Tuning Redox Potentials of Metal Centers in a Single Protein

调节单一蛋白质中金属中心的氧化还原电位

基本信息

批准号：
1413328
负责人：
Yi Lu
金额：
$ 50万
依托单位：
University of Illinois at Urbana-Champaign
依托单位国家：
美国
项目类别：
Standard Grant
财政年份：
2014
资助国家：
美国
起止时间：
2014-07-01 至 2017-06-30
项目状态：
已结题

来源：
https://www.nsf.gov/awardsearch/showAward?AWD_ID=1413328&HistoricalAwards=false
关键词：
Tuning Redox Potentials Metal Centers

项目摘要

The Chemistry of Life Processes Program in the Chemistry Division is funding Dr. Yi Lu of University of Illinois at Urbana-Champaign to study the dependence of the redox potential of metal centers in proteins on the secondary coordination sphere of the metal center. This effort is important because the redox potential of proteins is a property at the heart of many chemical and biological processes, ranging from electron transfer in photosynthesis and respiration, to catalysis in fuel cells and nitrogen fixation. Despite the importance of redox potentials, a comprehensive and systematic understanding of factors that control the redox potentials of the proteins, particularly those factors that do not perturb the primary coordination sphere of the metal centers, remains elusive. This project will contribute to filling this knowledge gap; the new knowledge will be applied in addressing interesting problems in chemistry and biology. The interdisciplinary research will be a ground for the sound training of students. The results of the research will be integrated in new and existing courses and in presentations to a broad range of audiences. This research project will advance the fundamental understanding of the factors that affect the redox potential of metal centers in proteins. The new understanding will be applied in the synthesis of new water-soluble, stable redox agents for biochemical studies, which in turn will be used to study the transfer of electrons in the inverted regime of Marcus theory, and of biocatalysts whose activity is tuned by changes in their redox potential. The methods by which the redox potential will be rationally modified include point mutation directed exclusively to the second-coordination sphere of the metal, use of non-natural amino acids to change the steric and electronic properties of the metal site in ways not possible using natural amino acids, and protein directed evolution to afford the fast exploration of a relatively large sequence space.

化学司的化学过程计划是为伊利诺伊大学伊利诺伊大学伊利诺伊大学 - 卢巴纳·坎普尼（Urbana-Champaign）的Yi lu博士提供资金，以研究金属中心在蛋白质中的氧化还原电位对金属中心的次级配位领域的依赖性。这项工作很重要，因为蛋白质的氧化还原潜力是许多化学和生物过程的核心，从光合作用和呼吸中的电子转移到燃料电池中的催化和氮固定。尽管氧化还原电位的重要性，但对控制蛋白质的氧化还原电位的因素，尤其是那些不会扰乱金属中心主要协调领域的因素的全面，系统地了解仍然难以捉摸。该项目将有助于填补这一知识差距；新知识将用于解决化学和生物学中有趣的问题。跨学科研究将是对学生进行合理培训的基础。该研究的结果将集成到新的和现有的课程中，并向广泛的受众介绍。该研究项目将提高对影响蛋白质金属中心氧化还原潜力的因素的基本理解。新的理解将应用于新的水溶性，稳定的氧化还原剂进行生物化学研究的合成，这反过来又将用于研究在Marcus理论倒转状态以及生物催化剂中的电子转移，其活性通过其氧化还原电位的变化调整了活性。氧化还原电势将合理修改的方法包括专门针对金属的第二配体球，使用非天然氨基酸来改变金属位点的空间和电子特性，无法使用天然氨基酸，蛋白质，蛋白质的进化来实现较大层次的快速探索。