l-Proline-derived ligands to mimic the 鈥?-His-1-carboxylate鈥?triad of the non-haem iron oxidase active site

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• 作者：Victoria J. Dungan ; Shwo Mun Wong ; Sarah M. Barry¹ ; Peter J. Rutledge ; ^{peter.rutledge@sydney.edu.au}
• 关键词：Amino acids ; Biomimetic chemistry ; Bioorganic chemistry ; Non-haem iron enzymes ; Oxidation ; Synthesis
• 刊名：Tetrahedron
• 出版年：2012
• 期刊代码：107_00404020
• 类别：ch
• 出版时间：15 April, 2012
• 卷：68
• 期：15
• 页码：3231-3236
• 文件大小：198 K

摘要

Non-haem iron(II) oxidases (NHIOs) catalyse a variety of oxidative transformations in biology. The iron-binding environment of the NHIO active site typically incorporates a 鈥?-His-1-carboxylate鈥?facial triad of amino acid side-chains, a motif that has emerged as a defining feature of the enzyme family. Towards the goal of biomimetic, iron-mediated C-H activation we have synthesized a series of peptidomimetic ligands from l-proline. By coupling l-proline to 2,6-bis(bromomethyl)pyridine, 2-(bromomethyl)-6-((tert-butyldimethylsilyloxy)methyl)pyridine and picolinic acid, we have generated several new ligand architectures designed to complex with iron(II) and mimic the NHIO active site. The resulting iron complexes promote modest levels of alkene dihydroxylation and allylic oxidation using hydrogen peroxide as oxidant.