PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 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 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