Ulas paper published in Nature Chemistry

molecular illustration

View of the metalloprotein (rainbow) - semiquinone (magenta) binding site

DGL postdoc, Gözde Ulas, published a paper in Nature Chemistry this week investigating how a designed metalloprotein stabilizes an organic radical.  The system is set to interrogate the key biological process of utilizing high-energy radicals.  The paper was also featured in C&EN this week!

Ulas and coworkers used a designed metalloprotein to specifically stabilize a semiquinone anion radical, making the protein-radical complex amenable for optical and magnetic spectroscopy studies. They then demonstrated that the protein-bound semiquinone radical experiences a drastically changed potential energy landscape compared to its free-in-solution counterpart, and that the radical is stabilized by 9 kcal/mol.