Electronic structure of cyanide complexes of hemes and heme proteins.
Electronic structure of cyanide complexes of hemes and heme proteins.
复制标题
血红素和血红素蛋白的氰化物复合物的电子结构。
DOI：
10.1016/0022-2836(71)90121-5
复制
发表时间：
1971
影响因子：
5.6
通讯作者：
M. Karplus
中科院分区：
文献类型：
--
作者：
R. Shulman;S. H. Glarum;M. Karplus
介绍了一个简单的量子力学模型来解释各种低自旋（S= 1 - 2）氰化亚铁血红素和血红素蛋白复合物的核磁共振测量的位移。该模型的一个重要元素是考虑了最高占据π轨道对，它们在D 4 h对称性中是简并的。所观察到的变化是有关的方向的扰动，解除轨道简并和耦合的非简并状态的结果对。它表明，在不同的化合物中的位移的变化可以作为一个敏感的探针的血红素基团与其环境的相互作用，特别感兴趣的是血红素在溶液中和绑定到球蛋白分子之间的差异。
A simple quantum mechanical model is introduced to interpret the shifts measured by nuclear magnetic resonance in a variety of low spin (S= 1 2) ferric cyanide heme and heme protein complexes. An essential element of the model is its consideration of the pair of highest occupied π-orbitals, which are degenerate in D 4h symmetry. The observed shifts are related to the orientation of perturbations that lift the orbital degeneracy and to a coupling of the resulting pair of non-degenerate states. It is demonstrated that the variation of the shifts in different compounds can serve as a sensitive probe for the interaction of the heme group with its environment; of particular interest is the difference between the heme in solution and bonded to a globin molecule.