PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
6326802-1	1984	The one-electron oxidation-reduction properties of flavin in hepatic NADH-cytochrome b5 reductase were investigated by optical absorption spectroscopy, electron paramagnetic resonance (EPR), and potentiometric titration.	4,6-dinitro-o-cresol	51-57	cytochrome b5 type A	Homo sapiens	74-87	
2847775-7	1988	These results showed that in the greater part of the complexes, the flavin-mediated pathway for reduction of cytochrome c or cytochrome b5 by pyridine nucleotide was intact.	4,6-dinitro-o-cresol	68-74	cytochrome b5 type A	Homo sapiens	125-138	
6326802-4	1984	This indicates that electron transfer from flavin to cytochrome b5 proceeds in two successive one-electron steps.	4,6-dinitro-o-cresol	43-49	cytochrome b5 type A	Homo sapiens	53-66	
11574067-0	2001	Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on protein stability and catalysis.	4,6-dinitro-o-cresol	11-17	cytochrome b5 type A	Homo sapiens	65-78	
29111436-4	2018	In addition, upon complex formation, we measured an increase of cytochrome b5 reductase flavin autofluorescence that was dependent upon the presence of cytochrome b5.	4,6-dinitro-o-cresol	88-94	cytochrome b5 type A	Homo sapiens	64-77	
29111436-4	2018	In addition, upon complex formation, we measured an increase of cytochrome b5 reductase flavin autofluorescence that was dependent upon the presence of cytochrome b5.	4,6-dinitro-o-cresol	88-94	cytochrome b5 type A	Homo sapiens	152-165	
17489100-8	2007	In contrast, the cytochrome b5-NADH pathway becomes dominant under conditions of excess metHb accumulation, only after the capacity of the flavin-NADPH pathway has reached its limit.	4,6-dinitro-o-cresol	139-145	cytochrome b5 type A	Homo sapiens	17-30	
11574067-1	2001	Porcine NADH-cytochrome b5 reductase catalytic domain (Pb5R) has the RXY(T/S)+(T/S) flavin-binding motif that is highly conserved among the structurally related family of flavoprotein reductases.	4,6-dinitro-o-cresol	84-90	cytochrome b5 type A	Homo sapiens	13-26	
8880927-4	1996	The electrostatic potential of the surface near the flavin-protruding side (dimethylbenzene end of the flavin ring) of NADH-cytochrome b5 reductase was positive over a wide area while that of the surface near the heme-binding site of cytochrome b5 was negative.	4,6-dinitro-o-cresol	52-58	cytochrome b5 type A	Homo sapiens	124-137	
8880927-4	1996	The electrostatic potential of the surface near the flavin-protruding side (dimethylbenzene end of the flavin ring) of NADH-cytochrome b5 reductase was positive over a wide area while that of the surface near the heme-binding site of cytochrome b5 was negative.	4,6-dinitro-o-cresol	52-58	cytochrome b5 type A	Homo sapiens	234-247	
8880927-4	1996	The electrostatic potential of the surface near the flavin-protruding side (dimethylbenzene end of the flavin ring) of NADH-cytochrome b5 reductase was positive over a wide area while that of the surface near the heme-binding site of cytochrome b5 was negative.	4,6-dinitro-o-cresol	103-109	cytochrome b5 type A	Homo sapiens	124-137	
8880927-4	1996	The electrostatic potential of the surface near the flavin-protruding side (dimethylbenzene end of the flavin ring) of NADH-cytochrome b5 reductase was positive over a wide area while that of the surface near the heme-binding site of cytochrome b5 was negative.	4,6-dinitro-o-cresol	103-109	cytochrome b5 type A	Homo sapiens	234-247	
8880927-5	1996	This implied that the flavin-protruding side of NADH-cytochrome b5 reductase is suitable for interacting with its electron-transfer partner, cytochrome b5.	4,6-dinitro-o-cresol	22-28	cytochrome b5 type A	Homo sapiens	53-66	
8880927-5	1996	This implied that the flavin-protruding side of NADH-cytochrome b5 reductase is suitable for interacting with its electron-transfer partner, cytochrome b5.	4,6-dinitro-o-cresol	22-28	cytochrome b5 type A	Homo sapiens	141-154	
2113027-0	1990	On the mechanism of one-electron reduction of quinones by microsomal flavin enzymes: the kinetic analysis between cytochrome B5 and menadione.	4,6-dinitro-o-cresol	69-75	cytochrome b5 type A	Homo sapiens	114-127