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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Involvement of the distal Arg residue in Cl(-) binding of midge larval haemoglobin.
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Involvement of the distal Arg residue in Cl(-) binding of midge larval haemoglobin.

机译：参与的远端Arg残留在Cl (-)绑定的蚊幼虫血红蛋白。

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摘要

Monomeric haemoglobin component V (Hb V) from the larva of the midge Propsilocerus akamusi shows high Cl(-) affinity under high salt concentrations at acidic pH. In order to understand the structural changes that depend on Cl(-) binding, crystal structures of Hb V were determined under acidic high-salt conditions and the structural changes arising from different haem-bound ligands were simulated. Crystal structures of Hb V under acidic high-salt conditions indicated that the side chain of ArgE10 on the distal face of the haem contributes to stabilizing haem-bound Cl(-). The conformation of the Arg side chain in the Cl(-)-bound form was almost identical to that in ligated Hb V at neutral pH but not to that in met Hb V under acidic salt-free conditions. Furthermore, preliminary molecular-dynamics simulations also indicated that the swinging of the Arg side chain into the haem pocket depends on Cl(-) ligation. This result suggests that, like pH change, Cl(-) binding affects the location of the distal Arg residue. Owing to the increased positive electrostatic potential observed in the haem pocket at acidic pH, it was concluded that electrostatic changes caused by pH change and anionic ligand binding may affect the behaviour of the polar Arg residue.
机译：单体的血红蛋白成分V (Hb)蚊的幼虫Propsilocerus akamusi节目在高盐高Cl(-)亲和力在酸性博士为了浓度理解依赖的结构性变化Cl(-)绑定,Hb V的晶体结构在酸性高盐条件和决定结构变化引起的不同haem-bound配体被模拟。结构的酸性高盐下Hb V表明,侧链的条件ArgE10远脸上血红素的贡献稳定haem-bound Cl(-)。Arg的侧链在Cl(-)绑定表单中在结扎Hb V几乎相同中性pH值而不是在遇到了Hb V酸性盐条件。也初步的分子动力学模拟表明,摆动的Arg侧链到血红素口袋取决于Cl(-)结扎。这个结果表明,pH值变化,Cl (-)绑定的影响远的位置参数残渣。静电势观察血红素口袋在酸性pH值,得出结论静电引起的pH值变化和变化阴离子配体结合可能会影响行为的极性参数残渣。

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