FE XAS K EDGE STUDIES OF NON HEME IRON ENZYMES

非血红素铁酶的 F XAS K 边缘研究

• 批准号: 6658660
• 负责人: KEITH O HODGSON
• 金额: $ 14.32万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2002
• 资助国家: 美国
• 起止时间: 2002-03-01 至 2003-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6658660
• 关键词: biomaterials; biomedical resource; proteins; spectrometry; structural biology

X-ray absorption edge and EXAFS spectroscopy will be used to study the electronic and geometric structure of a series of mononuclear non-heme iron enzymes. The systems to be studied include the lipoxygenases, phenylalanine hydroxylase and bleomycin. The ferrous and ferric active sites of these enzymes will be studied, along with the oxygen activated and small molecule bound forms. An understanding of the electronic and geometric structure of the active sites, as well as the intermediates involved in the catalytic processes, of these enzymes will enable us to gain a better understanding of the relationship between structure and how function is achieved and controlled.

X射线吸收边和EXAFS光谱将被用来研究 一系列单核分子的电子结构和几何结构 非血红素铁酶 研究的系统包括 脂氧合酶、苯丙氨酸羟化酶和博来霉素。 亚铁 这些酶的铁活性位点将被研究，沿着 氧活化和小分子结合形式。 的理解 活性部位的电子结构和几何结构， 作为参与催化过程的中间体， 酶将使我们能够更好地了解 结构与功能实现方式之间的关系， 控制。