Optimized Expression and Purification for High-Activity Preparations of Algal [FeFe]-Hydrogenase

摘要

BackgroundRecombinant expression and purification of metallo-enzymes, including hydrogenases, at high-yields is challenging due to complex, and enzyme specific, post-translational maturation processes. Low fidelities of maturation result in preparations containing a significant fraction of inactive, apo-protein that are not suitable for biophysical or crystallographic studies.