Many　studies　have　showed　that　peroxynitrite-mediated　injury　on　fibrinogen　has　some　relations　with　Thrombotic　diseases.　However　there　are　few　reports　about　structural　changes　of　nitrified　fibrinogen　when　metallic　ions　exist　in　this　reaction.　In　this　study,　we　use　methods　of　FTIR-ATR　spectra　and　3D　Fluorescence　spectra　to　study　the　structural　changes　on　fibrinogen　after　nitration　and　oxidation　damages　caused　by　ONOO-　with　Cu(II)　exist.　Our　results　showed　that　Cu(II)　enhance　the　production　of　3-nitrotyrosine　in　proteins,　The　FTIR　spectra　indicated　that　the　α-helix　in　fibrinogen　reacted　with　ONOO-　by　adding　Cu(II)　decreases　from　38.03　%　to　28.5　%,　whereas　β-sheet　increases　from　29.89%　to　43.99　%.　Consequently,　Cu(II)　could　promote　Fg　nitration　with　its　concentration　dependence.　©　2010　IEEE.