PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8095402-8	1993	The results indicate that the active site of CYP1A2 is open above all four quadrants of the heme group including, to some extent, the region above pyrrole ring B.	Heme	92-96	cytochrome P450, family 1, subfamily a, polypeptide 2	Rattus norvegicus	45-51	
2177399-1	1990	Asbestos fibers adsorb cytochrome P-450 and P-448 proteins from rat lung micosomal fractions and liberate heme from cytochrome P-448 on prolonged incubation in vitro.	Heme	106-110	cytochrome P450, family 1, subfamily a, polypeptide 2	Rattus norvegicus	116-132	
6415870-7	1983	Moreover, we found that during the metabolism of 3,4,3",4"-TCB, the heme content of the reconstituted system was lowered, probably reflecting the alkylation of the sulfhydryl groups in the active sites of cytochrome P-448.	Heme	68-72	cytochrome P450, family 1, subfamily a, polypeptide 2	Rattus norvegicus	205-221	
2153026-5	1990	Thus the spin state of P-450ds (the wild-type and all mutants) may not be solely due to specific characteristics of the distal site, but to the unique nature of the whole heme environment of P-450d.	Heme	171-175	cytochrome P450, family 1, subfamily a, polypeptide 2	Rattus norvegicus	23-29	
2153026-6	1990	It is also suggested that the amino acids at the distal region of P-450d may be located close to the heme, so that the water molecule cannot bind to the heme, thus taking the high-spin state.	Heme	101-105	cytochrome P450, family 1, subfamily a, polypeptide 2	Rattus norvegicus	66-72	
2153026-6	1990	It is also suggested that the amino acids at the distal region of P-450d may be located close to the heme, so that the water molecule cannot bind to the heme, thus taking the high-spin state.	Heme	153-157	cytochrome P450, family 1, subfamily a, polypeptide 2	Rattus norvegicus	66-72	
2153026-7	1990	Both the aromatic mutants showed rather large deviations of the g values from those of wild-type P-450d, suggesting that the aromatic region somehow interacts with the heme.	Heme	168-172	cytochrome P450, family 1, subfamily a, polypeptide 2	Rattus norvegicus	97-103	
3046664-0	1988	Site-directed mutageneses of rat liver cytochrome P-450d: axial ligand and heme incorporation.	Heme	75-79	cytochrome P450, family 1, subfamily a, polypeptide 2	Rattus norvegicus	39-56