Preparation of Artificial Dicopper Enzymes for the Catalytic Reduction of CO2

催化还原CO2人工二铜酶的制备

• 批准号: 9377497
• 负责人: Jonathan D Rittle
• 金额: $ 4.53万
• 依托单位: UNIVERSITY OF CALIFORNIA, SAN DIEGO
• 依托单位国家: 美国
• 财政年份: 2016
• 资助国家: 美国
• 起止时间: 2016-09-27 至 2018-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/9377497
• 关键词: Active Sites; Amino Acids; Ammonia; Binding; Bioinorganic Chemistry; Breathing; Carbon Dioxide; Catalysis; Chemicals; Computer Simulation; Computing Methodologies; Copper; Coupling; Cytochromes; DNA Sequence Alteration; Development; Dioxygen; Engineering; Environment; Enzymes; Exhibits; Generations; Housing; Ions; Life; Ligands; Ligation; Link; Maltose; Measurement; Mediating; Metal Binding Site; Metals; Methods; Modification; Mononuclear; Motion; Nature; Oxalates; Oxidation-Reduction; Planets; Preparation; Property; Protein Engineering; Proteins; Reaction; Research; Site; Study models; System; Systems Development; Testing; Water; X-Ray Crystallography; biological systems; design; flexibility; interfacial; metalloenzyme; monomer; oxidation; periplasm; programs; protein folding; receptor; receptor binding; sample fixation; small molecule; solid state

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.

项目概要 人工金属酶的成功研发考验了我们对酶学的认识 催化、蛋白质折叠和生物无机化学。这个领域的一个独特且尚未解决的挑战是 开发具有氧化还原活性的人造金属酶，这些酶具有小分子催化活性 分子。大自然使用了多种含铜酶，这些酶利用了可调性 这种普遍存在的金属离子的氧化还原特性。该提案概述了柔性金属装订的设计 在界面处容纳两个氧化还原活性和配位不饱和铜离子的位点 互补的蛋白质单体或重新设计的麦芽糖结合受体蛋白质内。这些 设计将以计算方法、X 射线晶体学和双金属模板为指导 策略。作为对设计位点催化性能的测试，我们将研究 CuI2- CO2 催化还原偶联为草酸盐。