Physical Studies of Xanthine Oxidase and Aresenite Oxidase

希尔博士将继续他对钼羟基酶--黄嘌呤氧化酶的研究。他将从物理角度全面描述这种酶，特别是可能与催化有关的特征。由于各种原因，黄嘌呤氧化酶已经成为钼羟基酶的原型，这是一类很小但很重要的金属蛋白。对该酶的物理化学研究处于了解钼酶的前沿，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。钼羟基酶是一小类但极其重要的酶的成员，负责将氧结合到各种有机和无机化合物中。与其他羟化体系相比，人们对它们的理解还不够深入。这在很大程度上是因为没有钼中心的实验探针，这缺乏其他氧化还原中心所表现出的方便的分光光度性质。然而，目前可用的关于钼羟基酶作用机制的信息表明，这些酶有几个有趣的方面。

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.