MOSSBAUER INVESTIGATIONS OF HIGH-SPIN FERROUS HEME PROTEINS .1. CYTOCHROME-P-450
MOSSBAUER INVESTIGATIONS OF HIGH-SPIN FERROUS HEME PROTEINS .1. CYTOCHROME-P-450
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DOI：
10.1021/bi00690a001
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发表时间：
1975-01-01
期刊：
影响因子：
2.9
通讯作者：
GUNSALUS, IC
中科院分区：
文献类型：
--
作者：
CHAMPION, PM;LIPSCOMB, JD;GUNSALUS, IC
P. M. Champion,* 1 J. D. Lipscomb, § E. Münck, § P. Debrunner,* 和 I. C. Gunsalus 摘要：通过 Móss-bauer 光谱法研究了来自 Pseudomonas pulida 的细胞色素 P-450 的厌氧还原样品。在施加磁场的情况下，高自旋亚铁血红素表现出复杂的电和磁超精细相互作用模式，可以根据自旋哈密顿形式成功地进行参数化。结果表明血红素铁的对称性非常低（三斜）。配体环境和自旋轨道耦合的影响导致电子基态的大的零场分裂。电场梯度张量的特点是具有较大的不对称性
P. M. Champion,* 1 J. D. Lipscomb, § E. Münck, § P. Debrunner,* and I. C. Gunsalus abstract: Anaerobically reduced samples of cytochrome P-450 from Pseudomonas pulida were studied by Móss-bauer spectroscopy. In the presence of an applied magnetic field the high-spin ferrous heme iron showed an intricate pattern of electric and magnetichyperfine interactions which could be parametrized successfully in terms of a spin Hamiltonian formalism. The results imply a very low (tri-clinic) symmetry of the heme iron. The effects of the ligand environment and ofspin-orbit coupling result in a large zero-field splitting of the electronic ground state. The elec-tric-field gradient tensor is characterized by a large asym-