PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1847624-1	1991	The direct electrochemistry of cytochrome c at a gold electrode was investigated by cyclic voltammetry using, as promoters, microperoxidase (the haem-undecapeptide obtained by hydrolysis of cytochrome c), Fe(III)-protoporphyrin IX or protoporphyrin-IX, all entrapped in a cellulose triacetate membrane.	protoporphyrin IX	234-251	cytochrome c, somatic	Homo sapiens	31-43	
32612451-1	2020	Protoporphyrin IX (PPIX) is the porphyrin scaffold of heme b, a ubiquitous prosthetic group of proteins responsible for oxygen binding (hemoglobin, myoglobin), electron transfer (cytochrome c) and catalysis (cytochrome P450, catalases, peroxidases).	protoporphyrin IX	0-17	cytochrome c, somatic	Homo sapiens	179-191	
32612451-1	2020	Protoporphyrin IX (PPIX) is the porphyrin scaffold of heme b, a ubiquitous prosthetic group of proteins responsible for oxygen binding (hemoglobin, myoglobin), electron transfer (cytochrome c) and catalysis (cytochrome P450, catalases, peroxidases).	protoporphyrin IX	19-23	cytochrome c, somatic	Homo sapiens	179-191	
31748766-1	2019	Protoporphyrin IX iron complex (heme) is an important cofactor for oxygen transfer, oxygen storage, oxygen activation, and electron transfer when bound to the heme proteins hemoglobin, myoglobin, cytochrome P450 and cytochrome c, respectively.	protoporphyrin IX	0-17	cytochrome c, somatic	Homo sapiens	216-228	
24631867-2	2014	Their biosynthesis relies on a complex post-translational process, called cytochrome c biogenesis, responsible for the formation of stereo-specific thioether bonds between the vinyl groups of heme b (protoporphyrin IX-Fe) and the thiol groups of apocytochromes c heme-binding site (C1XXC2H) cysteine residues.	protoporphyrin IX	200-217	cytochrome c, somatic	Homo sapiens	74-86	
31332208-1	2019	Mitochondrial respiratory chain complexes II, III, and IV and cytochrome c contain haem, which is generated by the insertion of Fe2+ into protoporphyrin IX.	protoporphyrin IX	138-155	cytochrome c, somatic	Homo sapiens	62-74	
18555026-9	2008	In addition, the enzymatic site of cytochrome c was sensitive to the attack of both superoxide and hydroxyl radicals as observed through the reduction of Fe(3+), the degradation of the protoporphyrin IX and the oxidative disruption of the Met80-Fe(3+) bond.	protoporphyrin IX	185-202	cytochrome c, somatic	Homo sapiens	35-47	
12417624-4	2002	Stable expression of M11L prevents the release of mitochondrial cytochrome c induced by staurosporine or protoporphyrin IX (PPIX), a ligand of the PBR.	protoporphyrin IX	105-122	cytochrome c, somatic	Homo sapiens	64-76	
12417624-4	2002	Stable expression of M11L prevents the release of mitochondrial cytochrome c induced by staurosporine or protoporphyrin IX (PPIX), a ligand of the PBR.	protoporphyrin IX	124-128	cytochrome c, somatic	Homo sapiens	64-76