Using antibodies to perturb the coordination sphere of a transition metal complex
Using antibodies to perturb the coordination sphere of a transition metal complex
复制标题
使用抗体扰乱过渡金属络合物的配位范围
作者：
P. Ghosh;D. Shabat;Sandeep Kumar;S. Sinha;F. Grynszpan;Jian Li;Louis Noodleman;E. Keinan
许多金属酶活性部位的金属离子表现出不同于小的无机络合物的独特的光谱和化学特征1，2。这些特征是在蛋白质环境中对金属离子施加的不寻常的几何和电子约束的结果。为了在合成系统中模拟金属酶的这一特征，人们投入了大量的精力，但这仍然是一项艰巨的任务。在这里，我们展示了从催化抗体科学中学到的关键经验之一--结合能可以转化为化学能--可以被用来‘微调’金属络合物的物理化学性质。我们发现，抗体的结合部位可以可逆地扰乱金属离子的配位几何结构，并可以稳定高能配位物种。具体地说，旨在结合有机硅化合物1的抗体(图1)也与几何上相似的铜(I)配合物2结合。然而，抗体结合的是略有压缩的2，其大小更接近1。这种扭曲表现为光谱位移--一种“免疫变色”效应。
METAL ions in the active sites of many metalloenzymes exhibit distinctive spectral and chemical features which are different from those of small inorganic complexes1,2. These features are the result of the unusual geometric and electronic constraints that are imposed on the metal ion within the protein environment3. Much effort has been invested to try to mimic this feature of metalloenzymes in synthetic systems, but this remains a formidable task. Here we show that one of the key lessons learned from the science of catalytic antibodies—that binding energy can be converted into chemical energy4—can be exploited to 'fine-tune' the physicochemical properties of a metal complex. We show that an antibody's binding site can reversibly perturb the coordination geometry of a metal ion, and can stabilize a high-energy coordinated species5. Specifically, antibodies designed to bind the organosilicon compound 1 (Fig. 1) also bind the geometrically similar Cu(I) complex 2. However, the antibody binds a slightly compressed form of 2, which is closer in size to 1. This distortion is manifested by a spectral shift—an 'immunochromic' effect.
影响因子：
56.9
作者：
SOLOMON, EI;LOWERY, MD
通讯作者：
LOWERY, MD