Preparation of Artificial Dicopper Enzymes for the Catalytic Reduction of CO2

项目摘要 人工金属酶的成功开发考验了我们对酶的理解 催化、蛋白质折叠和生物无机化学。这个竞技场上一个独特而未得到满足的挑战是 具有氧化还原活性的人工金属酶的开发 分子。大自然使用了一系列不同的含铜酶来利用可调的 这种普遍存在的金属离子的氧化还原性质。本提案概述了柔性金属装订的设计 在界面上容纳两个氧化还原活性和配位不饱和铜离子的位置 补充蛋白单体或在重组麦芽糖结合受体蛋白内。这些 设计将以计算方法、X射线结晶学和双金属模板为指导 战略。作为对设计位置的催化性能的测试，我们将研究CuI2- 二氧化碳催化还原偶联生成草酸。

Project Summary The successful development of artificial metalloenzymes tests our understanding of enzymatic catalysis, protein folding, and bioinorganic chemistry. A distinct and unmet challenge in this arena is the development of redox-active, artificial metalloenzymes that exhibit catalytic activity with small molecules. Nature employs a diverse array of copper-containing enzymes that make use of the tunable redox properties of this ubiquitous metal ion. This proposal outlines the design of flexible metal binding sites that accommodate two redox-active and coordinatively-unsaturated copper ions at the interface of complementary protein monomers or within a reengineered maltose binding receptor protein. These designs will be guided by computational methods, X-ray crystallography and bimetallic templating strategies. As a test for the catalytic properties of the designed site, we will investigate the CuI2- catalyzed reductive coupling of CO2 to oxalate.