We begin with a fundamental question: how does a protein environment make difficult chemistry possible? Our research follows that question from natural far-red photosynthesis to engineered catalysts and photosynthetic biomaterials.
Research at a glance
Our work connects fundamental molecular events to the design of new light-powered systems.
Some cyanobacteria use wavelengths beyond those available to most oxygenic photosynthetic organisms. We study the molecular adaptations that allow these systems to capture lower-energy photons and sustain electron transfer.
How does the protein environment tune energy conversion when every photon carries less energy?
We investigate how the protein environment tunes the paired chlorophylls that initiate charge separation in Photosystem I. Site-resolved electrostatics helps us identify which residues, waters and hydrogen-bonding interactions shift donor energetics under visible and far-red illumination.
The Fₓ, Fₐ and Fᵦ clusters form the acceptor-side pathway of Photosystem I. We ask how local electrostatics tune their redox energetics while the overall electron-transfer sequence remains functional across photosynthetic organisms.
Proteins are dynamic electrostatic environments rather than fixed structures. We map protonation states, side-chain conformations, internal waters and correlated microstates to understand how many small interactions collectively shape function.
By comparing visible-light and far-red-light systems, we separate broadly conserved features from species-specific adaptations. These comparisons reveal transferable molecular principles rather than isolated structural differences.
Nature separates charge and moves electrons with molecular precision. We are exploring how those principles can guide hybrid systems that connect photosynthetic proteins with synthetic catalysts.
How can biological light capture be coupled to artificial catalysts without losing directional electron flow?
We are exploring how biological reaction centres can be coupled to synthetic catalysts and nanoparticles. Computation can identify interfacial arrangements that support electron delivery while limiting unproductive charge recombination.
Efficient hybrid catalysis requires the energetic levels of the protein cofactors and synthetic catalyst to work together. We model this alignment to identify where electron transfer is favourable and where molecular redesign may help.
Natural photosynthesis offers strategies for light capture, charge separation and directional electron transfer. We translate these strategies into testable principles for artificial energy-conversion systems, including hydrogen-producing assemblies.
This emerging program connects our expertise in computational photosynthesis with questions in soft and functional materials.
How can molecular insight guide the next generation of photosynthetic materials?
We are exploring how computational biophysics can inform the design of photosynthetic biomaterials. For more information or interest in working on this project, contact dmatta@brocku.ca.
How we investigate
No single method can connect protein motion, electrostatics and electronic structure. We combine complementary approaches and test their predictions against structural and spectroscopic observations from collaborators.