铁硫蛋白的穆斯堡尔光谱学
Mossbauer spectroscopy of the iron-sulfur proteins.
作者信息
Johnson C E, Bray R C, Cammack R, Hall D O
出版信息
Proc Natl Acad Sci U S A. 1969 Aug;63(4):1234-8. doi: 10.1073/pnas.63.4.1234.
Abstract
The Mössbauer spectra of (57)Fe in two plant ferredoxins (from spinach and Euglena) and in xanthine oxidase have been measured at a series of temperatures and magnetic fields, and are found to be similar in all three proteins. In the oxidized state the iron is nonmagnetic. In the reduced state, the iron nuclei show magnetic hyperfine interaction with an electron spin S of (1/2), producing an effective field of about 180 kG at the nuclei.
摘要
已在一系列温度和磁场条件下测量了两种植物铁氧化还原蛋白（来自菠菜和眼虫）以及黄嘌呤氧化酶中(57)Fe的穆斯堡尔谱，发现这三种蛋白质的谱图相似。在氧化态下，铁是非磁性的。在还原态下，铁核显示出与电子自旋S为(1/2)的磁超精细相互作用，在核处产生约180 kG的有效场。
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