Duhme A K, Meyer-Klaucke W, White D J, Delarbre L, Mitchenall L A, Pau R N
Department of Chemistry, The University of York, Heslington York YO10 5DD, UK.
J Biol Inorg Chem. 1999 Oct;4(5):588-92. doi: 10.1007/s007750050381.
We have studied the molybdenum K-edge X-ray absorption spectra of Mo bound in the Mo-binding proteins Mop from Haemophilus influenzae, ModG from Azotobacter vinelandii and the Escherichia coli ModE transcriptional regulatory protein, and compared them with the absorption spectra of A. vinelandii ModA and monomeric molybdate. Pre-edge and extended fine structure data indicate that the Mo-binding proteins with molbindin-like domains bind tetrahedral molybdate with a Mo-O distance of 1.76 A. The molbindin subunits or sub-domains represent a novel protein fold that is used by proteins with distinct functions to bind molybdate in the cytoplasm. The high specificity of the proteins for molybdenum does not depend on a change of coordination number or geometry.
我们研究了与钼结合的蛋白质（来自流感嗜血杆菌的Mop、来自棕色固氮菌的ModG以及大肠杆菌ModE转录调节蛋白）中钼的K边X射线吸收光谱，并将它们与棕色固氮菌ModA和单体钼酸盐的吸收光谱进行了比较。边前和扩展精细结构数据表明，具有类钼结合蛋白结构域的钼结合蛋白以1.76埃的Mo-O距离结合四面体钼酸盐。钼结合蛋白亚基或亚结构域代表一种新型蛋白质折叠，具有不同功能的蛋白质利用它在细胞质中结合钼酸盐。这些蛋白质对钼的高特异性并不取决于配位数或几何形状的变化。
