to diffuse to, and react at, the 15LOX-2 catalytic site., in further support of the ability of NO.donor and in RAW264.7 M2 macrophages treated with ferroptosis-inducer RS元 in the presence of NO.We detected nitrosylated PE species in a biochemical system consisting of 15LOX-2/PEBP1 and NO The functional significance of these residues is supported by in silico saturation mutagenesis. to the catalytic site, as well as those stabilizing the esterified ETE-PE phospholipid tail.We identified residues that direct O 2 and NO use the same entry pores and channels connecting to 15LOX-2 catalytic site, resulting in a competition for the catalytic site. Here, we use a biochemical model of recombinant 15LOX-2 complexed with PEBP1, LC-MS redox lipidomics, and structure-based modeling and simulations to uncover the mechanism through which NO interference with 15LOX/PEBP1 activity remained unclear.suppressed ferroptosis via inhibition of hydroperoxy-eicosatetraenoyl-phosphatidylethanolamine (HpETE-PE) production by 15-lipoxygenase (15LOX) complexed with PE-binding protein 1 (PEBP1).We recently discovered an anti-ferroptotic mechanism inherent to M1 macrophages whereby high levels of NO
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