Bertrand P, Gayda J P
Biochim Biophys Acta. 1982 Jun 18;680(3):331-5. doi: 10.1016/0005-2728(82)90146-3.
It is shown that in the [2Fe-2S] ferredoxins, the exchange interactions between the two iron atoms of the redox cluster provide stabilization of the oxidized state. Compared to the uncoupled situation, this leads to a significant lowering of the redox potential which can be larger than 100 mV. This effect could be one of the main origins of the low potential of these ferredoxins, compared to the potential of rubredoxins.
结果表明，在[2Fe-2S]铁氧化还原蛋白中，氧化还原簇的两个铁原子之间的交换相互作用为氧化态提供了稳定性。与未耦合的情况相比，这导致氧化还原电位显著降低，其降低幅度可能大于100 mV。与红素氧还蛋白的电位相比，这种效应可能是这些铁氧化还原蛋白低电位的主要来源之一。
