PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15452775-1	2004	The mechanism for the reaction between nitric oxide (NO) and O(2) bound to the heme iron of myoglobin (Mb), including the following isomerization to nitrate, has been investigated using hybrid density functional theory (B3LYP).	Nitrates	149-156	myoglobin	Homo sapiens	92-101	
29722627-9	2018	Deoxygenated [hemoglobin + myoglobin] was not different for 40% peak ( P > 0.05) but was elevated throughout 85% peak ( P < 0.05) after nitrate.	Nitrates	136-143	myoglobin	Homo sapiens	27-36	
11258960-9	2001	This result indicates that, as confirmed from protein analysis after reacting the proteins with NO* for 10 times, when peroxynitrite is coordinated to the heme of myoglobin or hemoglobin it rapidly isomerizes to nitrate without nitrating the globins in physiologically significant amounts.	Nitrates	212-219	myoglobin	Homo sapiens	163-172	
12189042-10	2002	However, oxygenated myoglobin readily reacts with *NO to yield higher order N-oxides such as nitrate, while both the ferrous and ferric forms of the protein form a stable complex with *NO.	Nitrates	93-100	myoglobin	Homo sapiens	20-29	
22062097-5	2008	Nitrite added to a batter of meat is partially oxidized to nitrate by sequestering oxygen - thus it acts as an antioxidant - a part of nitrite is bound to myoglobin, forming the heat stable NO-myoglobin, a part is bound to proteins or other substances in meat.	Nitrates	59-66	myoglobin	Homo sapiens	193-202