Crystallographic Studies of p-Cresol Methylhydroxylase and Methylamine Dehydrogenase Enzyme Systems

将对两种细菌酶系统进行x射线衍射研究，每一种系统都涉及氧化还原和电子转移反应。在3.0 A分辨率下计算了对甲酚甲基羟化酶晶体的电子密度图，并对多肽链的路径进行了追踪。在氨基酸序列与密度拟合后，将对结构进行细化，并研究底物与抑制剂的结合。制备了氨基花青素、甲胺脱氢酶及其分子间复合物的结晶。Mathews博士从事生物大分子的结构研究多年，使用x射线衍射方法。他对b型细胞色素的研究在一定程度上导致了一个关于电子传递蛋白如何相互作用并将电子传递给另一个的工作假设。他的方法的独特之处在于，研究中的一个系统在同一分子中同时具有供体和受体电子转移基团，而另一个系统包含一个新的假基

X-ray diffraction studies will be carried out on two bacterial enzyme systems each involving oxidation-reduction and electron transfer reactions. An electron density map for crystals of p-cresol methylhydroxylase has been computed at 3.0 A resolution and the paths of the polypeptide chains have been traced. After the amino acid sequence has been fitted to the density, the structure will be refined and the binding of substrate and inhibitors studied. Crystals of amicyanin, methylamine dehydrogenase and of their intermolecular complex have been prepared. Their structures will be analyzed by anomalous scattering, multiple isomorphous replacement and/or molecular replacement methods Dr. Mathews has engaged in structural studies of biological macromolecules using X-ray diffraction methods for many years. His work on b type cytochromes has led in part to a working hypothesis of how electron transport proteins interact and pass electrons from one to another. His approach is unique in that one of the systems under study has both the donor and acceptor electron transfer groups in the same molecule, while the other system contains a novel prosthetic group.***//