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Crystal structure of the ferric homotetrameric beta(4) human hemoglobin

机译:铁质同种聚明β(4)人血红蛋白的晶体结构

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摘要

Spectroscopic studies carried out in the early seventies have shown that the beta-homotetramer of human hemoglobin (beta(4)-HbA) in the ferric state is a mixture of aquomet and bis-histidyl forms. Here we present the first crystal structure, solved at 2.10 angstrom resolution, of the oxidized form of beta(4)-HbA. The overall quaternary structure of the protein in the ferric state is virtually indistinguishable from that of the ferrous deoxygenated and carbomonoxy forms. The structure reveals that the four hemes are exclusively in an aquomet coordination, without any trace of bis-histidyl coordination. The oxidation of beta(4)-HbA is associated with the formation of a disulfide bridge between residues Cys112(G14) of beta(1)/beta(4) and beta(2)/beta(3) chains. The coordination state of beta(4)-HbA has been compared to that known for other organisms that exhibit bis-histidyl heme coordination in the beta(4) state. This occurrence has been discussed in terms of different organism physiology.
机译:在初期进行的光谱研究表明,在亚铁状态下的人血红蛋白(β(4)-HBA)的β-同型异构体是水性和双组织基团的混合物。在这里,我们介绍了以2.10埃达到的β(4)-HBA的氧化形式溶解的第一晶体结构。在铁状态下蛋白质的整体季结构几乎无法区分,从含铁氧化氧化和碳环氧基形式的形式中难以区分。该结构表明,四个血液仅在仿生协调中,没有任何痕迹的双组织协调。 β(4)-HBA的氧化与β(1)/β(4)和β(2)/β(3)链之间的残基Cys112(G14)之间的二硫桥的形成有关。将β(4)-HBA的配位状态与其他生物体已知的,其在β(4)状态下表现出双组氨基血红素配位。这种发生已经在不同的生物体生理学方面讨论过。

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