PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9737862-4	1998	Mutation of the corresponding proline in rabbit CYP4B1 (Pro422 --> Ser) abolished heme incorporation.	Heme	85-89	cytochrome P450 4B1	Oryctolagus cuniculus	48-54	
28363936-2	2017	A co-crystal structure of the rabbit family 4 enzyme CYP4B1 with its substrate octane reveals that the propensity for omega-hydroxylation is orchestrated by active-site sterics, partially mediated by an unusual heme-polypeptide ester bond.	Heme	211-215	cytochrome P450 4B1	Oryctolagus cuniculus	53-59	
12859977-0	2003	Rabbit CYP4B1 engineered for high-level expression in Escherichia coli: ligand stabilization and processing of the N-terminus and heme prosthetic group.	Heme	130-134	cytochrome P450 4B1	Oryctolagus cuniculus	7-13	
12859977-4	2003	Notably, bacterial expression of CYP4B1 produced a holoenzyme with >98.5% of its heme prosthetic group covalently linked to the protein backbone.	Heme	84-88	cytochrome P450 4B1	Oryctolagus cuniculus	33-39	
12859977-6	2003	These studies shed new light on the consequences of covalent heme processing in CYP4B1 and provide a facile system for future mechanistic and structural studies with the enzyme.	Heme	61-65	cytochrome P450 4B1	Oryctolagus cuniculus	80-86	
12693958-0	2003	Covalent heme binding to CYP4B1 via Glu310 and a carbocation porphyrin intermediate.	Heme	9-13	cytochrome P450 4B1	Oryctolagus cuniculus	25-31	
12693958-1	2003	Recently we found that CYP4B1, and several other members of the CYP4 family of enzymes, are covalently linked to their prosthetic heme group through an ester linkage.	Heme	130-134	cytochrome P450 4B1	Oryctolagus cuniculus	23-29	
12693958-8	2003	These data show (i) that E310 serves as the site of covalent attachment of heme to the protein backbone of rabbit CYP4B1; (ii) this I-helix glutamate residue influences substrate orientation in the active site of CYP4B1; and (iii) the mechanism of covalent heme attachment most likely involves a carbocation species located on the porphyrin.	Heme	75-79	cytochrome P450 4B1	Oryctolagus cuniculus	114-120	
12693958-8	2003	These data show (i) that E310 serves as the site of covalent attachment of heme to the protein backbone of rabbit CYP4B1; (ii) this I-helix glutamate residue influences substrate orientation in the active site of CYP4B1; and (iii) the mechanism of covalent heme attachment most likely involves a carbocation species located on the porphyrin.	Heme	75-79	cytochrome P450 4B1	Oryctolagus cuniculus	213-219	
12693958-8	2003	These data show (i) that E310 serves as the site of covalent attachment of heme to the protein backbone of rabbit CYP4B1; (ii) this I-helix glutamate residue influences substrate orientation in the active site of CYP4B1; and (iii) the mechanism of covalent heme attachment most likely involves a carbocation species located on the porphyrin.	Heme	257-261	cytochrome P450 4B1	Oryctolagus cuniculus	114-120	
12693958-8	2003	These data show (i) that E310 serves as the site of covalent attachment of heme to the protein backbone of rabbit CYP4B1; (ii) this I-helix glutamate residue influences substrate orientation in the active site of CYP4B1; and (iii) the mechanism of covalent heme attachment most likely involves a carbocation species located on the porphyrin.	Heme	257-261	cytochrome P450 4B1	Oryctolagus cuniculus	213-219	
9737862-8	1998	Therefore, the presence of a consensus Pro-X-Arg motif is critical for incorporation of the heme prosthetic group in human and rabbit CYP4B1 proteins expressed in insect cells.	Heme	92-96	cytochrome P450 4B1	Oryctolagus cuniculus	134-140