Slappendel S, Veldink G A, Vliegenthart J F, Aasa R, Malmström B G
Biochim Biophys Acta. 1980 Jul 24;624(1):30-9. doi: 10.1016/0005-2795(80)90222-6.
The zero-field splitting constants (D) of the different components building up the high-spin Fe(III) EPR spectrum of lipoxygenase from soybeans were determined by two methods: (1) temperature dependence studies using the low-spin Fe(III) signal of cytochrome c at g 3 for accurate measuring of the temperature in the sample; (2) by establishing g-shift upon increasing the microwave frequency. The ranges of D for the axial and rhombic species contributing to the complex signal at g 6 are found to be 1.5-3.0 K and 1.8-4.4 K, respectively. The occurrence of such large ranges is attributed to variations in amount and number of species in the different samples. The combination of the applied methods offers a more generally applicable approach to the determination of zero-field splitting constants.
通过两种方法测定了构成大豆脂氧合酶高自旋Fe(III)电子顺磁共振谱的不同组分的零场分裂常数（D）：（1）利用细胞色素c在g 3处的低自旋Fe(III)信号进行温度依赖性研究，以精确测量样品中的温度；（2）通过增加微波频率来建立g位移。在g 6处对复杂信号有贡献的轴向和菱形物种的D值范围分别为1.5 - 3.0 K和1.8 - 4.4 K。出现如此大的范围归因于不同样品中物种的数量和种类的变化。所应用方法的结合为零场分裂常数的测定提供了一种更普遍适用的方法。
