Structural Basis of Green Hydrogen Catalysis in Nature (GreenH2)

In Nature proteins called redox enzymes catalyse key processes with high efficiency like H2 production and inspire the design of synthetic catalysts.

However, to date synthetic catalysts are not as efficient as the natural systems.I plan to resolve the molecular structure and dynamics of the key reaction intermediates in [FeFe]-hydrogenases (H2 production) to reveal their catalytic mechanism on an atomic scale.I aim to(1) perform spectroscopy on [FeFe]-hydrogenase crystals to monitor their reaction intermediates(2) artificially activate catalysis inside [FeFe]-hydrogenase crystals(3) record functional and temporal structural information of the H2 catalysis via time-resolved crystallographyTime resolved crystallography is the ideal method to study the structure of reaction intermediates, however redox enzymes lack the trigger to activate the reaction in a controlled manner.

I have shown that enzymes can be artificially activated before.

Based on this extensive experience I am perfectly qualified to transfer my activation approaches to crystalline samples to enable their structural real time investigation by time-resolved crystallography.This project will enable us to follow bio-catalysis on a molecular level over time and thereby address fundamental questions in redox enzyme catalysis with the potential to unravel their catalytic mechanism, knowledge crucial to develop synthetic catalysts addressing climate change and beyond.