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

生命过程化学(CLP)项目的这一奖项支持了J.Martin Bollinger，Jr.教授的工作。和宾夕法尼亚州立大学的卡斯滕·克雷布斯研究硫代链霉菌AurF酶的结构和反应活性。该酶参与了抗生素金黄色的生物合成，并催化对氨基苯甲酸酯氧化成对硝基苯甲酸酯。它使用稳定的过氧二铁(III/III)中间体作为氧化剂。中间体的不同寻常的稳定性将允许通过结晶学、光谱和计算方法的组合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，该团队将揭开反应的机理。过氧二铁(III/III)络合物是许多直接使用氧气作为氧化剂的重要生物氧化的共同之处。可以设计新的催化剂来模拟这些络合物的结构和反应活性。

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.