Luisi B, Liddington B, Fermi G, Shibayama N
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.
J Mol Biol. 1990 Jul 5;214(1):7-14. doi: 10.1016/0022-2836(90)90139-d.
We have determined the structure of a T-state haemoglobin in which the haem groups of the beta subunits have carbon monoxide bound, and the alpha subunits have nickel replacing the haem iron and are ligand-free. The structural adjustments on binding ligand in the T state are in the same direction as those associated with the quaternary transition, and a translational shift of the haem is severely restricted. We explain how these observations may account for the low ligand affinity of the beta haem of T-state haemoglobin.
我们已经确定了一种T态血红蛋白的结构，其中β亚基的血红素基团结合了一氧化碳，而α亚基则用镍取代了血红素铁且无配体。T态中结合配体时的结构调整方向与四级结构转变相关的调整方向相同，并且血红素的平移移动受到严重限制。我们解释了这些观察结果如何能够解释T态血红蛋白β血红素的低配体亲和力。
