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首页> 外文期刊>Nature >USING ANTIBODIES TO PERTURB THE COORDINATION SPHERE OF A TRANSITION METAL COMPLEX
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USING ANTIBODIES TO PERTURB THE COORDINATION SPHERE OF A TRANSITION METAL COMPLEX

机译：使用抗体干扰过渡金属配合物的配位

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摘要

METAL ions in the active sites of many metalloenzymes exhibit distinctive spectral and chemical features which are different from those of small inorganic complexes(1,2). These features are the result of the unusual geometric and electronic constraints that are imposed on the metal ion within the protein environment(3). 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 energy(4)-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 species(5). 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. [References: 29]
机译：许多金属酶活性位点中的金属离子具有独特的光谱和化学特征，与小型无机络合物（1,2）不同。这些特征是蛋白质环境中金属离子受到异常几何和电子约束的结果（3）。为了模拟合成系统中金属酶的这一特性，已经进行了很多努力，但这仍然是一项艰巨的任务。在这里，我们证明了从催化抗体科学中学到的重要经验之一-结合能可以转化为化学能（ 4）-可用于“微调”金属配合物的物理化学性质。我们证明了抗体的结合位点可以可逆地扰动金属离子的配位几何，并可以稳定高能配位物种（5）。具体而言，旨在结合有机硅化合物1（图1）的抗体也结合几何相似的Cu（I）配合物2。但是，抗体结合的2略微压缩形式，其大小更接近1。通过光谱偏移表现出来-一种“免疫变色”效应。 [参考：29]

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