Rupp H, de la Torre A, Hall D O
Biochim Biophys Acta. 1979 Dec 6;548(3):552-64. doi: 10.1016/0005-2728(79)90064-1.
Photosystem I particles from spinach were reduced by illumination at 77 K. Under these conditions the one-electrom transfer from P-700 resulted in a reduction of only one acceptor molecule of the reaction centre. The EPR signals at g=2.05, 1.94 and 1.86 were attributed to reduced centre A and the smaller signals at g=2.07, 1.92 and 1.89 to reduced centre B. Reduction of both centres by dithionite in the dark lead to signals at g=2.05, 1.99, 1.96, 1.94, 1.92 and 1.89. Thus, the features at g=2.07 and 1.86 disappeared and new signals at g=1.99 and 1.96 were observed. From the spectral changes it followed that the iron-sulphur centres A and B interact magnetically. Temperature dependent EPR spectra demonstrated a faster electron spin relaxation of centre A than of centre B. These conclusions were corroborated using microwave power saturation of the respective EPR signals. The saturation data of the fully reduced centres A and B could not be fitted using the saturation equation for a one-electron spin system. The magnetic interaction between the (4Fe-4S) CENTRes of the electron acceptors A and B resulted in saturation properties which are simular to those of the 2(4Fe-4S) ferredoxin from Clostridium pasteurianum. For centre X a high proportion of homogeneous broadening of the EPR lines was inferred from the inhomogeneity parameter (b=1.83). It was, therefore, concluded that centre X is most probably an anion radical of chlorophyll. From the low temperature necessary for observing the EPR signal of centre X followed that the drastic relaxation enhancement has to be attributed to a magnetic interaction of the anion radical with iron.
菠菜的光系统I颗粒在77K下光照被还原。在这些条件下,来自P-700的单电子转移仅导致反应中心的一个受体分子被还原。g=2.05、1.94和1.86处的电子顺磁共振(EPR)信号归因于还原的中心A,而g=2.07、1.92和1.89处较小的信号归因于还原的中心B。在黑暗中用连二亚硫酸盐还原两个中心导致g=2.05、1.99、1.96、1.94、1.92和1.89处出现信号。因此,g=2.07和1.86处的特征消失,观察到g=1.99和1.96处的新信号。从光谱变化可知,铁硫中心A和B存在磁相互作用。温度依赖的EPR光谱表明,中心A的电子自旋弛豫比中心B快。使用相应EPR信号的微波功率饱和证实了这些结论。完全还原的中心A和B的饱和数据不能用单电子自旋系统的饱和方程拟合。电子受体A和B的(4Fe-4S)中心之间的磁相互作用导致了与巴氏梭菌的2(4Fe-4S)铁氧化还原蛋白相似的饱和特性。对于中心X,从不均匀性参数(b=1.83)推断EPR线有很大比例的均匀展宽。因此,得出结论,中心X很可能是叶绿素的阴离子自由基。从观察中心X的EPR信号所需的低温可以推断,剧烈的弛豫增强必须归因于阴离子自由基与铁的磁相互作用。