Photosynthetic proteins convert light into chemical potential through coupled processes involving excitation, charge separation, electron transfer, proton movement, and changes in local hydration. These processes are not determined by cofactors alone; they are shaped by the surrounding protein matrix, which modulates electrostatics, solvent organization, and redox energetics.
In this talk, I will discuss how hybrid computational methods and continuum electrostatic calculations can be used to probe the molecular factors that regulate energy flow in photosynthetic complexes. Our work examines how local protein environments influence charge localization, redox tuning, hydration networks, and proton-coupled processes that support light-driven function.
By connecting structure, electrostatics, and energetics, this work aims to identify how photosynthetic proteins maintain functional efficiency across different molecular and energetic contexts. Understanding these principles is important not only for explaining how natural photosynthetic systems sustain efficient light-driven chemistry, but also for informing the design of bioinspired materials and molecular systems for energy conversion.