Bagirov R M, Stukan R A, Dontsov A E, Ostrovskiĭ M A, Lapina V A
Biofizika. 1986 May-Jun;31(3):469-74.
Interaction between Fe2+ ions and melanoproteid granules (MPG) of bovine eye pigment epithelium was studied by gammaresonance spectroscopy. MPG was found to form complexes with bi- and three-valent ferrum ions. MPG can both directly bind Fe2+ ions and oxidize them Fe3+ inactive in prooxidant state and bind the latter. The activity of ferrum ion binding increases when suspension is illuminated with visible light and pH of the incubation solution increases. The protein part of MPG does not participate in the complex formation with ferrum ions. The complex formation proceeds mainly by carboxyl, amino- and imino-groups of melanin polymer.
利用伽马共振光谱研究了Fe2+离子与牛眼色素上皮黑素蛋白颗粒（MPG）之间的相互作用。发现MPG与二价和三价铁离子形成络合物。MPG既能直接结合Fe2+离子，又能将其氧化为处于前氧化态无活性的Fe3+并结合后者。当悬浮液用可见光照射且孵育溶液的pH值升高时，铁离子结合活性增加。MPG的蛋白质部分不参与与铁离子的络合物形成。络合物形成主要通过黑色素聚合物的羧基、氨基和亚氨基基团进行。
