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几种凝集素的锰离子电子自旋共振光谱

Mn2+-electron spin resonance spectra of several lectins.

作者信息

Meirovitch E, Brumberger H, Lis H

出版信息

Biophys Chem. 1978 Jul;8(3):215-9. doi: 10.1016/0301-4622(78)87003-3.

DOI:10.1016/0301-4622(78)87003-3
PMID:210854
Abstract

Mn2+-ESR spectra of soybean, wax bean and lima bean agglutinin at Q- and X-band frequencies show nearly axially symmetric zero field splitting (ZFS); the dominant anisotropic term of the spin hamiltonian is the quadratic ZFS interaction. There is a relatively large distribution of ZFS parameters. No effects of specific inhibitor (N-acetylgalactosamine) on the soybean agglutinin spectrum were observed. The stoichiometric complex obtained on addition of Mn2+ to a Mn2+-free sample of this protein has a spectrum similar to that of the native protein. The small changes in the spectrum are interpreted in terms of a wider distribution of the ZFS parameters at the Mn binding site. Addition of Ca2+ to Mn2+-soybean agglutinin sharpens the lines, possibly because Ca2+ increases the rigidity of the complex.

摘要

大豆、黄荚菜豆和利马豆凝集素在Q波段和X波段频率下的Mn2+-ESR光谱显示出近乎轴向对称的零场分裂(ZFS);自旋哈密顿量的主要各向异性项是二次ZFS相互作用。ZFS参数存在相对较大的分布。未观察到特异性抑制剂(N-乙酰半乳糖胺)对大豆凝集素光谱的影响。向该蛋白质的无Mn2+样品中添加Mn2+得到的化学计量复合物的光谱与天然蛋白质的光谱相似。光谱中的微小变化被解释为Mn结合位点处ZFS参数的分布更宽。向Mn2+-大豆凝集素中添加Ca2+会使谱线变尖锐,可能是因为Ca2+增加了复合物的刚性。

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Q-band EPR of the S2 state of photosystem II confirms an S = 5/2 origin of the X-band g = 4.1 signal.光系统II S2态的Q波段电子顺磁共振证实了X波段g = 4.1信号的S = 5/2起源。
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