PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16249336-5	2005	The reduction of the artificial electron acceptors cytochrome c, 2,6-dichlorophenolindophenol, and ferricyanide was inhibited by the addition of any of these C termini to CYPOR, whereas the reduction of molecular O(2) was increased.	hexacyanoferrate III	99-111	cytochrome p450 oxidoreductase	Homo sapiens	171-176	
12730215-8	2003	A chimera consisting of the heme domain of nNOS and the reductase domain of CYPOR reduced cytochrome c and ferricyanide at rates 2-fold higher than that of native CYPOR, suggesting that the presence of the heme domain affected electron transfer through the reductase domain.	hexacyanoferrate III	107-119	cytochrome p450 oxidoreductase	Homo sapiens	76-81	
15451555-5	2004	Hemin also inhibited reduction of cytochrome c and ferricyanide by NPR, as much as 47%.	hexacyanoferrate III	51-63	cytochrome p450 oxidoreductase	Homo sapiens	67-70	
15943915-2	2005	Various spectrophotometric assays have been performed to examine electron-accepting properties of CPR and its ability to reduce cytochrome b5, cytochrome c, and ferricyanide.	hexacyanoferrate III	161-173	cytochrome p450 oxidoreductase	Homo sapiens	98-101	
15479629-2	2004	Various forms of spectrophotometric titration have been performed to investigate the electron-accepting properties of CPR, particularly, to examine its ability to reduce cytochrome c and ferricyanide.	hexacyanoferrate III	187-199	cytochrome p450 oxidoreductase	Homo sapiens	118-121