PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17705494-5	2007	The coordination structures and ligand (O2 and CO) binding properties of nine rHSA(triple mutant)-heme complexes have been physicochemically and kinetically characterized.	Heme	98-102	immunoglobulin kappa variable 1D-39	Homo sapiens	40-49	
10092643-9	1999	Whereas diphenyliodonium chloride inhibited O-2, blockers of heme such as NaCN, 1-phenylimidazole, and imidazole likewise prevented the formation of O-2 at concentrations that inhibited NO.	Heme	61-65	immunoglobulin kappa variable 1D-39	Homo sapiens	149-152	
10092643-11	1999	Taken together these data demonstrate that NOS I generates O-2 and the formation of this free radical occurs at the heme domain.	Heme	116-120	immunoglobulin kappa variable 1D-39	Homo sapiens	59-62	
9712892-1	1998	In the absence of L-arginine, the heme center of the oxygenase domain of neuronal nitric-oxide synthase reduces molecular oxygen to superoxide (O-2).	Heme	34-38	immunoglobulin kappa variable 1D-39	Homo sapiens	144-147	
1654851-1	1991	Heme compound, hematin or cytochrome c, catalyzes the decomposition of 13-hydroperoxy linoleic acid yielding both O2- and 1O2 under aerobic conditions.	Heme	0-4	immunoglobulin kappa variable 1D-39	Homo sapiens	114-125