Physiochemical Studies on Xanthine Oxidizing Enzymes

黄嘌呤氧化酶的理化研究

• 批准号: 8803843
• 负责人: Vincent Massey
• 金额: $ 44.82万
• 依托单位: Regents of the University of Michigan - Ann Arbor
• 依托单位国家: 美国
• 项目类别: Continuing Grant
• 财政年份: 1988
• 资助国家: 美国
• 起止时间: 1988-11-01 至 1993-10-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=8803843&HistoricalAwards=false
• 关键词: Physiochemical; Studies; Xanthine; Oxidizing; Enzymes

Dr. Massey is continuing his study of milk xanthine oxidase in which the chemical, physical and structural properties of the four redox centers of the enzyme and the interactions between them will be examined. The project will also include a comparative study with two closely related enzymes, the dehydrogenase form of the milk enzyme and the stable xanthine dehydrogenase from chicken liver. Major use will be made of stopped flow optical techniques to monitor oxidation and reduction of the redox centers under various conditions as well as extensive use of 13C NMR to study the interaction of substrates, products and inhibitors with the molybdenum center. Xanthine oxidase is a well-studied molybdenum-containing hydroxylase and studies on the enzyme lie at the forefront of our efforts to establish the structure of the molybdenum centers and the chemical mechanisms operative in this small but important class of enzymes. Because xanthine oxidase contains no fewer than four centers capable of reversibly taking up reducing equivalents, the enzyme also serves as a useful model for the interaction of redox-active centers in the more complicated systems of photosynthetic and mitochondrial electron transport. ***

梅西博士正在继续他对牛奶黄嘌呤氧化酶的研究 其中的化学、物理和结构特性 酶的四个氧化还原中心和相互作用 他们之间将被审查。 该项目还将包括 对两种密切相关的酶进行了比较研究， 脱氢酶形式的牛奶酶和稳定的黄嘌呤 从鸡肝中提取脱氢酶 将主要利用 停止流动光学技术来监测氧化， 还原的氧化还原中心在各种条件下， 以及广泛使用13C NMR来研究 与钼的底物、产物和抑制剂 中心 黄嘌呤氧化酶是一种被充分研究的含铼 羟化酶及其研究处于前沿 我们努力建立钼的结构 中心和化学机制运作在这个小 但很重要的一类酶 因为黄嘌呤氧化酶 包含不少于四个能够可逆地 吸收还原当量，该酶还充当 氧化还原活性中心相互作用的有用模型， 更复杂的光合系统， 线粒体电子传递***