanine hydroxylase	Homo sapiens	68-93	
11718561-1	2001	The crystal structures of the catalytic domain (DeltaN1-102/DeltaC428-452) of human phenylalanine hydroxylase (hPheOH) in its catalytically competent Fe(II) form and binary complex with the reduced pterin cofactor 6(R)-L-erythro-5,6,7,8-tetrahydrobiopterin (BH4) have been determined to 1.7 and 1.5 A, respectively.	ammonium ferrous sulfate	150-156	phenylalanine hydroxylase	Homo sapiens	84-109	
6324864-7	1984	Dithionite can substitute for 6-methyltetrahydropterin in an anaerobic prereduction step, generating a catalytically active phenylalanine hydroxylase containing Fe2+ that functions aerobically to produce tyrosine from added 6-methyltetrahydropterin in a 1/1 stoichiometry.	ammonium ferrous sulfate	161-165	phenylalanine hydroxylase	Homo sapiens	124-149	
32996242-1	2021	In previous work, lab-scale reactors designed to study microbial Fe(II) oxidation rates at low pH were found to have stable rates under a wide range of pH and Fe(II) concentrations.	ammonium ferrous sulfate	65-71	phenylalanine hydroxylase	Homo sapiens	95-97	
32996242-1	2021	In previous work, lab-scale reactors designed to study microbial Fe(II) oxidation rates at low pH were found to have stable rates under a wide range of pH and Fe(II) concentrations.	ammonium ferrous sulfate	65-71	phenylalanine hydroxylase	Homo sapiens	152-154	
32996242-1	2021	In previous work, lab-scale reactors designed to study microbial Fe(II) oxidation rates at low pH were found to have stable rates under a wide range of pH and Fe(II) concentrations.	ammonium ferrous sulfate	159-165	phenylalanine hydroxylase	Homo sapiens	95-97