PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3223948-9	1988	The rate constant for cytochrome b reduction, unlike that for flavin reduction, increased with enzyme concentration, prompting the conclusion that any given cytochrome b centre is reduced preferentially by flavin groups in different molecules rather than by its partner flavin within the same monomer.	4,6-dinitro-o-cresol	62-68	mitochondrially encoded cytochrome b	Homo sapiens	157-169	
3223948-9	1988	The rate constant for cytochrome b reduction, unlike that for flavin reduction, increased with enzyme concentration, prompting the conclusion that any given cytochrome b centre is reduced preferentially by flavin groups in different molecules rather than by its partner flavin within the same monomer.	4,6-dinitro-o-cresol	206-212	mitochondrially encoded cytochrome b	Homo sapiens	22-34	
3223948-9	1988	The rate constant for cytochrome b reduction, unlike that for flavin reduction, increased with enzyme concentration, prompting the conclusion that any given cytochrome b centre is reduced preferentially by flavin groups in different molecules rather than by its partner flavin within the same monomer.	4,6-dinitro-o-cresol	206-212	mitochondrially encoded cytochrome b	Homo sapiens	157-169	
3223948-9	1988	The rate constant for cytochrome b reduction, unlike that for flavin reduction, increased with enzyme concentration, prompting the conclusion that any given cytochrome b centre is reduced preferentially by flavin groups in different molecules rather than by its partner flavin within the same monomer.	4,6-dinitro-o-cresol	206-212	mitochondrially encoded cytochrome b	Homo sapiens	22-34	
3223948-9	1988	The rate constant for cytochrome b reduction, unlike that for flavin reduction, increased with enzyme concentration, prompting the conclusion that any given cytochrome b centre is reduced preferentially by flavin groups in different molecules rather than by its partner flavin within the same monomer.	4,6-dinitro-o-cresol	206-212	mitochondrially encoded cytochrome b	Homo sapiens	157-169	
7165731-7	1982	Phagocytic vesicles were prepared from normal neutrophils and found to contain FAD and cytochrome b in a ratio 2.22:1, suggesting that activation of neutrophils many involve the incorporation of an additional flavin into the membrane.	4,6-dinitro-o-cresol	209-215	mitochondrially encoded cytochrome b	Homo sapiens	87-99	
7165731-8	1982	Under anaerobic conditions in the presence of EDTA to act as an electron donor to a flavin, the cytochrome b(-245) of neutrophil membranes was partly (12%) photoreducible, an effect increased to 100% by the addition of FMN.	4,6-dinitro-o-cresol	84-90	mitochondrially encoded cytochrome b	Homo sapiens	96-108	
6461017-0	1982	Photoreduction of cytochrome b557 of partially purified Neurospora nitrate reductase via its internal flavin.	4,6-dinitro-o-cresol	102-108	mitochondrially encoded cytochrome b	Homo sapiens	18-30	
7608214-6	1995	Mixing of 8-mercapto-FAD with flavin-depleted cytochrome b558 caused a red-shift of the flavin absorption maximum from 520 nm to around 560 nm, as has been seen when a variety of other apoflavoprotein dehydrogenases bind this analog.	4,6-dinitro-o-cresol	30-36	mitochondrially encoded cytochrome b	Homo sapiens	46-58	
31172469-3	2019	In a flavin-dependent fashion, cytochrome b558 shuttles electrons from cytoplasmic NADPH across membranes to molecular oxygen and thereby generates superoxide anion.	4,6-dinitro-o-cresol	5-11	mitochondrially encoded cytochrome b	Homo sapiens	31-43	
28755362-4	2017	The Cytb 558 is the membrane catalytic core of the NADPH oxidase complex, through which the reducing equivalent provided by NADPH is transferred via the associated prosthetic groups (one flavin and two hemes) to reduce dioxygen into superoxide anion.	4,6-dinitro-o-cresol	187-193	mitochondrially encoded cytochrome b	Homo sapiens	4-8	
8307196-5	1994	It is shown that, depending on the composition of the phospholipid environment, cytochrome b599 binds FAD with high or low affinity, this being accompanied by changes in flavin absorbance and fluorescence.	4,6-dinitro-o-cresol	170-176	mitochondrially encoded cytochrome b	Homo sapiens	80-92	
7896790-6	1995	Here, we provide direct evidence that p67phox alone can facilitate electron flow from NADPH to the flavin center of NADPH oxidase in the absence of p47phox, resulting in the reduction of enzyme FAD, whereas the presence of p47phox is required in order for electron transfer to proceed beyond the flavin center to the heme in cytochrome b-245 and thence to oxygen.	4,6-dinitro-o-cresol	99-105	mitochondrially encoded cytochrome b	Homo sapiens	325-337	
7896790-6	1995	Here, we provide direct evidence that p67phox alone can facilitate electron flow from NADPH to the flavin center of NADPH oxidase in the absence of p47phox, resulting in the reduction of enzyme FAD, whereas the presence of p47phox is required in order for electron transfer to proceed beyond the flavin center to the heme in cytochrome b-245 and thence to oxygen.	4,6-dinitro-o-cresol	296-302	mitochondrially encoded cytochrome b	Homo sapiens	325-337