PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17907785-4	2007	In the present study, we have systematically assessed the NADPH-dependent covalent binding of [(3)H]paroxetine to human liver microsomes and S-9 preparations in the absence and presence of cofactors of the various phase II drug-metabolizing enzymes involved in the downstream metabolism/detoxification of the putative paroxetine-catechol intermediate.	catechol	329-337	2,4-dienoyl-CoA reductase 1	Homo sapiens	58-63	
8593536-1	1995	NADPH-cytochrome1 P450 reductase and DT-diaphorase catalyze and one- and two-electron reduction of adrenochrome to its o-semiquinone and o-hydroquinone, respectively.	catechol	137-151	2,4-dienoyl-CoA reductase 1	Homo sapiens	0-5	
8593536-2	1995	Under aerobic conditions both adrenochrome o-semiquinone and o-hydroquinone proved to be unstable, undergoing autoxidation with concomitant oxygen consumption and continuous NADPH and NADH oxidation.	catechol	61-75	2,4-dienoyl-CoA reductase 1	Homo sapiens	174-179