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鲤鱼脱氧血红蛋白从紧张态到松弛态转变过程中的局部铁位点结构:一项X射线吸收近边结构(XANES)研究。

Local Fe site structure in the tense-to-relaxed transition in carp deoxyhemoglobin: a XANES (x-ray absorption near edge structure) study.

作者信息

Bianconi A, Congiu-Castellano A, Dell'Ariccia M, Giovannelli A, Morante S, Burattini E, Durham P J

出版信息

Proc Natl Acad Sci U S A. 1986 Oct;83(20):7736-40. doi: 10.1073/pnas.83.20.7736.

Abstract

The Fe-site structure variation in the transition from the low-affinity tense (T) quaternary structure to the high-affinity relaxed (R) structure in carp deoxyhemoglobin was studied by analysis of multiple scattering resonances in the XANES (x-ray absorption near edge structure) spectra. High signal-to-noise XANES spectra were measured at the Frascati "wiggler" synchrotron radiation facility. We find that the forces on the Fe active site due to the change of quaternary protein conformation do not induce variations greater than 0.01 A in interatomic Fe-N distances, variations greater than 0.1 A in the Fe displacement toward the heme plane, or the "doming" of the heme. The relevance of these results to the mechanism of protein control of ligand binding is discussed.

摘要

通过分析X射线吸收近边结构(XANES)光谱中的多重散射共振,研究了鲤鱼脱氧血红蛋白从低亲和力紧张(T)四级结构向高亲和力松弛(R)结构转变过程中的铁位点结构变化。在弗拉斯卡蒂“摆动器”同步辐射设施上测量了高信噪比的XANES光谱。我们发现,由于四级蛋白质构象变化而施加在铁活性位点上的力,不会导致铁-氮原子间距离的变化大于0.01埃,铁向血红素平面位移的变化大于0.1埃,也不会导致血红素的“隆起”。讨论了这些结果与蛋白质控制配体结合机制的相关性。

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本文引用的文献

4
X-ray-absorption near-edge structure of 3d transition elements in tetrahedral coordination: The effect of bond-length variation.
Phys Rev B Condens Matter. 1985 Sep 15;32(6):4292-4295. doi: 10.1103/physrevb.32.4292.
9
Resonance Raman studies of the quaternary structural change in carp deoxy hemoglobin.
FEBS Lett. 1982 Apr 19;140(2):303-6. doi: 10.1016/0014-5793(82)80919-8.

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