Structure and function of intermediates involved in metalloenzymatic N-oygenation and oxidation reactions

金属酶氮合和氧化反应中间体的结构和功能

• 批准号: 1058931
• 负责人: Carsten Krebs
• 金额: $ 39万
• 依托单位: Pennsylvania State Univ University Park
• 依托单位国家: 美国
• 项目类别: Continuing Grant
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-02-15 至 2015-01-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=1058931&HistoricalAwards=false
• 关键词: Structure; function; intermediates; involved; metalloenzymatic

This award in the Chemistry of Life Processes (CLP) program supports work by Professors J. Martin Bollinger, Jr. and Carsten Krebs at the Pennsylvania State University to study the structure and reactivity of the enzyme AurF from Streptomyces thioluteus. This enzyme is involved in the biosynthesis of the antibiotic aureothin and catalyzes the oxidation of para-aminobenzoate to para-nitrobenzoate. It employs a stable peroxo-diiron(III/III) intermediate as the oxidant. The unusual stability of the intermediate will permit determination of the intermediate's structure by a combination of crystallographic, spectroscopic, and computational methods. By defining the intermediate's reactivity toward substrate analogues, the team will unravel the mechanism of the reaction.Peroxo-diiron(III/III) complexes are common to a number of important biological oxidations that use dioxygen directly as the oxidant. New catalysts can be designed that mimic the structures and reactivities of these complexes.

这个生命过程化学（CLP）项目的奖项支持宾夕法尼亚州立大学的J. Martin Bollinger, Jr.和Carsten Krebs教授对硫硫链霉菌AurF酶的结构和反应性的研究。这种酶参与抗生素金黄色葡萄素的生物合成，并催化对氨基苯甲酸酯氧化为对硝基苯甲酸酯。它采用稳定的过氧二铁（III/III）中间体作为氧化剂。中间体不寻常的稳定性将允许通过结合晶体学、光谱和计算方法来确定中间体的结构。通过定义中间体对底物类似物的反应性，研究小组将揭开反应的机制。过氧二铁（III/III）配合物在许多直接使用二氧作为氧化剂的重要生物氧化中是常见的。可以设计新的催化剂来模拟这些配合物的结构和反应活性。