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Zn2Fe2杂合血红蛋白的扩展X射线吸收精细结构研究:半结合状态下血红素键长无变化

Extended X-ray absorption fine structure studies of Zn2Fe2 hybrid hemoglobins: absence of heme bond length changes in half-ligated species.

作者信息

Simolo K, Korszun Z R, Stucky G, Moffat K, McLendon G, Bunker G

出版信息

Biochemistry. 1986 Jul 1;25(13):3773-8. doi: 10.1021/bi00361a007.

DOI:10.1021/bi00361a007
PMID:3741835
Abstract

Metal hybrid hemoglobins, in which Zn(II) replaces Fe(II), have been structurally characterized by extended X-ray absorption structure (EXAFS) studies. Since Zn and Fe have very different K absorption edge energies, the structures of the ligated (Fe) and unligated (Zn) sites could be examined independently within a single molecule that mimics an intermediate ligation state. The observed EXAFS spectra and associated structural parameters are compared among the ligand free (alpha Zn)2(beta Zn)2, half-ligated (alpha FeCO)2(beta Zn)2 and (alpha Zn)2(beta FeCO)2, and fully ligated (alpha FeCO)2(beta FeCO)2 systems.

摘要

其中锌(II)取代铁(II)的金属杂合血红蛋白已通过扩展X射线吸收结构(EXAFS)研究进行了结构表征。由于锌和铁具有非常不同的K吸收边能量,因此可以在模拟中间连接状态的单个分子中独立检查连接的(铁)和未连接的(锌)位点的结构。在无配体的(α锌)2(β锌)2、半连接的(α铁-一氧化碳)2(β锌)2和(α锌)2(β铁-一氧化碳)2以及完全连接的(α铁-一氧化碳)2(β铁-一氧化碳)2系统之间比较了观察到的EXAFS光谱和相关的结构参数。

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