Electron nuclear double-resonance (ENDOR) spectroscopy of amine oxidase from pig plasma.
Electron nuclear double-resonance ('ENDOR') spectroscopic studies on pig plasma amine oxidase have been carried out at 15 K. Deuterium-exchange studies show the presence of two sets of exchangeable protons, probably from two water molecules; from the magnitude of their hyperfine couplings, one is assigned to be equatorially, and the other axially, co-ordinated. Only one 14N hyperfine coupling is observed, suggesting that the bonding of all amino acid (histidine) or organic cofactor ligands is similar. Upon addition of azide, a further hyperfine coupling to nitrogen is observed which is smaller than that observed for the native enzyme; the hyperfine couplings to the remaining nitrogens are slightly altered.
D006631:Amine Oxidase (Copper-Containing); D000818:Animals; D001386:Azides / Q000494:pharmacology; D003300:Copper / Q000097:blood; D003903:Deuterium; D017666:Deuterium Oxide; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000097:blood*; D013552:Swine; D014867:Water
D001386:Azides; D014867:Water; D003300:Copper; D003903:Deuterium; D006631:Amine Oxidase (Copper-Containing); D000587:Oxidoreductases Acting on CH-NH Group Donors; D017666:Deuterium Oxide