Skjeldal L, Krane J, Ljones T
Department of Chemistry, University of Trondheim, Dragvoll, Norway.
Int J Biol Macromol. 1989 Dec;11(6):322-5. doi: 10.1016/0141-8130(89)90001-9.
Proton magnetic resonance spectra at 500 MHz are reported for the oxidized and reduced forms of the 2[4Fe-4S]-ferredoxin from Clostridium pasteurianum. The reduced protein showed additional peaks in the 10-60 ppm region, which were previously unobserved, and there were significant differences between oxidized and reduced states in the whole region. The electron exchange rate in partially reduced ferredoxin is slow on the n.m.r. time scale when reduced with sodium dithionite, but fast when zinc reduced methyl viologen is used as reducing agent. We explain the difference between fast and slow exchange as being due to the different chemical properties of the two reducing agents.
报道了来自巴氏梭菌的2[4Fe-4S]铁氧化还原蛋白氧化态和还原态在500MHz下的质子磁共振谱。还原态蛋白质在10 - 60ppm区域显示出额外的峰，这是之前未观察到的，并且在整个区域氧化态和还原态之间存在显著差异。当用连二亚硫酸钠还原时，部分还原的铁氧化还原蛋白中的电子交换速率在核磁共振时间尺度上较慢，但当使用锌还原甲基紫精作为还原剂时则较快。我们解释快速交换和慢速交换之间的差异是由于两种还原剂的化学性质不同。
