PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16040185-8	2006	Enhanced peroxidase activity of nitrated cyt c was responsible for H2O2-induced oxidation of phospholipid membranes and H2O2/NO2--mediated nitration of other proteins.	Nitrogen Dioxide	125-128	cytochrome c, somatic	Homo sapiens	41-46	
24447894-0	2014	The kinetics of the reaction of nitrogen dioxide with iron(II)- and iron(III) cytochrome c.	Nitrogen Dioxide	32-48	cytochrome c, somatic	Homo sapiens	78-90	
24447894-5	2014	Based on these rate constants, we propose that the reaction with iron(II)cytochrome c proceeds via a mechanism in which 90% of NO2 oxidizes the iron center directly-most probably via reaction at the solvent-accessible heme edge-whereas 10% oxidizes the amino acid residues to the corresponding radicals, which, in turn, oxidize iron(II).	Nitrogen Dioxide	127-130	cytochrome c, somatic	Homo sapiens	73-85	
24447894-7	2014	Our results indicate that, in vivo, NO2 will attack preferentially the reduced form of cytochrome c; protein damage is expected to be marginal, the consequence of formation of amino acid radicals on iron(III)cytochrome c.	Nitrogen Dioxide	36-39	cytochrome c, somatic	Homo sapiens	87-99	
24447894-7	2014	Our results indicate that, in vivo, NO2 will attack preferentially the reduced form of cytochrome c; protein damage is expected to be marginal, the consequence of formation of amino acid radicals on iron(III)cytochrome c.	Nitrogen Dioxide	36-39	cytochrome c, somatic	Homo sapiens	208-220	
29257867-1	2018	The fundamental biogeochemical cycle of nitrogen includes cytochrome c nitrite reductase, which catalyzes the reduction of nitrite ions to ammonium with eight protons and six electrons (NO2- + 8H+ + 6e-   NH4+ + 2H2O).	Nitrogen Dioxide	186-189	cytochrome c, somatic	Homo sapiens	58-70	
15912211-4	2005	Peroxynitrite reacts with SDS-modified cytochrome c in the same way as with native cytochrome c, via intermediate radical products, *OH/*NO2, arising from peroxynitrite homolysis.	Nitrogen Dioxide	137-140	cytochrome c, somatic	Homo sapiens	39-51	
15912211-4	2005	Peroxynitrite reacts with SDS-modified cytochrome c in the same way as with native cytochrome c, via intermediate radical products, *OH/*NO2, arising from peroxynitrite homolysis.	Nitrogen Dioxide	137-140	cytochrome c, somatic	Homo sapiens	83-95	
14678790-3	2004	We report herein a novel function for cytochrome c as a catalyst for nitrite (NO2-) and hydrogen peroxide (H2O2)-mediated nitration reactions.	Nitrogen Dioxide	78-81	cytochrome c, somatic	Homo sapiens	38-50	
14678790-4	2004	Cytochrome c catalyzes both self- and adjacent-molecule (hydroxyphenylacetic acid, Mn-superoxide dismutase) nitration via heme-dependent mechanisms involving tyrosyl radical and *NO2 production, as for phagocyte peroxidases.	Nitrogen Dioxide	179-182	cytochrome c, somatic	Homo sapiens	0-12	
14678790-7	2004	Extensive tyrosine nitration of Mn-superoxide dismutase occurred when exposed to either cytochrome c or MPx-11 in the presence of H2O2 and NO2-, with no apparent decrease in catalytic activity.	Nitrogen Dioxide	139-142	cytochrome c, somatic	Homo sapiens	88-100