嗜铬粒蛋白高电位铁蛋白的质子磁共振研究。
Proton magnetic resonance studies of Chromatium high-potential iron protein.
作者信息
Phillips W D, Poe M, McDonald C C, Bartsch R G
出版信息
Proc Natl Acad Sci U S A. 1970 Oct;67(2):682-7. doi: 10.1073/pnas.67.2.682.
Abstract
Contact-shifted nuclear magnetic resonances, arising from molecular paramagnetism, have been observed in both reduced and oxidized forms of the high-potential iron protein (HiPIP) isolated from Chromatium. Contact shifts of the reduced, formally diamagnetic form increase with temperature, indicating antiferromagnetic exchange coupling of the component iron atoms with thermal population of a magnetic state. In the oxidized form of HiPIP (formally S = 1/2), contact-shifted resonances attributed to the beta-CH(2) groups of two cysteine residues display approximate Curie law behavior, while contact-shifted resonances assigned to the two other cysteine residues continue to exhibit a temperature dependence characteristic of antiferromagnetic exchange coupling. A cluster model for the redox center of Chromatium HiPIP that appears compatible with the PMR and preliminary x-ray results(4, 11) is discussed.
摘要
在从嗜色菌中分离出的高电位铁蛋白（HiPIP）的还原态和氧化态中，均观察到了由分子顺磁性引起的接触位移核磁共振现象。还原态（形式上为抗磁性）的接触位移随温度升高而增加，这表明组分铁原子之间存在反铁磁交换耦合，且有一个磁态的热布居。在HiPIP的氧化态（形式上S = 1/2）中，归属于两个半胱氨酸残基的β-CH(2)基团的接触位移共振呈现近似居里定律行为，而归属于另外两个半胱氨酸残基的接触位移共振则继续表现出反铁磁交换耦合的温度依赖性特征。本文讨论了一种与核磁共振和初步X射线结果（4, 11）相符的嗜色菌HiPIP氧化还原中心的簇模型。
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