Martí Marcelo A, Capece Luciana, Bikiel Damián E, Falcone Bruno, Estrin Darío A
Departamento de Química Inorgánica, Analítica y Química Física INQUIMAE-CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Buenos Aires, Argentina.
Proteins. 2007 Aug 1;68(2):480-7. doi: 10.1002/prot.21454.
The binding of diatomic ligands, such as O(2), NO, and CO, to heme proteins is a process intimately related with their function. In this work, we analyzed by means of a combination of classical Molecular Dynamics (MD) and Hybrid Quantum-Classical (QM/MM) techniques the existence of multiple conformations in the distal site of heme proteins and their influence on oxygen affinity regulation. We considered two representative examples: soybean leghemoglobin (Lba) and Paramecium caudatum truncated hemoglobin (PcHb). The results presented in this work provide a molecular interpretation for the kinetic, structural, and mutational data that cannot be obtained by assuming a single distal conformation.
双原子配体，如O₂、NO和CO，与血红素蛋白的结合是一个与其功能密切相关的过程。在这项工作中，我们通过经典分子动力学（MD）和混合量子-经典（QM/MM）技术相结合的方法，分析了血红素蛋白远端位点的多种构象的存在及其对氧亲和力调节的影响。我们考虑了两个代表性的例子：大豆根瘤血红蛋白（Lba）和尾草履虫截短血红蛋白（PcHb）。这项工作中呈现的结果为无法通过假设单一远端构象获得的动力学、结构和突变数据提供了分子解释。
