PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9437521-4	1997	Here we report that in the presence of nitrite ions (NO2-), MXH2 undergoes oxidation by the mammalian enzyme lactoperoxidase (LPO) and hydrogen peroxide and that the process proceeds at a rate that is proportional to NO2- concentration.	Nitrogen Dioxide	53-56	lactoperoxidase	Homo sapiens	109-124	
10218656-0	1999	Oxidation of biological electron donors and antioxidants by a reactive lactoperoxidase metabolite from nitrite (NO2-): an EPR and spin trapping study.	Nitrogen Dioxide	112-115	lactoperoxidase	Homo sapiens	71-86	
10218656-1	1999	We report that a lactoperoxidase (LPO) metabolite derived from nitrite (NO2-) catalyses one-electron oxidation of biological electron donors and antioxidants such as NADH, NADPH, cysteine, glutathione, ascorbate, and Trolox C.	Nitrogen Dioxide	72-75	lactoperoxidase	Homo sapiens	17-32	
10218656-1	1999	We report that a lactoperoxidase (LPO) metabolite derived from nitrite (NO2-) catalyses one-electron oxidation of biological electron donors and antioxidants such as NADH, NADPH, cysteine, glutathione, ascorbate, and Trolox C.	Nitrogen Dioxide	72-75	lactoperoxidase	Homo sapiens	34-37	
10218656-5	1999	We propose that in the LPO/H2O2/NO2-/biological electron donor systems the nitrite functions as a catalyst because of its preferential oxidation by LPO to a strongly oxidizing metabolite, most likely a nitrogen dioxide radical *NO2, which then reacts with the biological substrates more efficiently than does LPO/H2O2 alone.	Nitrogen Dioxide	32-35	lactoperoxidase	Homo sapiens	23-26	
10218656-5	1999	We propose that in the LPO/H2O2/NO2-/biological electron donor systems the nitrite functions as a catalyst because of its preferential oxidation by LPO to a strongly oxidizing metabolite, most likely a nitrogen dioxide radical *NO2, which then reacts with the biological substrates more efficiently than does LPO/H2O2 alone.	Nitrogen Dioxide	32-35	lactoperoxidase	Homo sapiens	148-151	
10218656-5	1999	We propose that in the LPO/H2O2/NO2-/biological electron donor systems the nitrite functions as a catalyst because of its preferential oxidation by LPO to a strongly oxidizing metabolite, most likely a nitrogen dioxide radical *NO2, which then reacts with the biological substrates more efficiently than does LPO/H2O2 alone.	Nitrogen Dioxide	32-35	lactoperoxidase	Homo sapiens	148-151	
10218656-5	1999	We propose that in the LPO/H2O2/NO2-/biological electron donor systems the nitrite functions as a catalyst because of its preferential oxidation by LPO to a strongly oxidizing metabolite, most likely a nitrogen dioxide radical *NO2, which then reacts with the biological substrates more efficiently than does LPO/H2O2 alone.	Nitrogen Dioxide	228-231	lactoperoxidase	Homo sapiens	23-26	
10218656-5	1999	We propose that in the LPO/H2O2/NO2-/biological electron donor systems the nitrite functions as a catalyst because of its preferential oxidation by LPO to a strongly oxidizing metabolite, most likely a nitrogen dioxide radical *NO2, which then reacts with the biological substrates more efficiently than does LPO/H2O2 alone.	Nitrogen Dioxide	228-231	lactoperoxidase	Homo sapiens	148-151	
10218656-5	1999	We propose that in the LPO/H2O2/NO2-/biological electron donor systems the nitrite functions as a catalyst because of its preferential oxidation by LPO to a strongly oxidizing metabolite, most likely a nitrogen dioxide radical *NO2, which then reacts with the biological substrates more efficiently than does LPO/H2O2 alone.	Nitrogen Dioxide	228-231	lactoperoxidase	Homo sapiens	148-151	
11389723-1	2001	The reactions of lactoperoxidase (LPO) intermediates compound I, compound II and compound III, with nitrite (NO2(-)) were investigated.	Nitrogen Dioxide	109-112	lactoperoxidase	Homo sapiens	17-32	
11389723-1	2001	The reactions of lactoperoxidase (LPO) intermediates compound I, compound II and compound III, with nitrite (NO2(-)) were investigated.	Nitrogen Dioxide	109-112	lactoperoxidase	Homo sapiens	34-37	
9667498-0	1998	Lactoperoxidase-catalyzed oxidation of melanin by reactive nitrogen species derived from nitrite (NO2-): an EPR study.	Nitrogen Dioxide	98-102	lactoperoxidase	Homo sapiens	0-15	
9667498-6	1998	We propose that the mechanism for the generation of melanin radicals by the LPO/H2O2/nitrite system involves oxidation of NO2- by LPO/H2O2 to a reactive metabolite, most likely the nitrogen dioxide radical (.NO2), which subsequently reacts with melanin 5,6-dihydroxyindole subunits producing the respective semiquinone radicals.	Nitrogen Dioxide	122-125	lactoperoxidase	Homo sapiens	76-79	
9667498-6	1998	We propose that the mechanism for the generation of melanin radicals by the LPO/H2O2/nitrite system involves oxidation of NO2- by LPO/H2O2 to a reactive metabolite, most likely the nitrogen dioxide radical (.NO2), which subsequently reacts with melanin 5,6-dihydroxyindole subunits producing the respective semiquinone radicals.	Nitrogen Dioxide	122-125	lactoperoxidase	Homo sapiens	130-133	
9667498-6	1998	We propose that the mechanism for the generation of melanin radicals by the LPO/H2O2/nitrite system involves oxidation of NO2- by LPO/H2O2 to a reactive metabolite, most likely the nitrogen dioxide radical (.NO2), which subsequently reacts with melanin 5,6-dihydroxyindole subunits producing the respective semiquinone radicals.	Nitrogen Dioxide	208-211	lactoperoxidase	Homo sapiens	76-79	
9667498-6	1998	We propose that the mechanism for the generation of melanin radicals by the LPO/H2O2/nitrite system involves oxidation of NO2- by LPO/H2O2 to a reactive metabolite, most likely the nitrogen dioxide radical (.NO2), which subsequently reacts with melanin 5,6-dihydroxyindole subunits producing the respective semiquinone radicals.	Nitrogen Dioxide	208-211	lactoperoxidase	Homo sapiens	130-133	
9437521-4	1997	Here we report that in the presence of nitrite ions (NO2-), MXH2 undergoes oxidation by the mammalian enzyme lactoperoxidase (LPO) and hydrogen peroxide and that the process proceeds at a rate that is proportional to NO2- concentration.	Nitrogen Dioxide	53-56	lactoperoxidase	Homo sapiens	126-129	
9437521-7	1997	We propose that oxidation of MXH2 is mediated by an LPO/ H2O2 metabolite of NO2-, most likely the .NO2 radical.	Nitrogen Dioxide	76-79	lactoperoxidase	Homo sapiens	52-55	
9065416-8	1997	Collectively, our results suggest that NO2-, at physiological or pathological levels, is a substrate for the mammalian peroxidases MPO and lactoperoxidase and that formation of NO2.	Nitrogen Dioxide	39-42	lactoperoxidase	Homo sapiens	139-154	
2827739-4	1987	Interconversion of the ferrous LPO/NO complex and the ferric LPO/NO2- complex is achieved by addition of the appropriate oxidizing or reducing agent.	Nitrogen Dioxide	65-68	lactoperoxidase	Homo sapiens	31-34	
2827739-4	1987	Interconversion of the ferrous LPO/NO complex and the ferric LPO/NO2- complex is achieved by addition of the appropriate oxidizing or reducing agent.	Nitrogen Dioxide	65-68	lactoperoxidase	Homo sapiens	61-64