Watt G D, Frankel R B, Papaefthymiou G C
Proc Natl Acad Sci U S A. 1985 Jun;82(11):3640-3. doi: 10.1073/pnas.82.11.3640.
Mammalian ferritin from horse spleen undergoes an electrochemical or chemical reduction reaction in which each iron atom present is reduced by one electron (2300 electrons per ferritin molecule containing 2300 Fe3+ ions). Midpoint potentials of -190 mV, -310 mV, and -416 mV were determined at pH 7.0, 8.0, and 9.0. This variation of potential with pH indicates that approximately 2 H+ are transferred to the core for each Fe3+ reduced to Fe2+. Mössbauer measurements of partially reduced ferritin give spectra that consist of a ferric quadrupole doublet with a superposed ferrous quadrupole doublet. The relative intensities of these doublets are consistent with the electrochemically determined degree of reduction.
来自马脾的哺乳动物铁蛋白会发生电化学或化学反应，其中每个存在的铁原子被一个电子还原（每个含有2300个Fe3+离子的铁蛋白分子有2300个电子）。在pH值为7.0、8.0和9.0时测定的中点电位分别为-190 mV、-310 mV和-416 mV。这种电位随pH值的变化表明，每一个从Fe3+还原为Fe2+的铁离子大约有2个H+转移到铁蛋白核心。对部分还原的铁蛋白进行穆斯堡尔测量，得到的光谱由一个叠加在亚铁四极双峰上的铁三极双峰组成。这些双峰的相对强度与电化学测定的还原程度一致。
