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红氧还蛋白的电子和磁性特性:一项低温磁圆二色性研究。

The electronic and magnetic properties of rubredoxin: a low-temperature magnetic circular dichroism study.

作者信息

Bennett D E, Johnson M K

出版信息

Biochim Biophys Acta. 1987 Jan 5;911(1):71-80. doi: 10.1016/0167-4838(87)90272-x.

DOI:10.1016/0167-4838(87)90272-x
PMID:3024732
Abstract

Oxidized rubredoxin from Clostridium pasteurianum has been investigated by magnetic circular dichroism (MCD) spectroscopy over the temperature range 1.5 to 150 K and at magnetic fields between 0 and 4.5 tesla. The results show that studies of the temperature and field dependence of MCD transitions afford insight into the polarization of electronic transitions for ground states with large g-value anisotropy, in addition to estimates of ground-state g values and zero-field splitting parameters. In agreement with the assignment made by Eaton and Lovenberg (Eaton, W.A. and Lovenberg, W. (1973) in Iron-Sulfur Proteins, Vol. II (Lovenberg, W., ed.), pp. 131-162, Academic Press, New York), the ultraviolet-visible spectrum of oxidized rubredoxin is assigned to two S----Fe(III) charge transfer transitions (both 6A1----6T2 under tetrahedral symmetry), each spanning a range of 650-430 nm and 430-330 nm, respectively. The observed splitting in each of these transitions is attributed to a predominant axial distortion in the excited state resulting in effective D2d symmetry.

摘要

利用磁圆二色性(MCD)光谱,在1.5至150 K的温度范围以及0至4.5特斯拉的磁场条件下,对来自巴氏芽孢杆菌的氧化型红素氧还蛋白进行了研究。结果表明,除了对基态g值和零场分裂参数进行估计外,研究MCD跃迁的温度和场依赖性有助于深入了解具有大g值各向异性的基态电子跃迁的极化情况。与伊顿和洛文贝格(伊顿,W.A.和洛文贝格,W.(1973年),《铁硫蛋白》,第二卷(洛文贝格,W.主编),第131 - 162页,学术出版社,纽约)所做的归属一致,氧化型红素氧还蛋白的紫外可见光谱被归属为两个S→Fe(III)电荷转移跃迁(在四面体对称性下均为6A1→6T2),分别跨越650 - 430 nm和430 - 330 nm的范围。在这些跃迁中观察到的分裂归因于激发态中主要的轴向畸变,从而导致有效的D2d对称性。

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