Physical Studies of Xanthine Oxidase and Aresenite Oxidase

希勒博士将继续他对钼羟化酶的研究， 黄嘌呤氧化酶 他将充分表征酶从一个 物理立场，特别是关于可能 与催化有关。 由于各种原因，黄嘌呤 氧化酶已成为典型的钼羟化酶， 小但重要的一类金属蛋白。 理化 对这种酶的研究是理解 钼酶，并将提供重要的洞察力， 生物电子转移过程的一般特征。 钼羟化酶是一个小的，但非常 一类重要的酶，负责 将氧掺入各种有机和无机 化合物. 与其他人相比，他们并不了解。 羟基化系统。 这在很大程度上是由于缺乏 钼中心的实验探针，缺乏 其他光谱仪显示的方便的分光光度特性 氧化还原中心 然而，目前 现有的关于药物作用机制的资料， 钼羟化酶提出了几个有趣的方面， 这些酶。

Dr. Hille will continue his study of the molybdenum hydroxylase, xanthine oxidase. He will fully characterize the enzyme from a physical stand point with particular regard to features likely to be relevant to catalysis. For a variety of reasons, xanthine oxidase has become the prototypical molybdenum hydroxylase, a small but important class of metalloproteins. Physicochemical studies of the enzyme lie at the forefront of understanding molybdenum enzymes and will provide important insight into the general features of biological electron transfer processes. Molybdenum hydroxylases are members of a small but extremely important class of enzymes that are responsible for the incorporation of oxygen into a variety of organic and inorganic compounds. They are not well understood in comparison to other hydroxylating systems. This is due in large part to the absence of experimental probes for molybdenum centers, which lack the convenient spectrophotometric properties exhibited by other oxidation - reduction centers. Nevertheless, the presently available information regarding the mechanism of action of the molybdenum hydroxylase suggests several fascinating aspects of these enzymes.