Iron core formation in ferritins.
Iron core formation in ferritins.
复制标题
铁蛋白中铁核的形成。
DOI：
10.1007/978-1-4684-8041-2_18
复制
发表时间：
1989
期刊：
影响因子：
--
通讯作者：
Sayers,DE
中科院分区：
文献类型：
--
作者：
Theil,EC;Sayers,DE
Iron is the most abundant transition metal in biology. Proteins containing iron are important for DNA synthesis, respiration, photosynthesis, nitrogen fixation and the transport and activation of dioxygen. Two properties of Fe(III) in aqueous solution lead to the formation of large, insoluble aggregates of iron and oxygen: first, the pKa of a proton in water coordinated to Fe(III) is ca 3; second, after proton loss, the conjugate bases form stable oxygen bridges to each other with the elimination of water. Thus unless ligands other than water are coordinated to Fe(III), the solubility of Fe(III) is very low under physiological conditions (ca 10−18M) (Biedermann and Schindler, 1957). Animals, plants and microorganisms use ferritin, an iron protein complex, to accumulate reserves of iron sufficently high for the synthesis of proteins that have iron at the active center. Ferritin also provides a site for the detoxification of excess iron which enters an organism or cell when the normal barriers to controlled iron uptake are breached.
