PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23626907-5	2013	In this work, we tried to explain enzymatic oxidation in terms of redox potentials by employing competitive substrates for MPO such as chloride, which is oxidized by MPO to form a strong oxidant (hypochlorite), and antioxidants that have lower redox potentials than CNTs.	Chlorides	135-143	myeloperoxidase	Homo sapiens	123-126	
23626907-5	2013	In this work, we tried to explain enzymatic oxidation in terms of redox potentials by employing competitive substrates for MPO such as chloride, which is oxidized by MPO to form a strong oxidant (hypochlorite), and antioxidants that have lower redox potentials than CNTs.	Chlorides	135-143	myeloperoxidase	Homo sapiens	166-169