Physical Studies of Xanthine Oxidase and Aresenite Oxidase

希尔博士将继续研究钼羟化酶，黄嘌呤氧化酶。他将从物理角度全面描述酶的特性，特别是关于可能与催化有关的特征。由于各种原因，黄嘌呤氧化酶已成为典型的钼羟化酶，这是一类小而重要的金属蛋白。酶的物理化学研究处于理解钼酶的前沿，并将为了解生物电子转移过程的一般特征提供重要的见解。钼羟化酶是一种很小但非常重要的酶的成员，它负责将氧结合到各种有机和无机化合物中。与其他羟基化系统相比，它们还没有被很好地理解。这在很大程度上是由于缺乏钼中心的实验探针，钼中心缺乏其他氧化还原中心所表现出的方便的分光光度特性。然而，目前关于钼羟化酶的作用机制的可用信息表明了这些酶的几个迷人的方面。

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.