PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17964805-2	2008	The hydroxylases obtain reducing equivalents from NAD(P)H via an electron transfer chain that is initiated by an oxidoreductase containing an N-terminal ferredoxin domain and C-terminal flavin- and NAD-binding domains.	4,6-dinitro-o-cresol	186-192	oxidoreductase	Escherichia coli	113-127	
11371181-7	2001	Reoxidation of the reduced flavin by CH(2)-H(4)folate is substantially rate limiting in the physiological NADH-CH(2)-H(4)folate oxidoreductase reaction.	4,6-dinitro-o-cresol	27-33	oxidoreductase	Escherichia coli	128-142	
11371181-8	2001	In the NADH-menadione oxidoreductase reaction, the reduction of the flavin by NADH is rate limiting as is the reduction of flavin by CH(3)-H(4)folate in the CH(3)-H(4)folate-menadione oxidoreductase reaction.	4,6-dinitro-o-cresol	68-74	oxidoreductase	Escherichia coli	22-36	
11371181-8	2001	In the NADH-menadione oxidoreductase reaction, the reduction of the flavin by NADH is rate limiting as is the reduction of flavin by CH(3)-H(4)folate in the CH(3)-H(4)folate-menadione oxidoreductase reaction.	4,6-dinitro-o-cresol	68-74	oxidoreductase	Escherichia coli	184-198	
11371181-8	2001	In the NADH-menadione oxidoreductase reaction, the reduction of the flavin by NADH is rate limiting as is the reduction of flavin by CH(3)-H(4)folate in the CH(3)-H(4)folate-menadione oxidoreductase reaction.	4,6-dinitro-o-cresol	123-129	oxidoreductase	Escherichia coli	22-36	
11371181-8	2001	In the NADH-menadione oxidoreductase reaction, the reduction of the flavin by NADH is rate limiting as is the reduction of flavin by CH(3)-H(4)folate in the CH(3)-H(4)folate-menadione oxidoreductase reaction.	4,6-dinitro-o-cresol	123-129	oxidoreductase	Escherichia coli	184-198