NEW SOFTWARE FOR OPERATION OF PULSE PROGRAMMER TO IMPLEMENT HYSCORE

启动了7.8 GHz、9.5 GHz和10.8 GHz的ESEEM研究，以便 研究了高能和高能分子的配体结构和电荷对称性 低pH形成的蛋白质。ESEEM光谱表明有两个 咪唑与铜配位，与两个氮基(A)偶联 CuD9组态的自旋离域测量)不同。 该蛋白质的高pH和低pH形态的ESEEM光谱为 在性质上相同的。然而，组合中的宽度变化 谱线表示相对几何结构的重组 这两种咪唑类化合物的pH升高。没有迹象表明有新的 高pH条件下的配位体。此外，还计算了四极杆的参数。 远程咪唑氮原子保持不变。唯一显而易见的是 这两种蛋白质之间的区别在于核的大小 超精细耦合，这似乎在高pH形式的 蛋白。一篇关于漆树的论文已经被接受为

ESEEM studies at 7.8, 9.5, and 10.8 GHz were initiated in order to investigate the ligand structure and charge symmetry of the high and low pH forms of the protein. ESEEM spectra suggest that there are two imidazoles coordinated to copper, with coupling to two nitrogens (a measure of spin delocalization for the Cu d9 configuration) differing. The ESEEM spectra of high and low pH forms of the protein are qualitatively identical. However, the change of width in combination lines of the spectrum indicate reorganization of relative geometry of the two imidazoles at elevated pH. There is no indication of a new ligands at high pH. Furthermore, the quadrupole parameters of the remote imidazole nitrogen atoms are unchanged. The only apparent difference between the two proteins is the magnitude of the nuclear hyperfine coupling, which seems to be less in the high pH form of the protein. A paper on the Rhus stellacyanin has been accepted for