Gayda J P, Gibson J F, Cammack R, Hall D O, Mullinger R
Biochim Biophys Acta. 1976 May 20;434(1):154-63. doi: 10.1016/0005-2795(76)90045-3.
A two-iron-two-sulphur non-haem iron protein, the ferredoxin from Spirulina maxima, has been studied by means of electron paramagnetic resonance (EPR) in the range where the spectrum loses resolution with increasing temperature. The spin-lattice relaxation times were deduced from linewidths measured by spectral simulation and their variation as a function of temperature is interpreted in terms of an Orbach mechanism. On this basis, the exchange integral between the two iron atoms, assuming as antiferromagnetic interaction between them, is estimated to be - 83 cm-1.
一种二铁二硫非血红素铁蛋白，即极大螺旋藻铁氧化还原蛋白，已通过电子顺磁共振（EPR）在光谱随温度升高而失去分辨率的范围内进行了研究。自旋晶格弛豫时间是根据通过光谱模拟测量的线宽推导出来的，并且它们随温度的变化根据奥巴赫机制进行了解释。在此基础上，假设两个铁原子之间存在反铁磁相互作用，估计它们之间的交换积分是 - 83厘米⁻¹。
