Collaborative Research: Study of A- and B-class dye-decolorizing peroxidases (DyPs): From molecular mechanisms to applications in dye removal and lignin degradation

利用该奖项，化学学部生命过程化学项目资助了堪萨斯州立大学的李平博士和佛罗里达州立大学的宋立凯博士，研究A级和b级染料脱色过氧化物酶（DyPs）的分子机制及其结构-性质-反应-功能（SPRF）关系。该研究结果可用于废水处理和生物燃料生产的生物催化剂的开发。所提出的研究填补了关于DyPs的关键知识空白，并指导蛋白质工程可能导致具有增强氧化活性的酶。这种追求使研究生和博士后学员能够获得从化学到生物学等多学科领域的专业知识，从而为他们成为成功的下一代科学家做好准备。此外，该公司还为一项外展计划做出了贡献，该计划鼓励来自STEM职业中代表性不足的群体的学生主修科学。本课题旨在阐明一类新的h2o2依赖性血红素过氧化物酶家族DyPs的分子机制和SPRF关系。本研究以弧面热孢菌的TcDyP和溶木质素肠杆菌的ElDyP分别作为该家族A类酶和b类酶的代表。利用结构生物学、酶学和电子顺磁共振（EPR）研究方法，研究了位于酶表面负责TcDyP中底物氧化的残基、控制涉及ElDyP化合物I的单电子和双电子还原反应的残基以及DyPs中血红素袋周围环的动力学。有机合成和蛋白质工程被用来定义和调节SPRF关系。该研究不仅填补了DyPs的基础知识空白，而且为DyPs在染料去除和木质素降解方面的应用铺平了道路。该奖项反映了美国国家科学基金会的法定使命，并通过使用基金会的知识价值和更广泛的影响审查标准进行评估，被认为值得支持。

With this award, the Chemistry of Life Processes Program in the Chemistry Division is funding Dr. Ping Li from Kansas State University and Dr. Likai Song from Florida State University to investigate the molecular mechanism of A- and B-class dye-decolorizing peroxidases (DyPs) and their structure-property-reactivity-function (SPRF) relationship. The results of this investigation can be used in the development of biocatalysts for wastewater treatment and biofuel production. The proposed studies fill the critical knowledge gap regarding DyPs and guide protein engineering that could lead to enzymes with enhanced oxidative activity. This pursuit allows the graduate students and postdoctoral trainees to acquire expertise in multidisciplinary areas spanning from Chemistry to Biology, thus preparing them to become successful next-generation scientists. Contributions are also made to an outreach program that encourages students from groups underrepresented in STEM careers to major in science. This research project seeks to elucidate the molecular mechanism and SPRF relationship of DyPs, a new family of H2O2-dependent heme peroxidases. The studies focus on TcDyP from Thermomonospora curvata and ElDyP from Enterobacter lignolyticus as the representatives for the A- and B-class enzymes from this family, respectively. The residues situated on the enzyme surface that are responsible for substrate oxidation in TcDyP, the residue(s) that control one- and two-electron reduction reactions that involve ElDyP compound I, and the dynamics of the loop surrounding the heme pocket in DyPs are being studied using structural biology, enzymology, and electron paramagnetic resonance (EPR) investigation methods. Organic synthesis and protein engineering are being utilized to define and modulate the SPRF relationship. Information from this study not only fills the fundamental knowledge gap on DyPs but also paves the way for DyPs' applications in dye removal and lignin degradation.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.