Some magnetic properties of Pseudomonas cytochrome oxidase.

Some magnetic properties of Pseudomonas cytochrome oxidase.
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假单胞菌细胞色素氧化酶的一些磁性。

DOI:
10.1042/bj1770029
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发表时间:
1979
期刊:
The Biochemical journal
影响因子:
--
通讯作者:
A. Thomson
A. Thomson
中科院分区:
--
文献类型:
--
作者:
T. A. Walsh;M. Johnson;C. Greenwood;D. Barber;J. Springall;A. Thomson

文献摘要

被引文献

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用m.c.d方法研究了假单胞菌细胞色素氧化酶及其氰化衍生物在氧化和还原状态下的血红素基的磁性。(磁性圆二向色性)在低温下。此外,还对该酶的氧化形式进行了研究。(电子-顺磁共振)波谱和一项平行研究,使用两者的E.P.R.和M.C.D.,在假单胞菌细胞色素c-551上进行了光谱归属。对于抗坏血酸还原的假单胞菌细胞色素氧化酶,这些特征在m.c.d.与血红素C对应的光谱以及与血红素D对应的信号的温度依赖性表明,前者是低自旋的,后者是高自旋的(S=2)。然而,在还原的酶中加入氰化物,得到了一种完全低自旋的蛋白质。环境保护局。和M.C.D.氧化假单胞菌细胞色素氧化酶及其氰化物的Sectra与两种情况下的haem c和d1组分都是低自旋的。假单胞菌细胞色素c-551在氧化和还原状态下都是低自旋的。
The magnetic properties of the haem groups of Pseudomonas cytochrome oxidase and its cyanide-bound derivatives were studied in both the oxidized and reduced states by means of m.c.d. (magnetic circular dichroism) at low temperatures. In addition, the oxidized forms of the enzyme were also investigated by e.p.r. (electron-paramagnetic-resonance) spectroscopy, and a parallel study, using both e.p.r. and m.c.d., was made on Pseudomonas cytochrome c-551 to aid spectral assignments. For ascorbate-reduced Pseudomonas cytochrome oxidase, the temperature-independence of those features in the m.c.d. spectrum corresponding to the haem c, and the temperature-dependence of those signals corresponding to the haem d1, showed the former to be low-spin and the latter to be high-spin (s = 2). However, addition of cyanide to the reduced enzyme gave a form of the protein that was completely low-spin. The e.p.r. and m.c.d. sectra of oxidized Pseudomonas cytochrome oxidase and its cyanide derivative were consistent with the haem c and d1 components being low-spin in both cases. Pseudomonas cytochrome c-551 was found to be low-spin in both its oxidized and reduced redox states.