Chemistry Prof. Warren F. Beck recently awarded two large federal grants
- Sep 17, 2019
- Warren Beck
Prof. Warren Beck has recently been awarded two grants from national funding agencies:
A second renewal for a Department of Energy, Basic Energy Sciences, Photosynthetic Systems program grant, for Energy Transfer and Radiationless Decay in Light-harvesting Proteins. $579,921.
This project continues studies on the mechanisms that control capture of solar energy and excitation energy transfer processes in photosynthetic organisms. This renewal focuses on the photochemical mechanisms that enable photoactivation of the Orange Carotenoid Protein (OCP), which mediates photoprotective regulation of the excitation energy transfer rate in the cyanobacterial phycobilisome. Two-dimensional electronic spectroscopy (2DES) and fluorescence spectroscopy will be used to probe the light-driven mechanism that enables the active ketocarotenoid in OCP to sense the ambient light intensity and solar spectrum. 2DES will also be used to characterize coherent excitation transfer processes and to detect the site and mechanisms that permit OCP to quench excitations in the intact phycobilisome for the first time.
A new National Science Foundation grant, in the Chemistry of Life Processes program for Combining Theory and Experiment to Understand Carotenoid Photophysics in Photosynthetic Light-Harvesting. Jose Gascon, University of Connecticut, $327,496; Warren Beck, Michigan State University, $262,240.
This new project expands the work of the Beck laboratory on carotenoid photophysics to focus on the excited state potential energy surfaces that mediate excitation energy transfer and photoprotection mechanisms. Among the experimental goals to be carried out at MSU, we will be developing a novel polarized two-dimensional electronic spectroscopy method that will be able to sense the motions of excited-state vibrational wavepackets after a carotenoid is optically excited. Information from this experiment will inform the theoretical studies at UConn, which will employ QC/MM methods to characterize potential surfaces and protein-binding interactions.