Research project Geometric and electronic architecture of protein-coordinated radical and high-valent metal cofactors
Enzymes utilize metal and radical cofactors to perform particularly challenging chemistry in energy conversion, chemical synthesis and for harvesting sunlight. If we could mimic these processes it would eliminate the need for fossil fuels and transform chemical industry while reducing its environmental impact.
Achieving this type of chemistry is an outstanding testament to evolution and understanding it is a glaring challenge to mankind.
The key catalytic species are highly reactive organic radicals or high-valent metal clusters with a varying ligand environment, provided by the protein and other bound molecules, that directly controls the reactivity. To be able to understand and mimic the chemistry it is of central importance to obtain the geometric and electronic structures of the cofactor as well as the entire ligand environment for these usually short-lived and very reactive intermediates. This has, for a number of reasons, proven extremely challenging for protein-coordinated catalysts.
Recent advances in free-electron laser femtosecond crystallography and advanced spectroscopy have now brought these questions into reach experimentally. The central goal of this project is to utilize and develop methods to determine structures of protein radicals and high-valent metal sites, and define how the protein controls the entatic state as well as reactivity and mechanism for some of the most potent catalysts in nature.
Project members
Project managers
Martin Högbom
Professor of Biochemistry
