人脱氧血红蛋白的飞行时间中子衍射初步研究。
Preliminary time-of-flight neutron diffraction study of human deoxyhemoglobin.
作者信息
Kovalevsky A Y, Chatake T, Shibayama N, Park S-Y, Ishikawa T, Mustyakimov M, Fisher S Z, Langan P, Morimoto Y
机构信息
Bioscience Division, MS M888, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Apr 1;64(Pt 4):270-3. doi: 10.1107/S1744309108005137. Epub 2008 Mar 21.
Human hemoglobin (HbA) is an intricate system that has evolved to efficiently transport oxygen molecules (O(2)) from lung to tissue. Its quaternary structure can fluctuate between two conformations, T (tense or deoxy) and R (relaxed or oxy), which have low and high affinity for O(2), respectively. The binding of O(2) to the heme sites of HbA is regulated by protons and by inorganic anions. In order to investigate the role of the protonation states of protein residues in O(2) binding, large crystals of deoxy HbA (approximately 20 mm(3)) were grown in D(2)O under anaerobic conditions for neutron diffraction studies. A time-of-flight neutron data set was collected to 1.8 A resolution on the Protein Crystallography Station (PCS) at the spallation source run by Los Alamos Neutron Science Center (LANSCE). The HbA tetramer (64.6 kDa; 574 residues excluding the four heme groups) occupies the largest asymmetric unit (space group P2(1)) from which a high-resolution neutron data set has been collected to date.
人类血红蛋白（HbA）是一个复杂的系统，它经过进化以有效地将氧分子（O₂）从肺部输送到组织。其四级结构可以在两种构象之间波动，即T（紧张或脱氧）和R（松弛或氧合），它们对O₂的亲和力分别较低和较高。O₂与HbA血红素位点的结合受质子和无机阴离子调节。为了研究蛋白质残基质子化状态在O₂结合中的作用，在厌氧条件下于重水中培养了脱氧HbA的大晶体（约20 mm³）用于中子衍射研究。在洛斯阿拉莫斯中子科学中心（LANSCE）运行的散裂源的蛋白质晶体学站（PCS）上收集了飞行时间中子数据集，分辨率达到1.8 Å。HbA四聚体（64.6 kDa；不包括四个血红素基团时有574个残基）占据了最大的不对称单元（空间群P2₁），迄今为止已从该单元收集到高分辨率中子数据集。
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