Collaborative Research: De Novo Protein Constructs for Photosynthetic Energy Transduction

University Of California-San Francisco, San Francisco CA

Investigators

Abstract

With the support of the Chemistry of Life Processes (CLP) Program in the Division of Chemistry, Professors Michael Therien and David Beratan of Duke University and William DeGrado of University of California-San Francisco are studying new approaches to design materials that direct, store, and release energy. Biology has developed numerous designs that carry out these functions; chemists, however, have yet to create energy harvesting, storage, and release systems from scratch that possess the sophistication of those seen in nature. Recent advances in protein design enable chemists to construct large molecules that capture and manage the flow of positive charges, negative charges, and energy. By designing protein-based materials that migrate and collect charges and energy, unique optical, electrical, and chemical functions will be realized. The experimental procedures used in this effort will (i) provide new tools to build proteins having innovative designed functions, and (ii) characterize the structures and energy storage and release functions of these proteins. This pursuit will allow graduate students and postdoctoral fellows to acquire specialized training in synthetic chemistry, protein design, protein biochemistry, modern computational methods, and techniques to monitor fast processes that move charge and energy. The protein design methods developed will be broadly applicable, and enable construction of new biologically inspired materials that carry out novel functions not seen in nature. Outreach activities of this project will introduce college and pre-college students to important new technologies, and teach skills important for future careers in science and engineering. Biological energy transduction relies on protein-cofactor assemblies that possess physico-chemical functionality that far exceeds that realized to date through molecular and macromolecular design and synthesis. This research project will be undertaken to realize such complex functionality through “design from scratch” strategies that exploit de novo proteins that bind abiological cofactors, and in the process, elucidate fundamental design principles required for photosynthetic energy transduction, storage, and release. This project takes advantage of an integrated, multi-disciplinary approach to evolve peptide-cofactor complexes that possess sophisticated electro-optic functionality, encompassing cofactor design and synthesis, advanced computational methods that provide proteins that bind these cofactors in precise, organized spatial arrangements, protein expression and characterization, state-of-the-art pump-probe transient optical methods that characterize function and reaction dynamics, and high resolution protein structure determination. Information from this study is expected to elucidate fundamental principles required for photosynthetic energy transduction, and designed proteins that possess novel electro-optical function and transduce energy via innovative pathways. 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.