牛细胞色素氧化酶的核磁共振氢谱研究。血红素a的顺磁位移共振
A 1H NMR study of bovine cytochrome oxidase. Paramagnetically shifted resonances of haem a.
作者信息
Rigby S E, Alleyne T A, Wilson M T, Moore G R
机构信息
School of Chemical Sciences, University of East Anglia, Norwich, England.
出版信息
FEBS Lett. 1989 Oct 23;257(1):155-8. doi: 10.1016/0014-5793(89)81809-5.
PMID:2553487
Abstract
Dimeric and monomeric forms of mitochondrial cytochrome oxidase (EC 1.9.3.1) have been examined using 1H NMR spectroscopy. Paramagnetically shifted resonances were detected in spectra of the monomeric protein. Studies of this protein in a number of oxidation and ligation states have assigned these resonances to ferrihaem a. The temperature and pH dependence of this new probe of haem a environment is reported.
摘要
已使用核磁共振氢谱对线粒体细胞色素氧化酶（EC 1.9.3.1）的二聚体和单体形式进行了研究。在单体蛋白的光谱中检测到顺磁位移共振。对处于多种氧化和连接状态的该蛋白进行的研究已将这些共振归因于高铁血红素a。报道了这种血红素a环境新探针的温度和pH依赖性。
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