Baker G J, Knowles P F, Pandeya K B, Rayner J B
Biochem J. 1986 Jul 15;237(2):609-12. doi: 10.1042/bj2370609.
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.
已在15K下对猪血浆胺氧化酶进行了电子核双共振(“ENDOR”)光谱研究。氘交换研究表明存在两组可交换质子,可能来自两个水分子;根据它们超精细耦合的大小,一个被指定为赤道配位,另一个为轴向配位。仅观察到一个14N超精细耦合,这表明所有氨基酸(组氨酸)或有机辅因子配体的键合是相似的。加入叠氮化物后,观察到与氮的另一个超精细耦合,其比天然酶观察到的要小;与其余氮的超精细耦合略有改变。